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Journal of Medicine and Pharmacy","Tạp chí Y Dược học Cần Thơ",{"EN":487,"VI":488},"\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">04\u002F10\u002F2015 Ministry of Information and Communications allowed Can Tho journal of medicine and pharmacy to operate (102 \u002FGP-BTTTT)\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">07\u002F16\u002F2015 Can Tho journal of medicine and pharmacy is internationally recognized: ISSN 2354-1210\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">In 2016, The journal has been included in the list of medical science journals by The State Council for professorship which is awarded a work score of 0-0.5 points for a published article.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Can Tho Journal of Medicine and Pharmacy welcome original works that haven’t been submitted or published in other medical journals. Posts must contain content related to one of the journal’s categories.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The content published\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The journal is divided into 3 categories:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Scientific research article: are valuable scientific works, which have been researched and accepted.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Overview of medicine, biology and pharmacy: serving the objective of continuing training in the fields of medicine, biology and pharmacy; to systematize classical and modern knowledge.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Update information on new knowledge about medicine, biology, pharmacy in the country and in the world.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Scope\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Publication and introduction of scientific research in the fields:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Medicine (internal medicine, surgery, pediatrics, obstetrics and gynecology, odonto-stomatology, laboratory, oncology, traditional medicine, nursing).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Biology (genetics, biotechnology).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">+ Pharmacology (pharmaceutics, drug quality analysis-control, synthetic pharmaceutical chemistry, biochemistry, pharmacognosy, botany, clinical pharmacy).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- To enhance the quality of undergraduate, postgraduate education, scientifically researching and meet the necessary treatment in hospital.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Introducing the updated domestic and oversea information about science technology to promote scientific research and exchanging technology in local, other universities.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">- Exchanging pharmaceutical and medical information for social health developing in the Mekong Delta and Vietnam.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">The object\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Postgraduate students, student of Can Tho University of Medicine and Pharmacy, scientists from schools, research institutes, hospitals, health centers, pharmaceutical companies of the Mekong Delta; other provinces and regions in Vietnam and other country.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Address\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Headquarters of Can Tho Journal of Medicine and Pharmacy, located Scientific Research and International Cooperation Office: 179 Nguyen Van Cu Street, An Khanh Ward, Ninh Kieu District, Can Tho City, Vietnam.\u003C\u002Fspan>\u003C\u002Fp>","\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Ngày 16\u002F7\u002F2015, Tạp chí Y Dược học Cần Thơ được cấp chỉ số quốc tế: ISSN 2354-1210.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 4\u002F2016, Tạp chí đã được Hội đồng Giáo sư ngành Y đưa vào danh sách các tạp chí khoa học Y học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Năm 2020 Tạp chí Y Dược học Cần Thơ đã được phê duyệt vào danh mục của các Hội đồng Giáo sư ngành Dược học được tính điểm công trình 0-0,5 điểm cho một bài báo đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ ra 12 số\u002Fnăm, 180-200 trang\u002Fsố.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Từ tháng 12\u002F2022 Tạp chí Y Dược học Cần Thơ là thành viên của hệ thống Crossref và từ tháng 01\u002F2023 tạp chí thực hiện bình duyệt online kín 2 chiều nhằm tăng tính minh bạch, tin cậy của các công trình nghiên cứu khoa học và đảm bảo tốt nhất chất lượng khoa học của bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ, mục đích và phạm vi của tạp chí\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tôn chỉ và mục đích hoạt động của tạp chí: xuất bản nhằm mục đích phổ biến kết quả từ các đề tài nghiên cứu khoa học; giao lưu trao đổi khoa học, chia sẻ kinh nghiệm, học tập, đồng thời cập nhật thông tin khoa học mới trong các lĩnh vực y, sinh, dược học trong và ngoài nước.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phạm vi của tạp chí: Tạp chí xuất bản được chia thành 3 chuyên mục: (i) Bài báo nghiên cứu khoa học là kết quả công trình nghiên cứu khoa học có giá trị đã được triển khai nghiên cứu, (ii) Bài tổng quan y, sinh, dược học: phục vụ mục tiêu đào tạo liên tục trong lĩnh vực y, sinh, dược học; nhằm hệ thống hóa những kiến thức kinh điển và hiện đại; (iii) Thông tin cập nhật kiến thức mới về y, sinh, dược học trong nước và trên thế giới.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Chính sách truy cập mở\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ áp dụng chính sách truy cập mở đối với các bài báo đã xuất bản đến với độc giả, nhằm mở rộng cơ hội tiếp cận các kết quả nghiên cứu chất lượng cao và tăng cường trao đổi kiến thức. Tạp chí đăng tải trực tuyến (miễn phí) toàn văn các bài báo được công bố trên website của Tạp chí (https:\u002F\u002Ftapchi.ctump.edu.vn).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đạo đức xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ cam kết tuân thủ đạo đức xuất bản phù hợp với các hướng dẫn và tiêu chuẩn của the Committee on Publication Ethics (COPE), tuân thủ các nguyên tắc của COPE’s Core Practices, Best Practices Guidelines for Journal Editors và Guidelines on Good Publication Practices.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Bản thảo bài báo chỉ được chấp nhận khi được tác giả chịu trách nhiệm chính cam kết các nội dung sau: Các nội dung của bản thảo chưa được đăng tải toàn bộ hoặc một phần ở các tạp chí khác; Tất cả các tác giả đều có đóng góp một cách đáng kể vào quá trình nghiên cứu hoặc chuẩn bị bản thảo và cùng chịu trách nhiệm về các nội dung của bản thảo; Tuân thủ các biện pháp đảm bảo đạo đức nghiên cứu (ví dụ thỏa thuận đồng ý tham gia nghiên cứu).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Cam kết bảo mật\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí cam kết thực hiện và tuân thủ các quy định của luật và các văn bản hướng dẫn liên quan đến bảo mật thông tin cá nhân trên không gian mạng. Các thông tin mà người dùng (tác giả, độc giả, biên tập viên, người phản biện) nhập vào các biểu mẫu trên Hệ thống Quản lý xuất bản trực tuyến của tạp chí chỉ được sử dụng vào các mục đích đã được tuyên bố rõ ràng và sẽ không được cung cấp cho bất kỳ bên thứ ba nào khác, hay dùng vào bất kỳ mục đích nào khác.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Phí gửi bài\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng bài: 1.000.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Lệ phí gửi đăng nhanh: 1.500.000đ\u002Fbài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với tác giả là cán bộ viên chức thuộc Trường Đại học Y Dược Cần Thơ thì được hỗ trợ 50% lệ phí gửi đăng bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Đối với sinh viên thực hiện đề tài nghiên cứu khoa học cấp trường được hỗ trợ 100% lệ phí đăng bài ( Tác giả gửi đính kèm “ Quyết định về việc giao tổ chức thực hiện đề tài nghiên cứu khoa học cấp Trường của sinh viên”).\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Hình thức nộp lệ phí:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Tiền mặt:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Nộp trực tiếp tại Phòng Tài chính - Kế toán, Trường Đại học Y Dược Cần Thơ, số 179 Nguyễn Văn Cừ, P. An Khánh, Q. Ninh Kiều, thành phố Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Chuyển khoản:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tên Tài khoản: Trường ĐHYD Cần Thơ, Số TK: 0111000115668, tại ngân hàng Vietcombank chi nhánh Cần Thơ.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Thời gian: Áp dụng từ ngày 01\u002F02\u002F2023.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">* Phí gửi bài không được hoàn trả khi bài viết bị từ chối hoặc tác giả xin rút bài viết.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Quy trình phản biện bài báo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tạp chí Y Dược học Cần Thơ thực hiện quy trình phản biện kín hai chiều nghiêm ngặt. Danh tính của những người phản biện không được tiết lộ cho các tác giả và ngược lại. Quy trình thẩm định bài báo đăng gồm các bước sau:\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tiếp nhận bản thảo\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Tác giả liên hệ gửi bản thảo đến Tạp chí qua hệ thống trực tuyến tại website: https:\u002F\u002Ftapchi.ctump.edu.vn. Hướng dẫn về cách đăng ký, gửi bài và chuẩn bị bản thảo được cung cấp trên website của Tạp chí.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sàng lọc sơ bộ\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Sau khi Tòa soạn nhận được bài báo của tác giả, Ban Thư ký sẽ tiến hành kiểm tra sơ bộ bài báo (các yêu cầu về nội dung và hình thức). Những bài báo không đúng quy cách hoặc có nội dung không phù hợp hoặc vi phạm bản quyền sẽ bị từ chối (Ban Thư ký thông báo phản hồi đến tác giả trong vòng 1 tuần). Những bài báo đủ điều kiện, được Ban Thư ký tòa soạn chuyển đến Ban Biên tập có cùng chuyên môn với nội dung bài báo để đề xuất người phản biện. Thời gian kể từ khi Ban Biên tập nhận bài báo đến khi đề xuất người phản biện bài báo chậm nhất là 5 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Vòng phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký gửi bài và yêu cầu phản biện đến 02 phản biện độc lập.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Các phản biện gởi nhận xét cho Ban Thư ký. Thời gian từ khi gửi bài cho phản biện đến khi nhận ý kiến của phản biện tối đa là 20 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xử ký kết quả phản biện\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Nếu ý kiến đồng ý cho đăng và không cần chỉnh sửa, Ban Thư ký tiếp tục đăng bài theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Nếu ý kiến đồng ý đăng và cần chỉnh sửa, Ban Thư ký sẽ thông tin đến tác giả chỉnh sửa theo yêu cầu của người phản biện. Thời gian chỉnh sửa và gửi lại kéo dài không quá 2 tuần, từ khi tác giả bài báo nhận được thông tin (Quá trình này có thể lặp lại tối đa 2 lần\u002F1 bài báo). Khi có sự thống nhất, đồng ý của người phản biện; bài báo được tiếp tục đăng theo qui trình.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Những bài báo có chất lượng không đạt yêu cầu, cả 2 phản biện không đồng ý cho đăng sẽ bị Tòa soạn từ chối đăng.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">Xuất bản\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">1. Ban Thư ký tổng hợp các bản thảo đã được tác giả hoàn thiện sau thẩm định trình Ban Biên tập xem xét, Tổng Biên tập phê duyệt, quyết định bài đăng theo các tiêu chí: sự phù hợp nội dung với tôn chỉ và mục đích, thể loại bài viết (ưu tiên các bài có bài có nghiên cứu chuyên sâu, hàm lượng khoa học cao), đóng góp mới bài báo, bài báo được ưu tiên đăng trong số gần nhất của Tạp chí theo thứ tự: tính thời sự, chất lượng bài báo và thời gian gửi bài.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">2. Ban Biên tập và Ban Thư ký biên tập bản thảo, chế bản, đọc rà soát lỗi. Thời gian hoàn thành từ 10-15 ngày.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">3. Ban Thư ký có trách nhiệm thông báo cho tác giả bài báo (bằng e-mail) về tình hình phê duyệt bài báo, thời gian, số kỳ, tập xuất bản bài báo theo qui định.\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>\u003Cp>\u003Cspan style=\"color: rgb(0, 0, 0);\">4. Danh sách bài báo theo số Tạp chí được in ấn và phát hành trong năm định kỳ được công bố chính thức trên website: https:\u002F\u002Ftapchi.ctump.edu.vn\u003C\u002Fspan>\u003C\u002Fp>\u003Cp>\u003Cbr>\u003C\u002Fp>",{"VOID":490},"wcQ1uqwAAAAJ","2023-05-30T08:17:21.868+00:00",[],[494],{"id":495,"createTime":28,"updateTime":28,"relativeEntities":496,"slug":28,"properties":497,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":507,"parentIds":508,"statistic":28},"6413896b-eca9-442b-a73f-182a58a0ce40",[],{"title":498,"address":501,"country":504,"abbreviation":505},{"EN":499,"VI":500},"Can Tho University of Medicine and Pharmacy","Trường Đại học Y Dược Cần Thơ",{"EN":502,"VI":503},"No 179, Nguyen Van Cu street, An Khanh ward, Ninh Kieu district, Can Tho city, Vietnam","Số 179, đường Nguyễn Văn Cừ, phường An Khánh, quận Ninh Kiều, thành phố Cần Thơ, Việt Nam",{"VOID":15},{"VOID":506},"ctump","http:\u002F\u002Fwww.ctump.edu.vn\u002F",[],[],"https:\u002F\u002Ftapchi.ctump.edu.vn\u002Findex.php\u002Fctump",{"impactFactor":32,"impactFactorByYear":512,"i10Index":32,"i10IndexLast5Year":32,"totalPublication":514,"totalPublicationByYear":515,"totalCitation":520,"totalCitationByYear":521,"totalCitationPerPublication":108,"totalCitationPerPublicationByYear":523,"hindexLast5Year":45,"hindex":45},{"2022":513,"2023":111,"2024":106},0.01,1556,{"2020":47,"2021":516,"2022":517,"2023":518,"2024":519,"2025":122},57,306,801,358,161,{"2021":146,"2022":280,"2023":522},99,{"2021":524,"2022":318,"2023":104},0.23,{"impactFactor":28,"impactFactorByYear":28,"i10Index":123,"i10IndexLast5Year":123,"totalPublication":526,"totalPublicationByYear":527,"totalCitation":526,"totalCitationByYear":528,"totalCitationPerPublication":40,"totalCitationPerPublicationByYear":531,"hindexLast5Year":49,"hindex":49},476,{"0":205,"2019":123,"2021":139,"2022":459,"2023":451,"2024":357,"2025":49,"2026":48},{"2021":42,"2022":123,"2023":161,"2024":529,"2025":360,"2026":530},136,83,{"2021":105,"2022":513,"2023":532,"2024":127,"2025":533,"2026":534},0.62,25.43,13.83,{"id":536,"createTime":537,"updateTime":382,"relativeEntities":538,"slug":539,"properties":540,"entityType":25,"verifyStatus":26,"verifyTime":28,"verifyNote":28,"languages":552,"translateLanguages":28,"viewCount":133,"subjectFields":553,"manageAffiliations":554,"indexDatabases":555,"url":556,"thumbnailPath":557,"statistic":558,"gsStatistic":594,"type":55,"analyzePriority":28},"6984a56a-db70-403b-9cc4-4013e1ceaffa","2023-05-09T06:47:40.346+00:00",[],"T%E1%BA%A1p%20ch%C3%AD%20Nghi%C3%AAn%20c%E1%BB%A9u%20n%C6%B0%E1%BB%9Bc%20ngo%C3%A0i",{"country":541,"issn":542,"title":544,"introduce":547,"gsId":550},{"VOID":15},{"VOID":543},"25252445",{"EN":545,"VI":546},"VNU Journal of Foreign Studies","Tạp chí Nghiên cứu nước ngoài",{"EN":548,"VI":549},"{\"ops\":[{\"insert\":\"\\n\\nThe \\n\"},{\"attributes\":{\"italic\":true},\"insert\":\"VNU Journal of Science\"},{\"insert\":\"\\n was established in 1985 for the publication of national and international research papers in all fields of natural sciences and technology, social sciences and humanities. 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The studies reported here suggest that the Edelhoch method is the best method for measuring ε for a protein. (This method is described by Gill and von Hippel [1989, \u003Cjats:italic>Anal Biochem 182\u003C\u002Fjats:italic>:319–326] and is based on data from Edelhoch [1967, \u003Cjats:italic>Biochemistry 6\u003C\u002Fjats:italic>:1948–1954].) The absorbance of a protein at 280 nm depends on the content of Trp, Tyr, and cystine (disulfide bonds). The average ε values for these chromophores in a sample of 18 well‐characterized proteins have been estimated, and the ε values in water, propanol, 6 M guanidine hydrochloride (GdnHCl), and 8 M urea have been measured. For Trp, the average ε values for the proteins are less than the ε values measured in any of the solvents. For Tyr, the average ε values for the proteins are intermediate between those measured in 6 M GdnHCl and those measured in propanol. Based on a sample of 116 measured ε values for 80 proteins, the ε at 280 nm of a folded protein in water, ε(280), can best be predicted with this equation\u003C\u002Fjats:p>\u003Cjats:p>ϵ(280) (M\u003Cjats:sup>−1\u003C\u002Fjats:sup> cm\u003Cjats:sup>−1\u003C\u002Fjats:sup>) = (#Trp)(5,500) + (#Tyr)(1,490) + (#cystine)(125).\u003C\u002Fjats:p>\u003Cjats:p>These ε(280) values are quite reliable for proteins containing Trp residues, and less reliable for proteins that do not. However, the Edelhoch method is convenient and accurate, and the best approach is to measure rather than predict ε.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>Hệ số hấp thụ mol, ε, của một protein thường được dựa trên nồng độ được đo bằng khối lượng khô, phân tích nitơ hoặc amino acid. Các nghiên cứu được báo cáo ở đây cho thấy phương pháp Edelhoch là phương pháp tốt nhất để đo ε cho một protein. (Phương pháp này được mô tả bởi Gill và von Hippel [1989, \u003Cjats:italic>Anal Biochem 182\u003C\u002Fjats:italic>:319–326] và dựa trên dữ liệu từ Edelhoch [1967, \u003Cjats:italic>Biochemistry 6\u003C\u002Fjats:italic>:1948–1954].) Độ hấp thụ của một protein tại 280 nm phụ thuộc vào nội dung của Trp, Tyr và cystine (liên kết disulfide). Các giá trị ε trung bình cho các chromophore này trong một mẫu 18 protein được đặc trưng tốt đã được ước tính, và các giá trị ε trong nước, propanol, 6 M guanidine hydrochloride (GdnHCl) và 8 M ure đã được đo. Đối với Trp, các giá trị ε trung bình cho các protein thấp hơn các giá trị ε được đo trong bất kỳ dung môi nào. Đối với Tyr, các giá trị ε trung bình cho các protein nằm giữa các giá trị đo trong 6 M GdnHCl và các giá trị đo trong propanol. Dựa trên một mẫu 116 giá trị ε đã đo cho 80 protein, ε tại 280 nm của một protein gập trong nước, ε(280), có thể được dự đoán tốt nhất bằng phương trình này\u003C\u002Fjats:p>\u003Cjats:p>ϵ(280) (M\u003Cjats:sup>−1\u003C\u002Fjats:sup> cm\u003Cjats:sup>−1\u003C\u002Fjats:sup>) = (#Trp)(5,500) + (#Tyr)(1,490) + (#cystine)(125).\u003C\u002Fjats:p>\u003Cjats:p>Các giá trị ε(280) này khá đáng tin cậy cho những protein chứa các dư lượng Trp, và ít đáng tin cậy hơn cho các protein không chứa. Tuy nhiên, phương pháp Edelhoch là thuận tiện và chính xác, và cách tiếp cận tốt nhất là đo thay vì dự đoán ε.\u003C\u002Fjats:p>",{"EN":1024,"VI":1025},"How to measure and predict the molar absorption coefficient of a protein","Cách đo và dự đoán hệ số hấp thụ mol của một protein",{"VOID":1027},"8563639",{"VOID":1029},"10.1002\u002Fpro.5560041120","PUBLICATION","2024-09-05T11:12:42.172+00:00","Auto Verify",[31],[30],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fpro.5560041120",[1037,1072,1089,1104,1119],{"id":1038,"sortIndex":32,"researcher":28,"roles":1039,"affiliations":1040,"properties":1065,"displayName":1069,"givenName":28,"familyName":28},"3f294b4e-635b-4194-9d76-33957abeed06",[],[1041,1049,1057],{"id":1042,"sortIndex":32,"affiliation":1043,"properties":28},"ae18dbcf-d1a0-454c-a699-df3572917a3a",{"id":1042,"createTime":28,"updateTime":28,"relativeEntities":1044,"slug":28,"properties":1045,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1048,"statistic":28},[],{"title":1046},{"EN":1047},"Center for Macromolecular Design, Texas A&M University, College Station, Texas 77843-1114",[],{"id":1050,"sortIndex":40,"affiliation":1051,"properties":28},"27aa073a-e2d5-43e8-ac9f-09f9ce82d348",{"id":1050,"createTime":28,"updateTime":28,"relativeEntities":1052,"slug":28,"properties":1053,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1056,"statistic":28},[],{"title":1054},{"VI":1055},"Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-1114",[],{"id":1058,"sortIndex":123,"affiliation":1059,"properties":28},"619b9962-dde2-4356-83a8-bf0531600a8a",{"id":1058,"createTime":28,"updateTime":28,"relativeEntities":1060,"slug":28,"properties":1061,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1064,"statistic":28},[],{"title":1062},{"VI":1063},"Department of Medical Biochemistry and Genetics, Texas A & M University, College Station, Texas 77843-1114",[],{"orcid":1066,"title":1068,"openalex":1070},{"VOID":1067},"https:\u002F\u002Forcid.org\u002F0000-0002-9998-7129",{"EN":1069},"C. 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Different types of atoms are distributed nonrandomly with respect to each other in proteins. Errors in model building lead to more randomized distributions of the different atom types, which can be distinguished from correct distributions by statistical methods.\u003C\u002Fjats:p>\u003Cjats:p>Atoms are classified in one of three categories: carbon (C), nitrogen (N), and oxygen (O). This leads to six different combinations of pairwise noncovalently bonded interactions (CC, CN, CO, NN, NO, and OO). A quadratic error function is used to characterize the set of pairwise interactions from nine‐residue sliding windows in a database of 96 reliable protein structures. Regions of candidate protein structures that are mistraced or misregistered can then be identified by analysis of the pattern of nonbonded interactions from each window.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>Trong bài báo này, một phương pháp mới được mô tả nhằm phân biệt giữa các vùng cấu trúc protein được xác định đúng và sai dựa trên các tương tác nguyên tử đặc trưng. Các loại nguyên tử khác nhau được phân bố không ngẫu nhiên với nhau trong các phân tử protein. Những sai sót trong việc xây dựng mô hình dẫn đến việc phân bố các loại nguyên tử khác nhau trở nên ngẫu nhiên hơn, điều này có thể được phân biệt so với các phân bố đúng bằng các phương pháp thống kê.\u003C\u002Fjats:p>\u003Cjats:p>Các nguyên tử được phân loại vào một trong ba loại: carbon (C), nitơ (N), và oxy (O). Điều này dẫn đến sáu tổ hợp khác nhau của các tương tác không liên kết cặp (CC, CN, CO, NN, NO, và OO). Một hàm lỗi bậc hai được sử dụng để đặc trưng hóa bộ các tương tác cặp từ các cửa sổ trượt chín dư trong cơ sở dữ liệu của 96 cấu trúc protein đáng tin cậy. Các vùng của cấu trúc protein ứng viên mà bị theo dõi sai hoặc đăng ký sai sau đó có thể được xác định thông qua phân tích mô hình của các tương tác không liên kết từ mỗi cửa sổ.\u003C\u002Fjats:p>",{"EN":1415,"VI":1416},"Verification of protein structures: Patterns of nonbonded atomic interactions","Xác thực cấu trúc protein: Mô hình tương tác nguyên tử không liên kết",{"VOID":1418},"8401235",{"VOID":1420},"10.1002\u002Fpro.5560020916",[31],[30],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fpro.5560020916",[1425,1444],{"id":1426,"sortIndex":32,"researcher":28,"roles":1427,"affiliations":1428,"properties":1437,"displayName":1441,"givenName":28,"familyName":28},"8e1e4542-b693-4294-a774-f0da3879bc6e",[],[1429],{"id":1430,"sortIndex":32,"affiliation":1431,"properties":28},"4bc438b2-dee2-42b7-87b8-58653762f018",{"id":1430,"createTime":28,"updateTime":28,"relativeEntities":1432,"slug":28,"properties":1433,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1436,"statistic":28},[],{"title":1434},{"VI":1435},"Department of Chemistry and Biochemistry, University of California, Los Angeles 90024-1569.",[],{"orcid":1438,"title":1440,"openalex":1442},{"VOID":1439},"https:\u002F\u002Forcid.org\u002F0000-0003-1054-5656",{"EN":1441},"Christos Colovos",{"VOID":1443},"A5050678734",{"id":1445,"sortIndex":40,"researcher":28,"roles":1446,"affiliations":1447,"properties":1456,"displayName":1460,"givenName":28,"familyName":28},"d40b5544-d335-4a9f-b59f-dbe5a100fca6",[],[1448],{"id":1449,"sortIndex":32,"affiliation":1450,"properties":28},"90cd4677-c002-44d0-a381-7e5ff857f546",{"id":1449,"createTime":28,"updateTime":28,"relativeEntities":1451,"slug":28,"properties":1452,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":1455,"statistic":28},[],{"title":1453},{"EN":1454},"Department of Chemistry & Biochemistry, University of California, 405 Hilgard Avenue, Los Angeles, California 90024–1569",[],{"orcid":1457,"title":1459,"openalex":1461},{"VOID":1458},"https:\u002F\u002Forcid.org\u002F0000-0001-5709-9839",{"EN":1460},"T.O. 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Biol. Chem., 267, 16980, 10.1016\u002FS0021-9258(18)41881-9",{"doi":1556},"10.1016\u002FS0021-9258(18)41881-9",{"id":28,"text":1558,"url":28,"identifiers":1559},"10.1126\u002Fscience.2448879",{"doi":1558},{"id":28,"text":1561,"url":28,"identifiers":1562},"10.1038\u002F319199a0",{"doi":1561},{"id":28,"text":1564,"url":28,"identifiers":1565},"Fitzgerald P.M.D., 1990, Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl‐pepstain at 2.0 Å resolution, J. Biol. Chem., 265, 14209, 10.1016\u002FS0021-9258(18)77288-8",{"doi":1566},"10.1016\u002FS0021-9258(18)77288-8",{"id":28,"text":1568,"url":28,"identifiers":1569},"10.1016\u002F0022-2836(82)90451-X",{"doi":1568},{"id":28,"text":1571,"url":28,"identifiers":1572},"10.1016\u002FS0022-2836(05)80068-3",{"doi":1571},{"id":28,"text":1574,"url":28,"identifiers":1575},"10.1107\u002FS0108767390010224",{"doi":1574},{"id":28,"text":1577,"url":28,"identifiers":1578},"10.1126\u002Fscience.2399465",{"doi":1577},{"id":28,"text":1580,"url":28,"identifiers":1581},"10.1038\u002F356083a0",{"doi":1580},{"id":28,"text":1583,"url":28,"identifiers":1584},"10.1126\u002Fscience.3024321",{"doi":1583},{"id":28,"text":1586,"url":28,"identifiers":1587},"10.1038\u002F337615a0",{"doi":1586},{"id":28,"text":1589,"url":28,"identifiers":1590},"10.1016\u002F0022-2836(84)90049-4",{"doi":1589},{"id":28,"text":1592,"url":28,"identifiers":1593},"10.1002\u002Fprot.340040105",{"doi":1592},{"id":28,"text":1595,"url":28,"identifiers":1596},"10.1073\u002Fpnas.84.16.5690",{"doi":1595},{"id":28,"text":1598,"url":28,"identifiers":1599},"10.1016\u002FS0065-3233(08)60402-7",{"doi":1598},{"id":28,"text":1601,"url":28,"identifiers":1602},"Schreuder H.A., 1990, The RuBisCO saga—Accuracy and reliability of macromolecular crystal structures, Proc. CCP4 Study Weekend, 26–27 January, 1990, 73",{},{"id":28,"text":1604,"url":28,"identifiers":1605},"10.1016\u002F0022-2836(92)91058-W",{"doi":1604},{"id":28,"text":1607,"url":28,"identifiers":1608},"10.1021\u002Fma60054a013",{"doi":1607},{"id":28,"text":1610,"url":28,"identifiers":1611},"Wilmanns M(1990). Ph.D. Thesis University of Basel Basel Switzerland.",{},{"id":28,"text":1613,"url":28,"identifiers":1614},"10.1016\u002F0022-2836(92)90665-7",{"doi":1613},{"id":28,"text":1616,"url":28,"identifiers":1617},"10.1126\u002Fscience.2548279",{"doi":1616},{"id":1619,"createTime":1620,"updateTime":1621,"relativeEntities":1622,"slug":1623,"properties":1624,"entityType":1030,"verifyStatus":26,"verifyTime":1620,"verifyNote":1032,"languages":1642,"translateLanguages":1643,"viewCount":32,"primaryUrl":1644,"fullTextUrl":28,"authors":1645,"publicationType":1136,"publisherRelationship":1682,"citationCount":1740,"citationInfo":1741,"publishDate":1748,"publishYear":1742,"citationAnalyzeStatus":884,"lastCitationAnalyze":28,"indexDatabases":1749,"openAccess":28,"references":1750,"isForceReanalyzing":1396},"eb2bb488-d1b5-4508-946c-777502c29e2e","2025-01-26T20:38:09.419+00:00","2025-02-06T01:52:55.314+00:00",[],"Statistical-potential-for-assessment-and-prediction-of-protein-structures",{"mag":1625,"keywords":1627,"pmc":1628,"openalex":1630,"abstract":1632,"title":1635,"pm":1638,"doi":1640},{"VOID":1626},"1999613945",{"VI":1015},{"VOID":1629},"2242414",{"VOID":1631},"W1999613945",{"EN":1633,"VI":1634},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:p>Protein structures in the Protein Data Bank provide a wealth of data about the interactions that determine the native states of proteins. Using the probability theory, we derive an atomic distance‐dependent statistical potential from a sample of native structures that does not depend on any adjustable parameters (Discrete Optimized Protein Energy, or DOPE). DOPE is based on an improved reference state that corresponds to noninteracting atoms in a homogeneous sphere with the radius dependent on a sample native structure; it thus accounts for the finite and spherical shape of the native structures. The DOPE potential was extracted from a nonredundant set of 1472 crystallographic structures. We tested DOPE and five other scoring functions by the detection of the native state among six multiple target decoy sets, the correlation between the score and model error, and the identification of the most accurate non‐native structure in the decoy set. For all decoy sets, DOPE is the best performing function in terms of all criteria, except for a tie in one criterion for one decoy set. To facilitate its use in various applications, such as model assessment, loop modeling, and fitting into cryo‐electron microscopy mass density maps combined with comparative protein structure modeling, DOPE was incorporated into the modeling package MODELLER‐8.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>Cấu trúc protein trong Ngân hàng Dữ liệu Protein cung cấp nhiều dữ liệu về các tương tác xác định trạng thái nguyên bản của protein. Sử dụng lý thuyết xác suất, chúng tôi xây dựng một tiềm năng thống kê phụ thuộc vào khoảng cách nguyên tử dựa trên một mẫu cấu trúc nguyên bản mà không phụ thuộc vào bất kỳ thông số điều chỉnh nào (Tiềm năng Năng lượng Protein Tối ưu rời rạc, hay DOPE). DOPE được dựa trên một trạng thái tham chiếu cải tiến tương ứng với các nguyên tử không tương tác trong một hình cầu đồng nhất với bán kính phụ thuộc vào cấu trúc nguyên bản mẫu; do đó, nó tính đến hình dạng hữu hạn và hình cầu của các cấu trúc nguyên bản. Tiềm năng DOPE đã được rút trích từ một tập hợp cấu trúc tinh thể không dư thừa gồm 1472 cấu trúc. Chúng tôi đã kiểm tra DOPE và năm hàm điểm số khác bằng cách phát hiện trạng thái nguyên bản trong sáu bộ giả mẫu đa đích, mối tương quan giữa điểm số và lỗi mô hình, và xác định cấu trúc không nguyên bản chính xác nhất trong bộ giả mẫu. Đối với tất cả các bộ giả mẫu, DOPE là hàm hoạt động tốt nhất theo tất cả các tiêu chí, ngoại trừ một tiêu chí có sự hòa nhau cho một bộ giả mẫu. Để tạo điều kiện cho việc sử dụng nó trong các ứng dụng khác nhau, như đánh giá mô hình, mô hình vòng, và phù hợp vào bản đồ mật độ khối lượng cryo-điện tử kết hợp với mô hình hóa cấu trúc protein so sánh, DOPE đã được tích hợp vào gói mô hình MODELLER-8.\u003C\u002Fjats:p>",{"EN":1636,"VI":1637},"Statistical potential for assessment and prediction of protein structures","Tiềm năng thống kê để đánh giá và dự đoán cấu trúc 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This change is dependent on the aggregated state as monomeric or dimeric peptides do not react, and guanidine dissociation of aggregates destroys the signal. There was no effect of high salt concentrations. Binding to the \u003Cjats:italic>β\u003C\u002Fjats:italic>(1–40) is of lower affinity, \u003Cjats:italic>K\u003Cjats:sub>d\u003C\u002Fjats:sub>\u003C\u002Fjats:italic> 2 \u003Cjats:italic>μ\u003C\u002Fjats:italic>M, while it saturates with a \u003Cjats:italic>K\u003Cjats:sub>d\u003C\u002Fjats:sub>\u003C\u002Fjats:italic> of 0.54 \u003Cjats:italic>μ\u003C\u002Fjats:italic>M for \u003Cjats:italic>β\u003C\u002Fjats:italic>(1–28). Insulin fibrils converted to a \u003Cjats:italic>β\u003C\u002Fjats:italic>‐sheet conformation fluoresce intensely with ThT. A variety of polyhydroxy, polyanionic, or polycationic materials fail to interact or impede interaction with the amyloid peptides. This fluorometric technique should allow the kinetic elucidation of the amyloid fibril assembly process as well as the testing of agents that might modulate their assembly or disassembly.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>Thioflavine T (ThT) liên kết nhanh chóng với các sợi kết tụ của các peptide được chiết xuất từ \u003Cjats:italic>β\u003C\u002Fjats:italic>\u002FA4, cụ thể là \u003Cjats:italic>β\u003C\u002Fjats:italic>(1–28) và \u003Cjats:italic>β\u003C\u002Fjats:italic>(1–40), tạo ra một cực đại hấp thụ (ex) mới tại 450 nm và phát xạ (em) gia tăng ở 482 nm, khác với các giá trị 385 nm (ex) và 445 nm (em) của thuốc nhuộm tự do. Sự thay đổi này phụ thuộc vào trạng thái kết tụ vì các peptide monomer hoặc dimer không phản ứng, và sự phân ly guanidine của các chuỗi kết tụ làm mất tín hiệu. Không có ảnh hưởng của nồng độ muối cao. Liên kết với \u003Cjats:italic>β\u003C\u002Fjats:italic>(1–40) có ái lực thấp hơn, \u003Cjats:italic>K\u003Cjats:sub>d\u003C\u002Fjats:sub>\u003C\u002Fjats:italic> 2 \u003Cjats:italic>μ\u003C\u002Fjats:italic>M, trong khi nó bão hòa với \u003Cjats:italic>K\u003Cjats:sub>d\u003C\u002Fjats:sub>\u003C\u002Fjats:italic> là 0.54 \u003Cjats:italic>μ\u003C\u002Fjats:italic>M cho \u003Cjats:italic>β\u003C\u002Fjats:italic>(1–28). Các sợi insulin chuyển đổi thành cấu hình \u003Cjats:italic>β\u003C\u002Fjats:italic>-sheet phát huỳnh quang mạnh mẽ với ThT. Một loạt các vật liệu polyhydroxy, polyanionic hoặc polycationic không tương tác hoặc cản trở sự tương tác với các peptide amyloid. Kỹ thuật huỳnh quang này sẽ cho phép làm sáng tỏ động học của quá trình lắp ráp sợi amyloid cũng như kiểm tra các tác nhân có thể điều chỉnh sự lắp ráp hoặc tháo rời của chúng.\u003C\u002Fjats:p>",{"EN":2093,"VI":2094},"Thioflavine T interaction with synthetic Alzheimer's disease \u003Ci>β\u003C\u002Fi>‐amyloid peptides: Detection of amyloid aggregation in solution","Tương tác của Thioflavine T với các peptide \u003Ci>β\u003C\u002Fi>‐amyloid tổng hợp trong bệnh Alzheimer: Phát hiện sự kết tụ amyloid trong dung dịch",{"VOID":2096},"8453378",{"VOID":2098},"10.1002\u002Fpro.5560020312",[31],[30],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fpro.5560020312",[2103],{"id":2104,"sortIndex":32,"researcher":28,"roles":2105,"affiliations":2106,"properties":2115,"displayName":2117,"givenName":28,"familyName":28},"89b0dd33-000f-4c48-a6ef-542490186828",[],[2107],{"id":2108,"sortIndex":32,"affiliation":2109,"properties":28},"b6b4f66d-a981-44c3-a1e7-309eb08d3963",{"id":2108,"createTime":28,"updateTime":28,"relativeEntities":2110,"slug":28,"properties":2111,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2114,"statistic":28},[],{"title":2112},{"EN":2113},"Department of Neuroscience Pharmacology, Parke-Davis Pharmaceutical Research Division, Warner-Lambert Company, Ann Arbor, Michigan 48106-1047.",[],{"title":2116,"openalex":2118},{"EN":2117},"Harry 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H., 1990, Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: Use of the fluorescent indicator thioflavine T, Lab. Invest., 62, 768",{},{"id":28,"text":2237,"url":28,"identifiers":2238},"Naiki H., 1991, Kinetic analysis of amyloid fibril polymerization in vitro, Lab. Invest., 65, 104",{},{"id":28,"text":2240,"url":28,"identifiers":2241},"10.1016\u002F0003-9861(92)90735-F",{"doi":2240},{"id":28,"text":2243,"url":28,"identifiers":2244},"Vassar P.S., 1959, Fluorescent stains, with special reference to amyloid and connective tissue, Arch. Pathol., 68, 487",{},{"id":28,"text":2246,"url":28,"identifiers":2247},"Venkataraman K., 1952, The Chemistry of Synthetic Dyes, 622",{},{"id":28,"text":2249,"url":28,"identifiers":2250},"10.1007\u002FBF01935322",{"doi":2249},{"id":2252,"createTime":2253,"updateTime":2254,"relativeEntities":2255,"slug":2256,"properties":2257,"entityType":1030,"verifyStatus":26,"verifyTime":2253,"verifyNote":1032,"languages":2274,"translateLanguages":2275,"viewCount":32,"primaryUrl":2276,"fullTextUrl":28,"authors":2277,"publicationType":1136,"publisherRelationship":2329,"citationCount":2386,"citationInfo":2387,"publishDate":2396,"publishYear":2388,"citationAnalyzeStatus":884,"lastCitationAnalyze":28,"indexDatabases":2397,"openAccess":28,"references":2398,"isForceReanalyzing":1396},"c5a7c24d-1ebc-48a1-9683-e2d239f7e685","2024-10-09T09:07:16.854+00:00","2025-02-06T01:54:54.592+00:00",[],"Modeling-of-loops-in-protein-structures",{"mag":2258,"keywords":2260,"pmc":2261,"openalex":2263,"abstract":2265,"title":2268,"pm":2271,"doi":2273},{"VOID":2259},"1980374511",{"VI":1015},{"VOID":2262},"2144714",{"VOID":2264},"W1980374511",{"EN":2266,"VI":2267},"\u003Cjats:title>Abstract\u003C\u002Fjats:title>\u003Cjats:p>Comparative protein structure prediction is limited mostly by the errors in alignment and loop modeling. We describe here a new automated modeling technique that significantly improves the accuracy of loop predictions in protein structures. The positions of all nonhydrogen atoms of the loop are optimized in a fixed environment with respect to a pseudo energy function. The energy is a sum of many spatial restraints that include the bond length, bond angle, and improper dihedral angle terms from the CHARMM‐22 force field, statistical preferences for the main‐chain and side‐chain dihedral angles, and statistical preferences for nonbonded atomic contacts that depend on the two atom types, their distance through space, and separation in sequence. The energy function is optimized with the method of conjugate gradients combined with molecular dynamics and simulated annealing. Typically, the predicted loop conformation corresponds to the lowest energy conformation among 500 independent optimizations. Predictions were made for 40 loops of known structure at each length from 1 to 14 residues. The accuracy of loop predictions is evaluated as a function of thoroughness of conformational sampling, loop length, and structural properties of native loops. When accuracy is measured by local superposition of the model on the native loop, 100, 90, and 30% of 4–, 8–, and 12–residue loop predictions, respectively, had <2 Å RMSD error for the mainchain N, Ca, C, and O atoms; the average accuracies were 0.59 6 0.05, 1.16 6 0.10, and 2.61 6 0.16 Å, respectively. To simulate real comparative modeling problems, the method was also evaluated by predicting loops of known structure in only approximately correct environments with errors typical of comparative modeling without misalignment. When the RMSD distortion of the main‐chain stem atoms is 2.5 Å, the average loop prediction error increased by 180, 25, and 3% for 4–, 8–, and 12–residue loops, respectively. The accuracy of the lowest energy prediction for a given loop can be estimated from the structural variability among a number of low energy predictions. The relative value of the present method is gauged by (1) comparing it with one of the most successful previously described methods, and (2) describing its accuracy in recent blind predictions of protein structure. Finally, it is shown that the average accuracy of prediction is limited primarily by the accuracy of the energy function rather than by the extent of conformational sampling.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>Dự đoán cấu trúc protein so sánh chủ yếu bị hạn chế bởi các lỗi trong việc căn chỉnh và mô hình hóa vòng. Chúng tôi giới thiệu một kỹ thuật mô hình hóa tự động mới, giúp cải thiện đáng kể độ chính xác của dự đoán vòng trong cấu trúc protein. Vị trí của tất cả các nguyên tử không hydro trong vòng được tối ưu hóa trong một môi trường cố định với một hàm năng lượng giả. Năng lượng là tổng của nhiều ràng buộc không gian, bao gồm độ dài liên kết, góc liên kết, và các thuật ngữ góc dihedral không chính xác từ miền lực CHARMM‐22, các sở thích thống kê cho các góc dihedral của chuỗi chính và chuỗi phụ, và các sở thích thống kê cho các tiếp xúc nguyên tử không liên kết, phụ thuộc vào hai loại nguyên tử, khoảng cách giữa chúng trong không gian, và khoảng cách trong chuỗi. Hàm năng lượng được tối ưu hóa bằng phương pháp gradient liên hợp kết hợp với động lực học phân tử và tôi luyện mô phỏng. Thông thường, cấu hình vòng dự đoán tương ứng với cấu hình năng lượng thấp nhất trong số 500 lần tối ưu hóa độc lập. Các dự đoán được thực hiện cho 40 vòng có cấu trúc đã biết ở mỗi chiều dài từ 1 đến 14 amino acid. Độ chính xác của các dự đoán vòng được đánh giá dựa trên mức độ đầy đủ của mẫu hình thái, chiều dài vòng, và các thuộc tính cấu trúc của các vòng tự nhiên. Khi độ chính xác được đo bằng sự chồng lấp cục bộ của mô hình lên vòng tự nhiên, 100%, 90%, và 30% của các dự đoán vòng dài 4, 8, và 12 amino acid, tương ứng, có sai số RMSD < 2 Å cho các nguyên tử N, Ca, C, và O của chuỗi chính; các độ chính xác trung bình lần lượt là 0,59 ± 0,05, 1,16 ± 0,10, và 2,61 ± 0,16 Å. Để mô phỏng các vấn đề mô hình so sánh thực tế, phương pháp này cũng được đánh giá qua việc dự đoán các vòng có cấu trúc đã biết trong chỉ các môi trường tương đối chính xác với các lỗi điển hình của mô hình so sánh mà không có sự căn chỉnh sai. Khi biến dạng RMSD của các nguyên tử thân chuỗi chính là 2,5 Å, sai số dự đoán vòng trung bình tăng thêm 180%, 25%, và 3% cho vòng dài 4, 8, và 12 amino acid, tương ứng. Độ chính xác của dự đoán năng lượng thấp nhất cho một vòng nhất định có thể được ước lượng từ sự biến thể cấu trúc giữa một số dự đoán năng lượng thấp. Giá trị tương đối của phương pháp hiện tại được đánh giá qua (1) việc so sánh với một trong các phương pháp thành công nhất đã được miêu tả trước đây, và (2) mô tả độ chính xác của nó trong các dự đoán mù gần đây về cấu trúc protein. Cuối cùng, cho thấy rằng độ chính xác trung bình của dự đoán chủ yếu bị giới hạn bởi độ chính xác của hàm năng lượng, chứ không phải là phạm vi của mẫu hình thái.",{"EN":2269,"VI":2270},"Modeling of loops in protein structures","Mô hình hóa các vòng trong cấu trúc 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MODELLER a protein structure modeling program release 5. 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Results of this analysis showed that these proteins do not possess uniform structural properties, as expected for members of a single thermodynamic entity. Rather, these proteins may be divided into two structurally different groups: intrinsic coils, and premolten globules. Proteins from the first group have hydrodynamic dimensions typical of random coils in poor solvent and do not possess any (or almost any) ordered secondary structure. Proteins from the second group are essentially more compact, exhibiting some amount of residual secondary structure, although they are still less dense than native or molten globule proteins. An important feature of the intrinsically unstructured proteins is that they undergo disorder–order transition during or prior to their biological function. In this respect, the Protein Quartet model, with function arising from four specific conformations (ordered forms, molten globules, premolten globules, and random coils) and transitions between any two of the states, is discussed.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>Vật liệu thử nghiệm tích lũy trong tài liệu về hành vi cấu hình của protein không cấu trúc tự nhiên (protein không gấp tự nhiên) đã được phân tích. Kết quả của phân tích này cho thấy rằng những protein này không sở hữu các đặc tính cấu trúc đồng nhất, như mong đợi đối với các thành viên của một thực thể nhiệt động lực học đơn lẻ. Thay vào đó, các protein này có thể được chia thành hai nhóm cấu trúc khác nhau: cuộn nội tại và globule tiền nóng chảy. Các protein từ nhóm đầu tiên có kích thước thủy động học điển hình của cuộn ngẫu nhiên trong dung môi kém và không có (hoặc hầu như không có) cấu trúc thứ cấp có trật tự nào. Các protein từ nhóm thứ hai thì gọn hơn về mặt cấu trúc, thể hiện một lượng cấu trúc thứ cấp dư thừa, mặc dù chúng vẫn kém đặc hơn so với các protein globule tự nhiên hoặc nóng chảy. Một đặc điểm quan trọng của các protein không cấu trúc tự nhiên là chúng trải qua sự chuyển tiếp từ hỗn loạn sang trật tự trong hoặc trước khi thực hiện chức năng sinh học của chúng. Trong khía cạnh này, mô hình Bộ tứ Protein, với chức năng phát sinh từ bốn dạng cấu hình cụ thể (hình thức có trật tự, globule nóng chảy, globule tiền nóng chảy, và cuộn ngẫu nhiên) và sự chuyển tiếp giữa bất kỳ hai trạng thái nào, được thảo luận.\u003C\u002Fjats:p>",{"EN":2822,"VI":2823},"Natively unfolded proteins: A point where biology waits for physics","Protein không cấu trúc tự nhiên: Một điểm mà sinh học chờ đợi vật lý",{"VOID":2825},"11910019",{"VOID":2827},"10.1110\u002Fps.4210102","2024-09-20T17:37:51.995+00:00",[31],[30],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1110\u002Fps.4210102",[2833],{"id":2834,"sortIndex":32,"researcher":28,"roles":2835,"affiliations":2836,"properties":2845,"displayName":2849,"givenName":28,"familyName":28},"189d5f0d-5a5c-40b7-a76a-1f7e9e3fc6fd",[],[2837],{"id":2838,"sortIndex":32,"affiliation":2839,"properties":28},"1825992c-3487-40d8-84bc-69fc7d11a5e7",{"id":2838,"createTime":28,"updateTime":28,"relativeEntities":2840,"slug":28,"properties":2841,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":2844,"statistic":28},[],{"title":2842},{"VI":2843},"Institute for Biological Instrumentation, Russian Academy of Sciences, 142292 Pushchino, Moscow Region, Russia",[],{"orcid":2846,"title":2848,"openalex":2850},{"VOID":2847},"https:\u002F\u002Forcid.org\u002F0000-0002-4037-5857",{"EN":2849},"Vladimir N. 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The \u003Cjats:italic>m\u003C\u002Fjats:italic> value correlates very strongly with the amount of protein surface exposed to solvent upon unfolding, with linear correlation coefficients of \u003Cjats:italic>R\u003C\u002Fjats:italic> = 0.84 for urea and \u003Cjats:italic>R\u003C\u002Fjats:italic> = 0.87 for guanidine hydrochloride. These correlations improve to \u003Cjats:italic>R\u003C\u002Fjats:italic> = 0.90 when the effect of disulfide bonds on the accessible area of the unfolded protein is included. A similar dependence on accessible surface area has been found previously for the heat capacity change (ΔC\u003Cjats:italic>\u003Cjats:sub>p\u003C\u002Fjats:sub>\u003C\u002Fjats:italic>), which is confirmed here for our set of proteins. Denaturant \u003Cjats:italic>m\u003C\u002Fjats:italic> values and heat capacity changes also correlate well with each other. For proteins that undergo a simple two‐state unfolding mechanism, the amount of surface exposed to solvent upon unfolding is a main structural determinant for both \u003Cjats:italic>m\u003C\u002Fjats:italic> values and Δ\u003Cjats:italic>C\u003Cjats:sub>p\u003C\u002Fjats:sub>\u003C\u002Fjats:italic>.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>Giá trị biến tính \u003Cjats:italic>m\u003C\u002Fjats:italic>, sự phụ thuộc của năng lượng tự do của quá trình mở ra vào nồng độ chất biến tính, đã được thu thập cho một tập hợp lớn các protein. Giá trị \u003Cjats:italic>m\u003C\u002Fjats:italic> tương quan rất mạnh với lượng bề mặt protein tiếp xúc với dung môi khi mở ra, với hệ số tương quan tuyến tính \u003Cjats:italic>R\u003C\u002Fjats:italic> = 0.84 cho urê và \u003Cjats:italic>R\u003C\u002Fjats:italic> = 0.87 cho guanidin hydrochloride. Những tương quan này cải thiện lên \u003Cjats:italic>R\u003C\u002Fjats:italic> = 0.90 khi hiệu ứng của liên kết disulfide trên diện tích có thể tiếp cận của protein đã được mở ra được đưa vào. Một sự phụ thuộc tương tự vào diện tích bề mặt có thể tiếp cận đã được phát hiện trước đó cho sự thay đổi nhiệt dung (ΔC\u003Cjats:italic>\u003Cjats:sub>p\u003C\u002Fjats:sub>\u003C\u002Fjats:italic>), điều này được xác nhận ở đây cho tập hợp protein của chúng tôi. Các giá trị \u003Cjats:italic>m\u003C\u002Fjats:italic> của chất biến tính và sự thay đổi nhiệt dung cũng tương quan tốt với nhau. Đối với các protein trải qua cơ chế mở ra đơn giản hai trạng thái, lượng bề mặt tiếp xúc với dung môi khi mở ra là một yếu tố cấu trúc chính cho cả giá trị \u003Cjats:italic>m\u003C\u002Fjats:italic> và Δ\u003Cjats:italic>C\u003Cjats:sub>p\u003C\u002Fjats:sub>\u003C\u002Fjats:italic>.\u003C\u002Fjats:p>",{"EN":3562,"VI":3563},"Denaturant \u003Ci>m\u003C\u002Fi> values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding","Giá trị \u003Ci>m\u003C\u002Fi> của chất biến tính và sự thay đổi nhiệt dung: Mối quan hệ với sự thay đổi trong diện tích bề mặt tiếp xúc của sự mở ra của protein",{"VOID":3565},"8535251",{"VOID":3567},"10.1002\u002Fpro.5560041020",[31],[30],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fpro.5560041020",[3572,3589,3605],{"id":3573,"sortIndex":32,"researcher":28,"roles":3574,"affiliations":3575,"properties":3584,"displayName":3586,"givenName":28,"familyName":28},"7723a0f4-6c60-465d-a84b-fb9f21693ec2",[],[3576],{"id":3577,"sortIndex":32,"affiliation":3578,"properties":28},"dda81646-bf0b-468e-8909-57e06ade6350",{"id":3577,"createTime":28,"updateTime":28,"relativeEntities":3579,"slug":28,"properties":3580,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":3583,"statistic":28},[],{"title":3581},{"EN":3582},"Department of Biochemistry and Biophysics, Texas A&M University, College Station, 77843, USA.",[],{"title":3585,"openalex":3587},{"EN":3586},"Jeffrey K. 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The analyses are primarily image‐based and include protein secondary structure, protein‐ligand and protein‐DNA interactions, PROCHECK analyses of structural quality, and many others. The 3D structures can be viewed interactively in RasMol, PyMOL, and a JavaScript viewer called 3Dmol.js. Users can upload their own PDB files and obtain a set of password‐protected PDBsum analyses for each. The server is freely accessible to all at: \u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"http:\u002F\u002Fwww.ebi.ac.uk\u002Fpdbsum\">http:\u002F\u002Fwww.ebi.ac.uk\u002Fpdbsum\u003C\u002Fjats:ext-link>.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p>PDBsum là một máy chủ web cung cấp thông tin cấu trúc về các mục trong Ngân hàng Dữ liệu Protein (PDB). Các phân tích chủ yếu dựa trên hình ảnh và bao gồm cấu trúc bậc hai của protein, tương tác giữa protein và ligand, tương tác giữa protein và DNA, phân tích PROCHECK về chất lượng cấu trúc, và nhiều phân tích khác. Các cấu trúc 3D có thể được xem tương tác trong RasMol, PyMOL, và một trình xem JavaScript có tên là 3Dmol.js. Người dùng có thể tải lên các tệp PDB của riêng họ và nhận một tập hợp các phân tích PDBsum được bảo vệ bằng mật khẩu cho mỗi tệp. Máy chủ này hoàn toàn miễn phí và có thể truy cập cho tất cả mọi người tại: \u003Cjats:ext-link xmlns:xlink=\"http:\u002F\u002Fwww.w3.org\u002F1999\u002Fxlink\" xlink:href=\"http:\u002F\u002Fwww.ebi.ac.uk\u002Fpdbsum\">http:\u002F\u002Fwww.ebi.ac.uk\u002Fpdbsum\u003C\u002Fjats:ext-link>.\u003C\u002Fjats:p>",{"EN":4243,"VI":4244},"PDBsum: Structural summaries of PDB entries","PDBsum: Tóm tắt cấu trúc của các mục trong PDB",{"VOID":4246},"28875543",{"VOID":4248},"10.1002\u002Fpro.3289","2024-10-15T10:47:34.530+00:00",[31],[30],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fpro.3289",[4254,4273,4292,4311,4328],{"id":4255,"sortIndex":32,"researcher":28,"roles":4256,"affiliations":4257,"properties":4266,"displayName":4270,"givenName":28,"familyName":28},"35c1275f-e057-42b2-ad2f-be598a33e17c",[],[4258],{"id":4259,"sortIndex":32,"affiliation":4260,"properties":28},"638ef433-fdf8-4770-9bba-a2b2fc6c13f2",{"id":4259,"createTime":28,"updateTime":28,"relativeEntities":4261,"slug":28,"properties":4262,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":4265,"statistic":28},[],{"title":4263},{"EN":4264},"European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL–EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, United Kingdom",[],{"orcid":4267,"title":4269,"openalex":4271},{"VOID":4268},"https:\u002F\u002Forcid.org\u002F0000-0001-5528-0087",{"EN":4270},"Roman A. 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new method based on protein fragmentation and directly coupled microbore high‐performance liquid chromatography–fast atom bombardment mass spectrometry (HPLC‐FABMS) is described for determining the rates at which peptide amide hydrogens in proteins undergo isotopic exchange. Horse heart cytochrome \u003Cjats:italic>c\u003C\u002Fjats:italic> was incubated in D\u003Cjats:sub>2\u003C\u002Fjats:sub>O as a function of time and temperature to effect isotopic exchange, transferred into slow exchange conditions (pH 2–3, 0 °C), and fragmented with pepsin. The number of peptide amide deuterons present in the proteolytic peptides was deduced from their molecular weights, which were determined following analysis of the digest by HPLC‐FABMS. The present results demonstrate that the exchange rates of amide hydrogens in cytochrome \u003Cjats:italic>c\u003C\u002Fjats:italic> range from very rapid (\u003Cjats:italic>k\u003C\u002Fjats:italic> > 140 h\u003Cjats:sup>−1\u003C\u002Fjats:sup>) to very slow (\u003Cjats:italic>k\u003C\u002Fjats:italic> < 0.002 h\u003Cjats:sup>−1\u003C\u002Fjats:sup>). The deuterium content of specific segments of the protein was determined as a function of incubation temperature and used to indicate participation of these segments in conformational changes associated with heating of cytochrome \u003Cjats:italic>c\u003C\u002Fjats:italic>. For the present HPLC‐FABMS system, approximately 5 nmol of protein were used for each determination. Results of this investigation indicate that the combination of protein fragmentation and HPLC‐FABMS is relatively free of constraints associated with other analytical methods used for this purpose and may be a general method for determining hydrogen exchange rates in specific segments of proteins.\u003C\u002Fjats:p>","\u003Cjats:title>Tóm tắt\u003C\u002Fjats:title>\u003Cjats:p> Một phương pháp mới dựa trên sự phân mảnh protein và độ phân giải cao của sắc ký lỏng nối trực tiếp với phổ khối ion hóa bằng bom nguyên tử nhanh (HPLC‐FABMS) được mô tả để xác định tốc độ mà hydro amide trong protein trải qua quá trình trao đổi đồng vị. Cytochrom \u003Cjats:italic>c\u003C\u002Fjats:italic> của tim ngựa được ủ trong D\u003Cjats:sub>2\u003C\u002Fjats:sub>O tùy theo thời gian và nhiệt độ để thực hiện quá trình trao đổi đồng vị, sau đó chuyển sang điều kiện trao đổi chậm (pH 2–3, 0 °C) và được phân mảnh bằng pepsin. Số lượng deuteron amide peptide có trong các peptide thủy phân được suy luận từ trọng lượng phân tử của chúng, được xác định sau khi phân tích sự tiêu hóa bằng HPLC‐FABMS. Các kết quả hiện tại cho thấy rằng tốc độ trao đổi của hydro amide trong cytochrom \u003Cjats:italic>c\u003C\u002Fjats:italic> dao động từ rất nhanh (\u003Cjats:italic>k\u003C\u002Fjats:italic> > 140 h\u003Cjats:sup>−1\u003C\u002Fjats:sup>) đến rất chậm (\u003Cjats:italic>k\u003C\u002Fjats:italic> \u003C 0.002 h\u003Cjats:sup>−1\u003C\u002Fjats:sup>). Hàm lượng deuterium của các đoạn cụ thể của protein được xác định tùy theo nhiệt độ ủ và được sử dụng để chỉ ra sự tham gia của các đoạn này vào các thay đổi cấu hình liên quan đến việc làm nóng cytochrom \u003Cjats:italic>c\u003C\u002Fjats:italic>. Đối với hệ thống HPLC‐FABMS hiện tại, khoảng 5 nmol protein đã được sử dụng cho mỗi lần xác định. Các kết quả của cuộc điều tra này chỉ ra rằng sự kết hợp giữa phân mảnh protein và HPLC‐FABMS tương đối không bị các ràng buộc liên quan đến các phương pháp phân tích khác được sử dụng cho mục đích này và có thể là một phương pháp chung để xác định tốc độ trao đổi hydro trong các đoạn cụ thể của protein.\u003C\u002Fjats:p>",{"EN":4561,"VI":4562},"Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation","Xác định sự trao đổi hydro amide bằng phổ khối: Một công cụ mới cho việc làm rõ cấu trúc protein",{"VOID":4564},"8390883",{"VOID":4566},"10.1002\u002Fpro.5560020404","Author affiliation is blank",[31],[30],"https:\u002F\u002Fonlinelibrary.wiley.com\u002Fdoi\u002F10.1002\u002Fpro.5560020404",[4572,4591],{"id":4573,"sortIndex":32,"researcher":28,"roles":4574,"affiliations":4575,"properties":4584,"displayName":4588,"givenName":28,"familyName":28},"c1a108b1-7a1a-41db-8b60-95529909da70",[],[4576],{"id":4577,"sortIndex":32,"affiliation":4578,"properties":28},"c8c129fe-e2ed-495a-bb2e-3e8004c5409c",{"id":4577,"createTime":28,"updateTime":28,"relativeEntities":4579,"slug":28,"properties":4580,"entityType":28,"verifyStatus":28,"verifyTime":28,"verifyNote":28,"languages":28,"translateLanguages":28,"viewCount":28,"url":28,"parentIds":4583,"statistic":28},[],{"title":4581},{"VI":4582},"Department of Medicinal Chemistry and Pharmacognosy, Purdue University, West Lafayette, Indiana 47907.",[],{"orcid":4585,"title":4587,"openalex":4589},{"VOID":4586},"https:\u002F\u002Forcid.org\u002F0000-0002-8326-6714",{"EN":4588},"Zhongqi Zhang",{"VOID":4590},"A5030829436",{"id":4592,"sortIndex":40,"researcher":28,"roles":4593,"affiliations":4594,"properties":4595,"displayName":4599,"givenName":28,"familyName":28},"e11802cb-221b-4e32-9d7f-b94c6ff9ed82",[],[],{"orcid":4596,"title":4598,"openalex":4600},{"VOID":4597},"https:\u002F\u002Forcid.org\u002F0000-0003-2559-7109",{"EN":4599},"David L. 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