Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding

Protein Science - Tập 4 Số 10 - Trang 2138-2148 - 1995
Jeffrey K. Myers1, C. Nick Pace2, J. Martin Scholtz2
1Department of Biochemistry and Biophysics, Texas A&M University, College Station, 77843, USA.
2Department of Biochemistry and Biophysics. Department of Medical Biochemistry and Genetics, and Center for Macromolecular Design, Texas A&M University, College Station, Texas 77843

Tóm tắt

Abstract

Denaturant m values, the dependence of the free energy of unfolding on denaturant concentration, have been collected for a large set of proteins. The m value correlates very strongly with the amount of protein surface exposed to solvent upon unfolding, with linear correlation coefficients of R = 0.84 for urea and R = 0.87 for guanidine hydrochloride. These correlations improve to R = 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 (ΔCp), which is confirmed here for our set of proteins. Denaturant m 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 m values and ΔCp.

Từ khóa


Tài liệu tham khảo

10.1021/bi00010a019

Ahmad F, 1982, Estimation of the free energy of stabilization of ribonuclease A, lysozyme,α‐lactalbumin and myoglobin, J Biol Chem, 257, 12935, 10.1016/S0021-9258(18)33605-6

10.1002/bip.360250906

10.1093/oxfordjournals.jbchem.a124336

10.1002/prot.340080106

10.1021/bi00129a007

10.1021/bi00238a023

10.1021/bi00839a053

10.1021/bi00065a035

10.1002/bip.360261104

10.1021/bi00421a015

10.1021/bi00444a001

Brenstein RJ, 1991, NonLin for Macintosh

10.1021/bi00335a011

10.1002/pro.5560030609

10.1021/bi00006a025

10.1021/bi00067a022

10.1002/pro.5560030811

10.1021/bi00386a048

10.1002/pro.5560030906

10.1021/bi00066a006

10.1146/annurev.bi.60.070191.004051

10.1016/0022-2836(91)90551-G

10.1021/bi00059a006

10.1021/bi00210a045

10.1021/bi00482a009

10.1021/bi00154a023

10.1016/S0021-9258(20)79739-5

10.1002/pro.5560030414

10.1006/jmbi.1994.1234

10.1021/bi00146a008

10.1021/bi00121a009

10.1021/bi00135a019

10.1021/bi00470a021

10.1021/bi00093a001

10.1021/bi00020a026

10.1016/S0076-6879(85)17018-7

10.1021/bi00379a029

10.1021/bi00473a010

10.1021/bi00078a034

10.1016/0022-2836(71)90324-X

10.1002/prot.340080104

10.1073/pnas.90.15.7010

10.1021/bi00132a025

10.1021/bi00231a019

10.1021/bi00197a037

10.1016/0022-2836(92)90963-K

10.1002/pro.5560031207

10.1021/bi00082a021

McLendon G, 1978, Equilibrium and kinetic studies of unfolding of homologous cytochromes c, J Biol Chem, 253, 4004, 10.1016/S0021-9258(17)34790-7

10.1016/0022-2836(87)90038-6

10.1016/0022-2836(85)90384-5

10.1002/pro.5560031110

10.1002/pro.5560031114

10.1016/S0065-3233(08)60556-2

10.1002/prot.340210103

10.3109/10409237509102551

10.1016/0076-6879(86)31045-0

10.1021/bi00125a013

10.1021/bi00462a019

10.1021/bi00569a008

10.1021/bi00384a004

10.1016/0003-9861(81)90209-5

10.1016/S0065-3233(08)60377-0

10.1021/bi00370a032

10.1146/annurev.bb.06.060177.001055

10.1021/bi00003a017

10.1021/bi00493a013

10.1002/bip.360220910

10.1021/bi00421a014

10.1021/bi00135a022

10.1002/bip.1978.360170515

10.1002/bip.360260408

10.1002/pro.5560040106

10.1073/pnas.92.1.185

10.1021/bi00118a013

10.1016/S0065-3233(08)60336-8

10.1002/prot.340010113

10.1021/bi00413a027

10.1016/0003-9861(89)90200-2

10.1021/bi00131a009

10.1021/bi00402a050

10.1021/bi00066a003

10.1002/pro.5560021205

10.1016/S0065-3233(08)60241-7

Taniyama Y, 1992, Folding mechanism of mutant human lysozyme C77/95A with increased secretion efficiency in yeast, J Bio! Chem, 267, 4619, 10.1016/S0021-9258(18)42878-5

10.1021/bi00415a024

10.1021/bi00174a022

10.1002/prot.340180305

Yadav S, 1992, Measuring the conformational stability of proteins, Indian J Chem, 31, 859

10.1021/bi00011a035

10.1021/bi00177a023

10.1002/prot.340090203

10.1021/bi00097a006

Thông tin
Thông tin xuất bản

Protein Science

Tập 4 Số 10

2138-2148

Thông tin tác giả