Biomolecular NMR Assignments

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1H, 15N and 13C backbone and side chain solution NMR assignments of the TPM domain-containing protein of the thermophilic bacterium Rhodothermus marinus
Biomolecular NMR Assignments - Tập 17 - Trang 229-233 - 2023
Leonardo Pellizza, Lila Ramis, Ignacio Argañaraz Araoz, Martín Aran
The InterPro family IPR007621 TPM_phosphatase is a widely conserved family of protein domains found in prokaryotes, plants and invertebrates. Despite similar predicted protein folding, members of this family are involved in different cellular processes. In recent years, the structural and biochemical characterization of evolutionarily divergent TPM domains has shown their ability to hydrolyze phos...... hiện toàn bộ
Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin
Biomolecular NMR Assignments - Tập 8 - Trang 225-228 - 2013
Michael C. Brothers, Brett Geissler, Grant S. Hisao, Brenda A. Wilson, Karla J. F. Satchell, Chad M. Rienstra
1H, 13C, and 15N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain from the domain of unknown function 5 (DUF5) effector (MLDVvDUF5) of the MARTX toxin from Vibrio vulnificus in its solution state. We have assigned 97 % of all backbone and side-chain carbon atoms, including 96 % of all backbone residues. Secondary ch...... hiện toàn bộ
Assignment of 1H, 13C and 15N resonances of the reduced human IgG1 CH3 domain
Biomolecular NMR Assignments - - 2007
Dingjiang Liu, Melanie J. Cocco, Masazumi Matsumura, Da Ren, Bridget A. Becker, Richard L. Remmele, David N. Brems
Backbone and side-chain chemical shift assignments of MarH, a critical intermediary epimerase for biosynthesis of Maremycins in Streptomyces
Biomolecular NMR Assignments - Tập 12 - Trang 335-338 - 2018
Bin Liu, Shiqi Fang, Xiaofang Ma, Zhiqiang Bai, Kaifeng Hu
MarH is an essential epimerase that catalyzes the isomerization of 3R-β-methyl-indolepyruvate (β-MeInPy) to 3S-β-MeInPy, which is the important precursor for biosynthesis of Maremycins. Biophysical study of the structure of MarH would be informative for better understanding of its catalytic mechanism and feasible application of the enzyme in isomerization reaction. Here, we report the backbone and...... hiện toàn bộ
Chemical shift assignments of the catalytic domain from the yeast proline isomerase Fpr4p
Biomolecular NMR Assignments - Tập 6 Số 2 - Trang 123-126 - 2012
Yoan R. Monneau, Christopher J. Nelson, Cameron D. Mackereth
Backbone and side chain NMR assignment of the heme-nitric oxide/oxygen binding (H-NOX) domain from Nostoc punctiforme
Biomolecular NMR Assignments - Tập 16 - Trang 379-384 - 2022
Styliani A. Chasapi, Aikaterini I. Argyriou, Georgios A. Spyroulias
Soluble guanylate cyclase (sGC) is considered as the primary NO receptor across several known eukaryotes. The main interest regarding the biological role and its function, focuses on the H-NOX domain of the β1 subunit. This domain in its active form bears a ferrous b type heme as prosthetic group, which facilitates the binding of NO and other diatomic gases. The key point that still needs to be an...... hiện toàn bộ
Resonance assignments and secondary structure of apolipoprotein E C-terminal domain in DHPC micelles
Biomolecular NMR Assignments - Tập 9 - Trang 187-190 - 2014
Chi-Jen Lo, Chia-Lin Chyan, Yi-Chen Chen, Chi-Fon Chang, Hsien-bin Huang, Ta-Hsien Lin
Human apolipoprotein E (apoE) has been known to play a key role in the transport of plasma cholesterol and lipoprotein metabolism. It is an apolipoprotein of 299 amino acids with a molecular mass, ~34 kDa. ApoE has three major isoforms, apoE2, apoE3, and apoE4 which differ only at residue 112 or 158. ApoE consists of two independently folded domains (N-terminal and C-terminal domain) separated by ...... hiện toàn bộ
13C, 15N and 1H backbone and side chain chemical shift assignment of acid-stress bacterial chaperone HdeA at pH 6
Biomolecular NMR Assignments - - 2014
Karin A. Crowhurst
Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists
Biomolecular NMR Assignments - Tập 1 - Trang 241-243 - 2007
Michael K. Fenwick, Robert E. Oswald
Backbone 1H, 13C, and 15N chemical shifts are reported for complexes of a perdeuterated glutamate receptor ligand binding domain with kainate, willardiine, and 5-substituted fluoro-, bromo-, and iodowillardiine. These ligands are partial agonists that induce distinct current responses at post-synaptic neurons. The chemical shifts pave the way for numerous NMR studies to identify structural and dyn...... hiện toàn bộ
Backbone and side-chain resonance assignments (1H, 15N and 13C) of the ubiquitin homology domain of mouse BAG-1
Biomolecular NMR Assignments - Tập 7 - Trang 235-239 - 2012
Hsiao-Wen Huang, Chin Yu
BAG-1, an important regulatory protein associates with several signaling molecules and is capable of suppressing apoptosis. A 97-amino acid segment that includes the ubiquitin homology domain of mouse BAG-1 interacts with the cytoplasmic tail domain of proHB-EGF, and this interaction is likely to have functional significance. Here we report the backbone and side-chain resonance assignments for thi...... hiện toàn bộ
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