Prediction of disulfide dihedral angles using chemical shifts
Author:
Affiliation:
1. The University of Queensland
2. Faculty of Medicine
3. School of Biomedical Sciences
4. Brisbane
5. Australia
6. Institute for Molecular Biosciences
Abstract
Chemical shifts can be used to predict the conformation of disulfide bonds, greatly improving resolution of solution NMR structures.
Funder
Australian Research Council
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2018/SC/C8SC01423J
Reference68 articles.
1. Structure determination of the three disulfide bond isomers of α-conotoxin GI: a model for the role of disulfide bonds in structural stability 1 1Edited by P. E. Wright
2. Thermal, Chemical, and Enzymatic Stability of the Cyclotide Kalata B1: The Importance of the Cyclic Cystine Knot
3. Roles of Individual Disulfide Bonds in the Stability and Folding of an ω-Conotoxin
4. Disulfide bonds as switches for protein function
5. Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
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