Linking inhibitor motions to proteolytic stability of sunflower trypsin inhibitor-1
Author:
Affiliation:
1. Institute of Theoretical and Computational Chemistry
2. Laboratory of Mesoscopic Chemistry
3. School of Chemistry and Chemical Engineering
4. Nanjing University
5. Nanjing 210023
Abstract
Besides the non-bonded interactions, inhibitor motions especially rotation of the scissile bond also influence proteolytic stability.
Funder
Natural Science Foundation of Jiangsu Province
National Natural Science Foundation of China
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2019/RA/C9RA02114K
Reference91 articles.
1. Rational design and synthesis of an orally bioavailable peptide guided by NMR amide temperature coefficients
2. Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics
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