Models for the binding channel of wild type and mutant transthyretin with glabridin
Author:
Affiliation:
1. School of Life Sciences
2. Jilin University
3. Changchun 130012
4. China
5. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education
Abstract
Our results indicate that additional high-occupancy hydrogen bonds were observed at the binding interface between the two dimers in V30A TTR, while stabilisation hydrophobic interactions between residues in the mutant AB loop decreased.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2016/RA/C6RA19814G
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