The relative stability of trpzip1 and its mutants determined by computation and experiment
Author:
Affiliation:
1. Department of Chemistry
2. Johns Hopkins University
3. Baltimore
4. USA
5. Kimberly-Clark Corporation
6. Atlanta
Abstract
The single-point mutations of tprzip1 are indicated at left, and their relative energetics are compared at right.
Funder
Division of Chemistry
National Science Foundation
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/RA/D0RA00920B
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1. Minimal model systems for β-sheet secondary structure in proteins
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4. Designed Trpzip-3 β-Hairpin Inhibits Amyloid Formation in Two Different Amyloid Systems
5. Stabilization of β-Hairpin Peptides by Salt Bridges: Role of Preorganization in the Energetic Contribution of Weak Interactions
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