A multifunnel energy landscape encodes the competing α-helix and β-hairpin conformations for a designed peptide
Author:
Affiliation:
1. Department of Chemistry
2. University of Cambridge
3. UK
4. Department of Integrative Structural Biology
5. Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC)
6. CNRS UMR 7104
7. INSERM U964
8. Université de Strasbourg
Abstract
The propensities to form different secondary structures are encoded in the multifunnel nature of the underlying free energy landscape, and conformational switching between such structures is a key element of protein folding and aggregation.
Funder
Engineering and Physical Sciences Research Council
Cambridge Commonwealth, European and International Trust
European Research Council
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2020/CP/C9CP04778F
Reference96 articles.
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5. Engineering Protein Switches: Sensors, Regulators, and Spare Parts for Biology and Biotechnology
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