External release of entropy by synchronized movements of local secondary structures drives folding of a small, disulfide-bonded protein.

External release of entropy by synchronized movements of local secondary structures drives folding of a small, disulfide-bonded protein.

A crucial mechanism to the formation of native, fully functional, 3D structures from local secondary structures is unraveled in this study. Through the introduction of various amino acid substitutions at four canonical β-turns in a three-fingered protein, Toxin α from Naja nigricollis, we found that...

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Bibliographic Details
Main Authors: Atsushi Sato, Andre Menez
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2018-01-01
Series:PLoS ONE
Online Access:https://storage.googleapis.com/plos-corpus-prod/10.1371/journal.pone.0198276/1/pone.0198276.pdf?X-Goog-Algorithm=GOOG4-RSA-SHA256&X-Goog-Credential=wombat-sa%40plos-prod.iam.gserviceaccount.com%2F20210220%2Fauto%2Fstorage%2Fgoog4_request&X-Goog-Date=20210220T180127Z&X-Goog-Expires=3600&X-Goog-SignedHeaders=host&X-Goog-Signature=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