Dynamic and conformational switching in proteins.
conformational switching
protein dynamics
sequence mobility
Journal
Biopolymers
ISSN: 1097-0282
Titre abrégé: Biopolymers
Pays: United States
ID NLM: 0372525
Informations de publication
Date de publication:
Oct 2021
Oct 2021
Historique:
revised:
13
11
2020
received:
24
08
2020
accepted:
18
11
2020
pubmed:
4
12
2020
medline:
14
1
2022
entrez:
3
12
2020
Statut:
ppublish
Résumé
Using bioinformatic methods for treating protein dynamics, developed in earlier work, we study the relationship between sequence mobility and dynamics in proteins. It is shown that sequence mobility drives a transition between two dynamic regimes in proteins, and that the specific details of this transition differ qualitatively between α-helical proteins and those in other structural classes. We examine the possibility that conformational switching is related to dynamic switching, by considering a specific system of sequences which exhibit the switching phenomenon. It is shown that a relationship between dynamic and conformational switching is entirely plausible.
Identifiants
pubmed: 33270217
doi: 10.1002/bip.23411
pmc: PMC8172660
mid: NIHMS1696921
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e23411Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM014312
Pays : United States
Organisme : NIH HHS
Pays : United States
Organisme : National Institutes of Health
Informations de copyright
© 2020 Wiley Periodicals LLC.
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