Localization of Energetic Frustration in Proteins.
Local frustration
Protein folding
Protein function
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
30
11
2021
pubmed:
1
12
2021
medline:
19
1
2022
Statut:
ppublish
Résumé
We present a detailed heuristic method to quantify the degree of local energetic frustration manifested by protein molecules. Current applications are realized in computational experiments where a protein structure is visualized highlighting the energetic conflicts or the concordance of the local interactions in that structure. Minimally frustrated linkages highlight the stable folding core of the molecule. Sites of high local frustration, in contrast, often indicate functionally relevant regions such as binding, active, or allosteric sites.
Identifiants
pubmed: 34845622
doi: 10.1007/978-1-0716-1716-8_22
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
387-398Informations de copyright
© 2022. Springer Science+Business Media, LLC, part of Springer Nature.
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