High-throughput thermal denaturation of tryptophanyl-tRNA synthetase combinatorial mutants reveals high-order energetic coupling determinants of conformational stability.
Journal
Structural dynamics (Melville, N.Y.)
ISSN: 2329-7778
Titre abrégé: Struct Dyn
Pays: United States
ID NLM: 101660872
Informations de publication
Date de publication:
Jul 2023
Jul 2023
Historique:
received:
07
02
2023
accepted:
13
07
2023
medline:
28
8
2023
pubmed:
28
8
2023
entrez:
28
8
2023
Statut:
epublish
Résumé
Landscape descriptions provide a framework for identifying functionally significant dynamic linkages in proteins but cannot supply details. Rate measurements of combinatorial mutations can implicate dynamic linkages in catalysis. A major difficulty is filtering dynamic linkages from the vastly more numerous static interactions that stabilize domain folding. The
Identifiants
pubmed: 37637481
doi: 10.1063/4.0000182
pii: 4.0000182
pmc: PMC10449480
doi:
Types de publication
Journal Article
Langues
eng
Pagination
044304Informations de copyright
© 2023 Author(s).
Déclaration de conflit d'intérêts
The authors have no conflicts to disclose.
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