Structural and mutational analyses of psychrophilic and mesophilic adenylate kinases highlight the role of hydrophobic interactions in protein thermal 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:
Mar 2019
Mar 2019
Historique:
received:
22
01
2019
accepted:
07
03
2019
entrez:
22
5
2019
pubmed:
22
5
2019
medline:
22
5
2019
Statut:
epublish
Résumé
Protein thermal stability is an important field since thermally stable proteins are desirable in many academic and industrial settings. Information on protein thermal stabilization can be obtained by comparing homologous proteins from organisms living at distinct temperatures. Here, we report structural and mutational analyses of adenylate kinases (AKs) from psychrophilic
Identifiants
pubmed: 31111079
doi: 10.1063/1.5089707
pii: 1.5089707
pii: 006902SDY
pmc: PMC6498869
doi:
Types de publication
Journal Article
Langues
eng
Pagination
024702Références
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