Curvature and Torsion of Protein Main Chain as Local Order Parameters of Protein Unfolding.
Journal
The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530
Informations de publication
Date de publication:
04 06 2020
04 06 2020
Historique:
pubmed:
12
5
2020
medline:
15
5
2021
entrez:
12
5
2020
Statut:
ppublish
Résumé
Thermal protein unfolding resembles a global (two-state) phase transition. At the local scale, protein unfolding is, however, heterogeneous and probe dependent. Here, we consider local order parameters defined by the local curvature and torsion of the protein main chain. Because chemical shifts (CS's) measured by NMR spectroscopy are extremely sensitive to the local atomic environment, CS has served as a local probe of thermal unfolding of proteins by varying the position of the atomic isotope along the amino acid sequence. The variation of the CS of each C
Identifiants
pubmed: 32392067
doi: 10.1021/acs.jpcb.0c01230
pmc: PMC7362589
mid: NIHMS1601121
doi:
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
4391-4398Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM014312
Pays : United States
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