Origins of Conformational Heterogeneity in Peptoid Helices Formed by Chiral
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:
13 07 2023
13 07 2023
Historique:
medline:
14
7
2023
pubmed:
28
6
2023
entrez:
28
6
2023
Statut:
ppublish
Résumé
N-substituted glycines (polypeptoids) containing chiral hydrophobic sidechains are known to fold into biomimetic alpha helices. These helix formers often produce conformationally heterogeneous structures and are difficult to characterize at a sub-nanometer resolution. Previously, peptoid
Identifiants
pubmed: 37379075
doi: 10.1021/acs.jpcb.3c02576
doi:
Substances chimiques
Peptoids
0
Water
059QF0KO0R
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM