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
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

Pagination

6163-6170

Auteurs

Sarah Alamdari (S)

Department of Chemical Engineering, University of Washington, Seattle, Washington 98195, United States.

Jim Pfaendtner (J)

Department of Chemical Engineering, University of Washington, Seattle, Washington 98195, United States.

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Classifications MeSH