The Ambivalent Role of Proline Residues in an Intrinsically Disordered Protein: From Disorder Promoters to Compaction Facilitators.
(13)C-detection
Intrinsically disordered proteins
NMR spectroscopy
Osteopontin
Proline
Journal
Journal of molecular biology
ISSN: 1089-8638
Titre abrégé: J Mol Biol
Pays: Netherlands
ID NLM: 2985088R
Informations de publication
Date de publication:
17 04 2020
17 04 2020
Historique:
received:
20
08
2019
revised:
23
10
2019
accepted:
14
11
2019
pubmed:
4
12
2019
medline:
31
10
2020
entrez:
4
12
2019
Statut:
ppublish
Résumé
Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a stable three-dimensional structure, but rather adopt many different conformations in dynamic equilibrium. The interplay between local dynamics and global rearrangements is key for their function. In IDPs, proline residues are significantly enriched. Given their unique physicochemical and structural properties, a more detailed understanding of their potential role in stabilizing partially folded states in IDPs is highly desirable. Nuclear magnetic resonance (NMR) spectroscopy, and in particular
Identifiants
pubmed: 31794728
pii: S0022-2836(19)30680-1
doi: 10.1016/j.jmb.2019.11.015
pii:
doi:
Substances chimiques
Avian Proteins
0
SPP1 protein, human
0
Osteopontin
106441-73-0
Proline
9DLQ4CIU6V
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3093-3111Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.