NMR Characterization of Long-Range Contacts in Intrinsically Disordered Proteins from Paramagnetic Relaxation Enhancement in
NMR spectroscopy
carbon
magnetic properties
proteins
structure elucidation
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
01 02 2019
01 02 2019
Historique:
received:
12
09
2018
pubmed:
9
11
2018
medline:
28
11
2019
entrez:
9
11
2018
Statut:
ppublish
Résumé
Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a stable 3D structure and are able to adopt many different conformations in dynamic equilibrium. The interplay between local dynamics and global rearrangements is key for their function. A widely used experimental NMR spectroscopy approach to study long-range contacts in IDPs exploits paramagnetic effects, and
Identifiants
pubmed: 30407719
doi: 10.1002/cbic.201800539
doi:
Substances chimiques
Carbon Isotopes
0
Intrinsically Disordered Proteins
0
Osteopontin
106441-73-0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
335-339Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.