Evaluating Models of Varying Complexity of Crowded Intrinsically Disordered Protein Solutions Against SAXS.


Journal

Journal of chemical theory and computation
ISSN: 1549-9626
Titre abrégé: J Chem Theory Comput
Pays: United States
ID NLM: 101232704

Informations de publication

Date de publication:
10 Dec 2019
Historique:
pubmed: 13 11 2019
medline: 19 12 2019
entrez: 13 11 2019
Statut: ppublish

Résumé

Intrinsically disordered proteins (IDPs) adopt heterogeneous conformational ensembles in solution. The properties of the conformational ensemble are dependent upon the solution conditions, including the presence of ions, temperature, and crowding, and often directly impact biological function. Many

Identifiants

pubmed: 31714774
doi: 10.1021/acs.jctc.9b00723
doi:

Substances chimiques

Intrinsically Disordered Proteins 0
Solutions 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

6968-6983

Auteurs

Eric Fagerberg (E)

Theoretical Chemistry , Lund University , POB 124, SE-221 00 Lund , Sweden.

Samuel Lenton (S)

Theoretical Chemistry , Lund University , POB 124, SE-221 00 Lund , Sweden.
LINXS - Lund Institute of Advanced Neutron and X-ray Science , Scheelevägen 19 , 223 70 Lund , Sweden.

Marie Skepö (M)

Theoretical Chemistry , Lund University , POB 124, SE-221 00 Lund , Sweden.
LINXS - Lund Institute of Advanced Neutron and X-ray Science , Scheelevägen 19 , 223 70 Lund , Sweden.

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Classifications MeSH