An extensive set of experimental NMR residual dipolar couplings (RDCs) has been used to determine the conformational behavior of the SH3 domain of CD2-associated protein. Analytical descriptions of the local dynamics were compared to restraint-free accelerated molecular dynamics simulation, providing a convergent and comprehensive description of conformational fluctuations on picosecond to millisecond timescales.
Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics / L. Salmon, L. Pierce, A. Grimm, J. Ortega roldan, L. Mollica, M.R. Jensen, N. Van nuland, P.R.L. Markwick, J.A. Mccammon, M. Blackledge. - In: ANGEWANDTE CHEMIE. - ISSN 0044-8249. - 124:25(2012 Jun), pp. 6207-6210. [10.1002/ange.201202026]
Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics
L. Mollica;
2012
Abstract
An extensive set of experimental NMR residual dipolar couplings (RDCs) has been used to determine the conformational behavior of the SH3 domain of CD2-associated protein. Analytical descriptions of the local dynamics were compared to restraint-free accelerated molecular dynamics simulation, providing a convergent and comprehensive description of conformational fluctuations on picosecond to millisecond timescales.
| File | Dimensione | Formato | |
|---|---|---|---|
|
Angewandte Chemie - 2012 - Salmon - Multi‐Timescale Conformational Dynamics of the SH3 Domain of CD2‐Associated Protein.pdf
accesso riservato
Tipologia:
Publisher's version/PDF
Dimensione
1.11 MB
Formato
Adobe PDF
|
1.11 MB | Adobe PDF | Visualizza/Apri Richiedi una copia |
Pubblicazioni consigliate
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
