A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
J Mol Biol
; 276(5): 939-54, 1998 Mar 13.
Article
em En
| MEDLINE
| ID: mdl-9566198
ABSTRACT
Two new NMR experiments are presented for measuring side-chain dynamics in proteins. The first method, requiring 15N, 13C, approximately 50% 2H-labeled protein, measures 2H T1 and T1p spin relaxation times at side-chain positions. A second experiment permits the straightforward measurement of 13C-1H dipole-dipole cross-correlation relaxation rates at 13C beta positions in 15N, 13C-labeled molecules. An excellent correlation is observed between order parameters, describing the amplitude of motion at these sites, obtained on the basis of 2H relaxation and dipole-dipole cross-correlation relaxation rates. Together these experiments provide a powerful approach for selecting appropriate motional models. The methods are applied to study the side-chain motional properties of the N-terminal SH3 domain from the signaling protein drk.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Espectroscopia de Ressonância Magnética
/
Proteínas de Insetos
/
Proteínas de Drosophila
Limite:
Animals
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Canadá