A STUDY OF PROTEIN SIDE-CHAIN DYNAMICS FROM NEW H-2 AUTOCORRELATION AND C-13 CROSS-CORRELATION NMR EXPERIMENTS - APPLICATION TO THE N-TERMINAL SH3 DOMAIN FROM DRK
Dw. Yang et al., A STUDY OF PROTEIN SIDE-CHAIN DYNAMICS FROM NEW H-2 AUTOCORRELATION AND C-13 CROSS-CORRELATION NMR EXPERIMENTS - APPLICATION TO THE N-TERMINAL SH3 DOMAIN FROM DRK, Journal of Molecular Biology, 276(5), 1998, pp. 939-954
Two new NMR experiments are presented for measuring side-chain dynamic
s in proteins. The first method, requiring N-15, C-13, similar to 50%
H-2-labeled protein, measures H-2 T-1 and T-1 rho spin relaxation time
s at side-chain positions. A second experiment permits the straightfor
ward measurement of C-13-H-1 dipole-dipole cross-correlation relaxatio
n rates at C-13(beta) positions in N-15, C-13-labeled molecules. An ex
cellent correlation is observed between order parameters, describing t
he amplitude of motion at these sites, obtained on the basis of 2H rel
axation and dipole-dipole cross-correlation relaxation rates. Together
these experiments provide a powerful approach for selecting appropria
te motional models. The methods are applied to study the side-chain mo
tional properties of the N-terminal SH3 domain from the signaling prot
ein drk. (C) 1998 Academic Press Limited.