Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.

N. Giraud (1) , A. Bockmann (2) , A. Lesage (1) , F. Penin (2) , M. Blackledge (2) , L. Emsley (1)

1 LC - Laboratoire de Chimie - UMR5182
2 IBCP - Institut de biologie et chimie des protéines [Lyon]

Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state.Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state.

Domaines: Biochimie, Biologie Moléculaire

N. Giraud, A. Bockmann, A. Lesage, F. Penin, M. Blackledge, et al.. Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.. Journal of the American Chemical Society, 2004, 126, pp.11422-11423. ⟨10.1021/ja046578g⟩. ⟨hal-00313002⟩