1u06
From Proteopedia
|
crystal structure of chicken alpha-spectrin SH3 domain
Overview
Water molecules are a major determinant of protein stability and are, important for understanding protein-protein interactions. We present two, experiments which allow to measure first the effective T(2) decay rate of, individual amide proton, and second the magnetization build-up rates for a, selective transfer from H(2)O to H(N) using spin diffusion as a mixing, element. The experiments are demonstrated for a uniformly (2)H, (15)N, labeled sample of a microcrystalline SH3 domain in which exchangeable, deuterons were back-substituted with protons. In order to evaluate the NMR, experimental data, as X-ray structure of the protein was determined using, the same crystallization protocol as for the solid-state NMR sample. The, NMR experimental data are correlated with the dipolar couplings calculated, from H(2)O-H(N) distances which were extracted from the X-ray structure of, the protein. We find that the H(N) T(2) decay rates and H(2)O-H(N), build-up rates are sensitive to distance and dynamics of the detected, water molecules with respect to the protein. We show that qualitative, information about localization and dynamics of internal water molecules, can be obtained in the solid-state by interpretation of the spin dynamics, of a reporter amide proton.
About this Structure
1U06 is a Single protein structure of sequence from Gallus gallus with AZI as ligand. Full crystallographic information is available from OCA.
Reference
Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR., Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B, J Biomol NMR. 2005 Apr;31(4):295-310. PMID:15928996
Page seeded by OCA on Wed Nov 21 03:44:22 2007
