NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation.

ABSTRACT: The denatured state of a double mutant of the chemotactic protein CheY (F14N/V83T) has been analyzed in the presence of 5 M urea, using small angle X-ray scattering (SAXS) and heteronuclear magnetic resonance. SAXS studies show that the denatured protein follows a wormlike chain model. Its backbone can be described as a chain composed of rigid elements connected by flexible links. A comparison of the contour length obtained for the chain at 5 M urea with the one expected for a fully expanded chain suggests that approximately 25% of the residues are involved in residual structures. Conformational shifts of the alpha-protons, heteronuclear (15)N-[(1)H] NOEs and (15)N relaxation properties have been used to identify some regions in the protein that deviate from a random coil behavior. Accordi

SUBMITTER: Garcia P 

PROVIDER: S-EPMC2374020 | biostudies-literature | 2001 Jun

REPOSITORIES: biostudies-literature