Re-evaluation of the model-free analysis of fast internal motion in proteins using NMR relaxation.

ABSTRACT: NMR spin relaxation retains a central role in the characterization of the fast internal motion of proteins and their complexes. Knowledge of the distribution and amplitude of the motion of amino acid side chains is critical for the interpretation of the dynamical proxy for the residual conformational entropy of proteins, which can potentially significantly contribute to the entropy of protein function. A popular treatment of NMR relaxation phenomena in macromolecules dissolved in liquids is the so-called model-free approach of Lipari and Szabo. The robustness of the mode-free approach has recently been strongly criticized and the remarkable range and structural context of the internal motion of proteins, characterized by such NMR relaxation techniques, attributed to artifacts arising from

SUBMITTER: Frederick KK 

PROVIDER: S-EPMC2556886 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature