Banding of NMR-derived methyl order parameters: implications for protein dynamics.

ABSTRACT: Our understanding of protein folding, stability, and function has begun to more explicitly incorporate dynamical aspects. Nuclear magnetic resonance has emerged as a powerful experimental method for obtaining comprehensive site-resolved insight into protein motion. It has been observed that methyl-group motion tends to cluster into three "classes" when expressed in terms of the popular Lipari-Szabo model-free squared generalized order parameter. Here the origins of the three classes or bands in the distribution of order parameters are examined. As a first step, a Bayesian based approach, which makes no a priori assumption about the existence or number of bands, is developed to detect the banding of Oaxis2 values derived either from NMR experiments or molecular dynamics simulations. The ana

SUBMITTER: Sharp KA 

PROVIDER: S-EPMC4142109 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature