Accurate structural correlations from maximum likelihood superpositions.

ABSTRACT: The cores of globular proteins are densely packed, resulting in complicated networks of structural interactions. These interactions in turn give rise to dynamic structural correlations over a wide range of time scales. Accurate analysis of these complex correlations is crucial for understanding biomolecular mechanisms and for relating structure to function. Here we report a highly accurate technique for inferring the major modes of structural correlation in macromolecules using likelihood-based statistical analysis of sets of structures. This method is generally applicable to any ensemble of related molecules, including families of nuclear magnetic resonance (NMR) models, different crystal forms of a protein, and structural alignments of homologous proteins, as well as molecular dynamics t

SUBMITTER: Theobald DL 

PROVIDER: S-EPMC2242818 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature