Protein conformational space in higher order phi-Psi maps.

ABSTRACT: We have mapped protein conformational space from two to seven residue lengths by employing multidimensional scaling on a data matrix composed of pair-wise angular distances for multiple phi-Psi values collected from high-resolution protein structures. The resulting global maps show clustering of peptide conformations that reveals a dramatic reduction of conformational space as sampled by experimentally observed peptides. Each map can be viewed as a higher order phi-Psi plot defining regions of space that are conformationally allowed.

SUBMITTER: Sims GE 

PROVIDER: S-EPMC543483 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature