Protein conformational space in higher order phi-Psi maps.
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.
Sims
Gregory E
GE
Biophysics Graduate Group and Department of Chemistry, University of California, Berkeley, CA 94720, USA.
Choi
In-Geol
IG
Kim
Sung-Hou
SH
D016000:Cluster Analysis; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D010455:Peptides; D011506:Proteins