Exploring the conformational space of protein loops using a mean field technique with MOLS sampling.
We have recently developed a computational technique that uses mutually orthogonal Latin square sampling to explore the conformational space of oligopeptides in an exhaustive manner. In this article, we report its use to analyze the conformational spaces of 120 protein loop sequences in proteins, culled from the PDB, having the length ranging from 5 to 10 residues. The force field used did not have any information regarding the sequences or structures that flanked the loop. The results of the analyses show that the native structure of the loop, as found in the PDB falls at one of the low energy points in the conformational landscape of the sequences. Thus, a large portion of the structural determinants of the loop may be considered intrinsic to the sequence, regardless of either adjacent sequences or structures, or the interactions that the atoms of the loop make with other residues in the protein or in neighboring proteins.
Kanagasabai
V
V
Department of Crystallography and Biophysics, University of Madras, Chennai 600 025, India.
Arunachalam
J
J
Prasad
P Arun
PA
Gautham
N
N
D000595:Amino Acid Sequence; D019295:Computational Biology; D018360:Crystallography, X-Ray; D005998:Glycine / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D012997:Solvents
D011506:Proteins; D012997:Solvents; D005998:Glycine