Conformational study of Met-enkephalin based on the ECEPP force fields.
We report a computational study of the small peptide Met-enkephalin based on the ECEPP/2 and ECEPP/3 force fields using the basin paving method. We have located a new global minimum when using the ECEPP/3 force field with peptide angles omega fixed at 180 degrees. With this new result, we can conclude that the lowest energy configurations of Met-enkephalin predicted based on all four versions of ECEPP have a classic gamma-turn centered at residue Gly3 and a beta-turn at residues Gly3-Phe4. However, minor differences between the structures also exist.
Zhan
Lixin
L
Department of Physics, University of Waterloo, Waterloo, Ontario, Canada. lzhan@sciborg.uwaterloo.ca
Chen
Jeff Z Y
JZ
Liu
Wing-Ki
WK
D003198:Computer Simulation; D004744:Enkephalin, Methionine / Q000737:chemistry*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary / Q000502:physiology; D013816:Thermodynamics
D010455:Peptides; D004744:Enkephalin, Methionine