Side-chain and backbone ordering in a polypeptide.
We report results from multicanonical simulations of polyglutamic acid chains of length of ten residues. For this simple polypeptide we observe a decoupling of backbone and side-chain ordering in the folding process. While the details of the two transitions vary between the peptide in gas phase and in an implicit solvent, our results indicate that, independent of the specific surroundings, upon continuously lowering the temperature side-chain ordering occurs only after the backbone topology is completely formed.
Wei
Yanjie
Y
Department of Physics, Michigan Technological University, Houghton, Michigan 49931, USA. yawei@mtu.edu
Nadler
Walter
W
Hansmann
Ulrich H E
UH
D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D013696:Temperature
D010455:Peptides