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.© 2006 American Institute of Physics.
Journal of Chemical Physics
Side-chain and backbone ordering in a polypeptide.
Journal of Chemical Physics,
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