作者: John Karanicolas , Charles L. Brooks
DOI: 10.1002/PROT.10459
关键词:
摘要: A class of models that represents a protein chain as sequence "folded" and "unfolded" residues has recently been used to correlate rates mechanisms folding with the native structure. In order better understand conditions under which these "Ising-like" apply, we compare results from this model those obtained an off-lattice uses same potential function. We find Ising-like by construction impose via highly sequential nucleation-condensation mechanism, in turn leads more rugged energy landscapes, fewer "pathways" state, specific case examined here, cold shock Escherichia coli, qualitative difference most likely events folding.