Abstract
We describe a computational method for constructing hydrophobically clustered compact conformations of polymer chains having hydrophobic and polar monomers. We call the method “hydrophobic zippers.”1,2 We have used hydrophobic zippers to construct conformational ensembles that resemble the compact denatured and molten globule states of proteins. We have also used hydrophobic zippers to attempt to find global minimum (“native”) conformations of simple HP (H: hydrophobic, P: polar) copolymers in lattice models. In addition, we believe that the sequence of serial steps followed by the hydrophobic zippers construction process closely parallels the sequence of kinetic events in the fast stages of the folding processes of globular proteins.
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© 1994 Springer Science+Business Media New York
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Dill, K.A., Fiebig, K.M. (1994). Hydrophobic Zippers: A Conformational Search Strategy for Proteins. In: Doniach, S. (eds) Statistical Mechanics, Protein Structure, and Protein Substrate Interactions. NATO ASI Series, vol 325. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1349-4_11
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DOI: https://doi.org/10.1007/978-1-4899-1349-4_11
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