Steric constraints in model proteins

Preprint

23 December 1997

preprint
Published by arXiv in arXiv

https://doi.org/10.48550/arXiv.cond-mat/9712277

Abstract

A simple lattice model for proteins that allows for distinct sizes of the amino acids is presented. The model is found to lead to a significant number of conformations that are the unique ground state of one or more sequences or encodable. Furthermore, several of the encodable structures are highly designable and are the non-degenerate ground state of several sequences. Even though the native state conformations are typically compact, not all compact conformations are encodable. The incorporation of the hydrophobic and polar nature of amino acids further enhances the attractive features of the model.

Keywords

MODEL FOR PROTEINS
STERIC CONSTRAINTS
SIMPLE LATTICE
LATTICE MODEL
CONFORMATIONS
AMINO ACIDS
HYDROPHOBIC
COMPACT
POLAR

All Related Versions

Version 1, 1997-12-23, ArXiv
Published version: Physical Review Letters, 80 (25), 5683.

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