Exact Sequence Analysis for Three-Dimensional HP Lattice Proteins

Abstract

We have exactly enumerated all sequences and conformations of HP proteins with chains of up to 19 monomers on the simple cubic lattice. For two variants of the hydrophobic-polar (HP) model, where only two types of monomers are distinguished, we determined and statistically analyzed designing sequences, i.e., sequences that have a non-degenerate ground state. Furthermore we were interested in characteristic thermodynamic properties of HP proteins with designing sequences. In order to be able to perform these exact studies, we applied an efficient enumeration method based on contact sets.

12 pages, RevTeX, 21 Postscript figures, Author Information under http://www.physik.uni-leipzig.de/CQT

References in corpus (3)

• Multicanonical Chain Growth Algorithm
• Thermodynamics of Lattice Heteropolymers
• Exact Enumeration of Three-Dimensional Lattice Proteins

Cited by in corpus (6)

• Freezing and Collapse of Flexible Polymers on Regular Lattices in Three Dimensions
• Intra-Globular Structures in Multiblock Copolymer Chains from a Monte Carlo Simulation
• HP-sequence design for lattice proteins - an exact enumeration study on diamond as well as square lattice
• Polymers in disordered environments
• Conformational Transitions of Heteropolymers
• The prion-like folding behavior in aggregated proteins