Conformational Transitions of Heteropolymers

Abstract

We study conformational transitions of simple coarse-grained models for protein-like heteropolymers on the simple cubic lattice and off-lattice, respectively, by means of multicanonical sampling algorithms. The effective hydrophobic/polar models do not require the knowledge of the native topology for a given sequence of residues as input. Therefore these models are eligible to investigate general properties of the tertiary folding behaviour of such protein-like heteropolymers.

7 pages

References in corpus (4)

• Multicanonical Chain Growth Algorithm
• Multicanonical Study of Coarse-Grained Off-Lattice Models for Folding Heteropolymers
• Thermodynamics of Lattice Heteropolymers
• Exact Sequence Analysis for Three-Dimensional HP Lattice Proteins

Cited by in corpus (3)

• Exact Partition Function Zeros of a Polymer on a Simple-Cubic Lattice
• Two-State Folding, Folding through Intermediates, and Metastability in a Minimalistic Hydrophobic-Polar Model for Proteins
• Identification of Characteristic Protein Folding Channels in a Coarse-Grained Hydrophobic-Polar Peptide Model