Energetic Components of Cooperative Protein Folding

Details Energetic Components of Cooperative Protein Folding Energetic Components of Cooperative Protein Folding

2000-10-11

arxiv.org/abs/cond-mat/0010167v1

Phys. Rev. Lett. 85 (2000) 4823-4826.

Physics

Condensed Matter

Statistical Mechanics

11 pages, 4 postscripts figures, Phys. Rev. Lett. (in press)

Scientific paper

10.1103/PhysRevLett.85.4823

A new lattice protein model with a four-helix bundle ground state is analyzed by a parameter-space Monte Carlo histogram technique to evaluate the effects of an extensive variety of model potentials on folding thermodynamics. Cooperative helical formation and contact energies based on a 5-letter alphabet are found to be insufficient to satisfy calorimetric and other experimental criteria for two-state folding. Such proteinlike behaviors are predicted, however, by models with polypeptide-like local conformational restrictions and environment-dependent hydrogen bonding-like interactions.

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