Energetic components of cooperative protein folding.
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 polypeptidelike local conformational restrictions and environment-dependent hydrogen-bondinglike interactions.
Kaya
H
H
Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada M5S 1A8.
Chan
H S
HS
D002151:Calorimetry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D009010:Monte Carlo Method; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013696:Temperature; D013816:Thermodynamics
D011506:Proteins