Effective potentials for Folding Proteins

Abstract

A coarse-grained off-lattice model that is not biased in any way to the native state is proposed to fold proteins. To predict the native structure in a reasonable time, the model has included the essential effects of water in an effective potential. Two new ingredients, the dipole-dipole interaction and the local hydrophobic interaction, are introduced and are shown to be as crucial as the hydrogen bonding. The model allows successful folding of the wild-type sequence of protein G and may have provided important hints to the study of protein folding.

4 pages, 4 figures, to appear in Physical Review Letters

References in corpus (4)

• Protein folding mediated by solvation: water expelling and formation of the hydrophobic core occurs after the structure collapse
• How native state topology affects the folding of Dihydrofolate Reductase and Interleukin-1beta
• Linking Rates of Folding in Lattice Models of Proteins with Underlying Thermodynamic Characteristics
• Origin of Native Driving Force in Protein Folding

Cited by in corpus (4)

• A solvable model of the genesis of amino-acid sequences via coupled dynamics of folding and slow genetic variation
• Folding a protein with equal probability of being helix or hairpin
• Monte Carlo simulations of proteins in cages: influence of confinement on the stability of intermediate states
• Hydrogen bond models for the simulation of protein folding and aggregation