title: Statistical mechanics of protein folding by cluster distance geometry.
abstract: This is our second type of model for protein folding where the configurational parameters and the effective potential energy function are chosen in such a way that all conformations are described and the canonical partition function can be evaluated analytically. Structure is described in terms of distances between pairs of sequentially contiguous blocks of eight residues, and all possible conformations are grouped into 71 subsets in terms of bounds on these distances. The energy is taken to be a sum of pairwise interactions between such blocks. The 210 energy parameters were adjusted so that the native folds of 32 small proteins are favored in free energy over the denatured state. We then found 146 proteins having negligible sequence similarity to any of the training proteins, yet the free energy of the respective correct native states were favored over the denatured state.
authors.affiliation: College of Pharmacy, University of Michigan, Ann Arbor, MI 48109-1065, USA. gcrippen@umich.edu
authors.forename: Gordon M
authors.initials: GM
authors.lastname: Crippen
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D016000:Cluster Analysis; D008962:Models, Theoretical; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013223:Statistics as Topic / Q000379:methods*; D013816:Thermodynamics
chemical_list: D000596:Amino Acids; D010455:Peptides; D011506:Proteins