Statistical mechanical treatment of protein conformation. I. Conformational properties of amino acids in proteins.
A statistical mechanical (one-dimensional Ising model) treatment, based on the dominance of short-range interactions, is developed in this series of papers; it is intended as an improvement over empirical prediction schemes for obtaining approximate initial conformations of proteins (to be used to try to deduce the native conformation by subsequent energy minimization). In the present paper, the statistical weights for a two-state model (alpha-helical and other conformations) and for a three-state model (alpha-helical, extended, and other conformations) are evaluated from x-ray data on 16 native proteins. The method for evaluating the statistical weights is presented. Asymmetric alpha-helical nucleation parameters are also evaluated for the 20 naturally occurring amino acids. On the basis of these statistical weights, the conformational properties of the twenty naturally occurring amino acids are discussed. The statistical weights evaluated from x-ray data are also discussed in comparison with experimental results on the helix--coil transition in polyamino acids in solution. The predominant role of short-range interactions, and some possible long-range effects in determining the statistical weights, are discussed in conjunction with the mechanism of protein folding.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D006860:Hydrogen Bonding; D008433:Mathematics; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000596:Amino Acids