QUANTITATIVE APPROACH TO CONFORMATIONS OF PROTEINS

A quantitative conformational theory of proteins is developed that enables one to predict the native structure of a protein from its amino acid sequence. The theory is based on the following principles: (1) the spatial structure and conformational properties of a protein are predetermined by its amino acid sequence; (2) the native conformation of a protein corresponds to the free energy minimum; (3) all interactions within a protein molecule are specified as short‐, mediumy‐, and long‐range types, interactions of different types being consistent with each other. The role of the short‐, medium‐, and long‐range interactions in the spatial organization of a protein globule is discussed, and a step‐by‐step analysis of amino acid sequences with gradually increasing lengths is presented. The proposed theory is based on a semiempirical computational method that involves quantitative evaluation of all pairwise atomic interactions within a protein molecule in an aqueous medium. Examples illustrating the suggested approach are presented. Copyright © 1979 John Wiley & Sons, Inc.