[Approach to a priori calculation of stable forms of proteins].
Basing on semi-empirical conformational analysis an approach is suggested to the calculation of stable forms of protein molecules. The physical model proposed implies: 1) that the most stable conformation of a protein corresponds to its native state, 2) that interactions of three types which determine conformational states of every residue should be treated separately, 3) that the protein molecule is highly compact structure with interactions of different kinds compensating each other, 4) that interactions of the three types contribute differently to the formation of the spatial structure of a globule. These interactions are: 1) those of peptide chain atoms within a particular residue, 2) interactions of the residue with the nearest neighbours in the chain, 3) interactions with residues which are remote in the chain but close in the globule. The approach proposed allows to separate the conformational analysis of a protein into a number of subsequently solved problems. The scheme of the calculation of stable forms is presented.
D004355:Drug Stability; D008956:Models, Chemical; D011487:Protein Conformation; D011506:Proteins
D011506:Proteins
Podkhod k apriornomu raschetu stabil'nykh konformatsiĭ belkovykh molekul