[Factors determining the instability of the conformation of human mutant hemoglobins. A method for evaluating the instability].
A method that allows to estimate the influence of single amino acid substitutions on the stability of proteins with known three-dimensional structure was developed. The role of 20 different physico-chemical properties of amino acids and some characteristics of the three-dimensional structure in the destabilization of protein structure caused by mutations was analyzed. Analysis of 54 proteins led us to reveal the characteristics of the three-dimensional structure. The parameters of the method were calculated on the basis of experimental data for 330 mutant human hemoglobins. The prediction accuracy of the method is on average 81%. The method may be used for the analysis of the total mutational spectra of the proteins and also for the estimation of effects of the single amino acid substitution on the protein structure in gene-engineering experiments.
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006455:Hemoglobins, Abnormal / Q000235:genetics*; D006801:Humans; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation
D006455:Hemoglobins, Abnormal
Faktory, opredeliaiushchie nestabil'nost' prostranstvennoĭ struktury mutantnykh gemoglobinov cheloveka. Metod otsenki nestabil'nosti.