Analysis of the factors and implications of an empirical method for estimating the stability of mutant human haemoglobins.
An empirical method for estimating the effects of single amino acid substitutions on structural stability of proteins with known spatial structure is developed. Twenty physical and chemical properties of amino acids and characteristics of protein tertiary structure were analysed to determine those most involved in producing instability. We employed data on 330 mutant variants of the alpha- and beta-subunits of human haemoglobin in choice of the parameters of the method developed which yielded a 81% of prediction accuracy of stability estimates for human mutant haemoglobins.
D000595:Amino Acid Sequence; D005998:Glycine; D006454:Hemoglobins / Q000235:genetics*; D006801:Humans; D046911:Macromolecular Substances; D009010:Monte Carlo Method; D009154:Mutation; D011336:Probability; D011487:Protein Conformation; D012694:Serine; D014364:Tryptophan; D014443:Tyrosine
D006454:Hemoglobins; D046911:Macromolecular Substances; D014443:Tyrosine; D012694:Serine; D014364:Tryptophan; D005998:Glycine