Abstract

244 point mutations have been recorded in human hemoglobin β-chain, of which some change the oxygen affinity of human hemoglobin β-chain. We use the amino-acid distribution probability to quantify these mutations, and use the cross-impact analysis with Bayes law to determine the probability that changes the oxygen affinity of human hemoglobin β-chain under mutations.

Keywords: Amino acid, Bayes' law, cross-impact analysis, distribution probability, hemoglobin, oxygen affinity