Building quantitative relationship between changed sequence and changed oxygen affinity in human hemoglobin beta-chain.
244 point mutations have been recorded in human hemoglobin beta-chain, of which some change the oxygen affinity of human hemoglobin beta-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 beta-chain under mutations.
Wu
Guang
G
Computational Mutation Project, DreamSciTech Consulting, 301, Building 12, Nanyou A-zone, Jiannan Road, Shenzhen, Guangdong Province CN-518054, China. hongguanglishibahao@yahoo.com
Yan
Shaomin
S
D001499:Bayes Theorem; D005914:Globins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D010100:Oxygen / Q000378:metabolism*; D017354:Point Mutation; D013329:Structure-Activity Relationship
D006454:Hemoglobins; D005914:Globins; D010100:Oxygen