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Building Quantitative Relationship Between Changed Sequence and Changed Oxygen Affinity in Human Hemoglobin β-Chain

[ Vol. 15 , Issue. 4 ]


Guang Wu and Shaomin Yan   Pages 341 - 345 ( 5 )


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.


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


Computational Mutation Project, DreamSciTech Consulting, 301, Building 12, Nanyou A-zone,Jiannan Road, Shenzhen, Guangdong Province CN-518054, China.

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