Building Quantitative Relationship Between Changed Sequence and Changed Oxygen Affinity in Human Hemoglobin β-Chain
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.
Document Type: Research Article
Publication date: 2008-05-01
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