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- ISSN: 0929-8665
- E-ISSN: 1875-5305
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Building Quantitative Relationship Between Changed Sequence and Changed Oxygen Affinity in Human Hemoglobin β-Chain
- Source: Protein and Peptide Letters, Volume 15, Issue 4, May 2008, p. 341 - 345
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- 01 May 2008
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.
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