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

Guang      Wu; Shaomin      Yan

doi:10.2174/092986608784246498

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

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Protein & Peptide Letters

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

Volume: 15 Issue: 4

Author(s): Guang Wu and Shaomin Yan

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

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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Wu Guang and Yan Shaomin, Building Quantitative Relationship Between Changed Sequence and Changed Oxygen Affinity in Human Hemoglobin β-Chain, Protein & Peptide Letters 2008; 15 (4) . https://dx.doi.org/10.2174/092986608784246498