Determination of amino acid pairs in human haemoglobin α chain sensitive to variants by means of a random approach |
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Authors: | Guang Wu Shaomin Yan |
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Affiliation: | (1) Laboratoire de Toxicocinétique et Pharmacocinétique, Faculté de Pharmacie, Université de la Méditerranée Aix-Marseille II, Marseille, France, FR;(2) Cattedra di Anatomia Patologica, Dipartimento di Ricerche Mediche e Morfologiche, Facoltaà di Medicina e Chirurgia, Universitaà degli Studi di Udine, Udine, Italy, IT;(3) c/o Mr Yan Yongqing, Shenzhen-Dic Ltd 1035 Nanshan Road Nanshan Shenzhen City GuangDong Province, China e-mail: hongguanglishibahao@yahoo.com, CN |
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Abstract: | In this data-based theoretical analysis, we use a random approach to analyse amino acid pairs in human haemoglobin a chain in order to determine which amino acid pairs are more sensitive to 133 positional variants in human haemoglobin a chain. The rationale of this study is based on our hypothesis and previous findings that variance is more likely to occur at randomly unpredictable amino acid pair positions than at randomly predictable positions. This is reasonable to argue as randomly predictable amino acid pairs are less likely to have deliberately evolved, whereas randomly unpredictable amino acid pairs have probably deliberately evolved in connection with protein function. A total of 93.99% of 133 variants occurred at randomly unpredictable amino acid pairs, which accounted for 68.57% of 140 amino acid pairs in human haemoglobin α chain. Thus randomly unpredictable amino acid pairs are more sensitive to variance in human haemoglobin α chain. The results also suggest that the human haemoglobin α chain has a natural tendency towards variants. Received: 16 May 2002 / Accepted: 18 July 2002 |
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Keywords: | Human haemoglobin α chain Mutations Probability Randomness |
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