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首页> 外文期刊>International journal of bioinformatics research and applications >Analysis of oxygen affinity in aquatic amphibian; homology modelling of the major haemoglobin component HbA1 from the African clawed frog (Xenopus laevis, Anura).
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Analysis of oxygen affinity in aquatic amphibian; homology modelling of the major haemoglobin component HbA1 from the African clawed frog (Xenopus laevis, Anura).

机译:分析水生两栖动物中的氧亲和力;非洲爪蛙(Xenopus laevis,Anura)的主要血红蛋白成分HbA1的同源性建模。

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摘要

The homology model of major haemoglobin component HbA1 of the African Clawed Frog was predicted using the pigeon (Columba livia) haemoglobin as a template. The model was built with the help of MODELLER9v8. The models were evaluated with ProSA and PROCHECK. In X. laevis Gln38α is unable to form a hydrogen bond with β97His or β99Asp, which is responsible for the increase in oxygen affinity of the Xenopus HbA1. The hydrogen bond between α34Thr and β124Pro, which stabilises the deoxy state of the haemoglobin, was absent in X. laevis. Hence it is predicted that the HbA1 component of X. laevis has higher oxygen affinity.
机译:以鸽子(Columba livia)血红蛋白为模板,预测了非洲爪蛙主要血红蛋白成分HbA1的同源性模型。该模型是在MODELLER9v8的帮助下构建的。使用ProSA和PROCHECK对模型进行了评估。在X. laevis中,Gln38α无法与β97His或β99Asp形成氢键,这导致非洲爪蟾HbA1的氧亲和力增加。 X. laevis中缺少稳定血红蛋白脱氧状态的α34Thr和β124Pro之间的氢键。因此,据预测,X.laevis的HbA1组分具有更高的氧亲和力。

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