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首页> 外文期刊>Biochemistry >Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants.
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Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants.

机译：氢键对人类溶菌酶构象稳定性的贡献：六个Ser-> Ala突变体的量热法和X射线分析。

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    摘要

    To further examine the contribution of hydrogen bonds to the conformational stability of the human lysozyme, six Ser to Ala mutants were constructed. The thermodynamic parameters for denaturation of these six Ser mutant proteins were investigated by differential scanning calorimetry (DSC), and the crystal structures were determined by X-ray analysis. The denaturation Gibbs energy (DeltaG) of the Ser mutant proteins was changed from 2.0 to -5.7 kJ/mol, compared to that of the wild-type protein. With an analysis in which some factors that affected the stability due to mutation were considered, the contribution of hydrogen bonds to the stability (Delta DeltaGHB) was extracted on the basis of the structures of the mutant proteins. The results showed that hydrogen bonds between protein atoms and between a protein atom and a water bound with the protein molecule favorably contribute to the protein stability. The net contribution of one intramolecular hydrogen bond to protein stability (DeltaGHB) was 8.9 +/- 2.6 kJ/mol on average. However, the contribution to the protein stability of hydrogen bonds between a protein atom and a bound water molecule was smaller than that for a bond between protein atoms.
    机译：为了进一步检查氢键对人溶菌酶构象稳定性的贡献，构建了六个Ser到Ala突变体。通过差示扫描量热法（DSC）研究了这六个Ser突变蛋白的变性的热力学参数，并通过X射线分析确定了晶体结构。与野生型蛋白相比，Ser突变蛋白的变性吉布斯能量（DeltaG）从2.0更改为-5.7 kJ / mol。通过分析，其中考虑了一些由于突变影响稳定性的因素，基于突变蛋白的结构提取了氢键对稳定性的贡献（Delta DeltaGHB）。结果表明，蛋白质原子之间以及与蛋白质分子结合的蛋白质原子与水之间的氢键有利于蛋白质稳定性。一个分子内氢键对蛋白质稳定性（DeltaGHB）的净贡献平均为8.9 +/- 2.6 kJ / mol。然而，对蛋白质原子和结合的水分子之间的氢键的蛋白质稳定性的贡献小于对蛋白质原子之间的键的氢稳定性的贡献。

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