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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >High-pressure protein crystallography of hen egg-white lysozyme
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High-pressure protein crystallography of hen egg-white lysozyme

机译:高压蛋白质晶体学的母鸡蛋清溶菌酶

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摘要

Crystal structures of hen egg-white lysozyme (HEWL) determined under pressures ranging from ambient pressure to 950?MPa are presented. From 0.1 to 710?MPa, the molecular and internal cavity volumes are monotonically compressed. However, from 710 to 890?MPa the internal cavity volume remains almost constant. Moreover, as the pressure increases to 950?MPa, the tetragonal crystal of HEWL undergoes a phase transition from P43212 to P43. Under high pressure, the crystal structure of the enzyme undergoes several local and global changes accompanied by changes in hydration structure. For example, water molecules penetrate into an internal cavity neighbouring the active site and induce an alternate conformation of one of the catalytic residues, Glu35. These phenomena have not been detected by conventional X-ray crystal structure analysis and might play an important role in the catalytic activity of HEWL.
机译:母鸡蛋清溶菌酶的晶体结构(HEWL)决定从下压力环境压力950 ?0.1到710 ?卷单调压缩。从710年到890年?仍然几乎不变。压力增加到950 ?水晶的HEWL经历从一个阶段过渡P43212 P43。酶的结构经历了几个地方和全球变化伴随着变化水化结构。渗透内部空腔附近活性部位和诱导一个替代构象的催化残基,Glu35。传统的x射线晶体结构分析和催化可能发挥重要作用HEWL的活动。

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