首页> 外文期刊>Journal of Molecular Biology >THE ALPHA-HELIX OF RIBONUCLEASE T-1 AS AN INDEPENDENT STABILITY UNIT - DIRECT COMPARISON OF PEPTIDE AND PROTEIN STABILITY
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THE ALPHA-HELIX OF RIBONUCLEASE T-1 AS AN INDEPENDENT STABILITY UNIT - DIRECT COMPARISON OF PEPTIDE AND PROTEIN STABILITY

机译:核糖核酸酶T-1的α-螺旋作为独立的稳定性单元-肽和蛋白质稳定性的直接比较。

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摘要

Measurements of the change in conformational stability, Delta(Delta G), upon mutation of two acidic residues at the C terminus of the helix of ribonuclease T-1 have recently been reported. Here, we investigate peptides based on the sequence of the helix with the same mutations: Glu28 replaced with Gin, Asp29 replaced with Asn, and the double mutant. In addition, the mutant Lys25 to Gin was studied. Changes in helix content of the peptides with pH confirm the conclusion found in the intact protein, that the charged forms of the acidic residues destabilize the protein by destabilizing the helix. The pH-dependence of the change in conformational free energy for the peptides and mutant proteins show fair correspondence for D29N and the double mutant. The mutants E28Q and K25Q, on the other hand, give striking agreement between the protein and peptide systems. This agreement suggests that the helix of ribonuclease T-1 behaves as an independently stabilized structural unit of the intact protein and that stabilization of the helical form of the peptide is mirrored in the protein. (C) 1996 Academic Press Limited [References: 41]
机译:最近已经报道了在核糖核酸酶T-1的螺旋的C末端的两个酸性残基突变后,构象稳定性的变化Δ(Delta G)的测量。在这里,我们基于具有相同突变的螺旋序列研究肽:Glu28替换为Gin,Asp29替换为Asn,以及双突变。另外,研究了Gin的突变体Lys25。肽的螺旋含量随pH的变化证实了在完整蛋白中发现的结论,即酸性残基的带电形式通过使螺旋不稳定而使蛋白质不稳定。肽和突变蛋白构象自由能变化的pH依赖性显示D29N和双突变体具有相当的对应性。另一方面,突变体E28Q和K25Q在蛋白质和肽系统之间达成了惊人的协议。该协议表明核糖核酸酶T-1的螺旋表现为完整蛋白的独立稳定的结构单元,并且该肽的螺旋形式的稳定反映在该蛋白中。 (C)1996 Academic Press Limited [参考号:41]

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