三氟乙醇对核糖核酸酶T1螺旋肽中螺旋倾向和静电相互作用的影响。
Trifluoroethanol effects on helix propensity and electrostatic interactions in the helical peptide from ribonuclease T1.
作者信息
Myers J K, Pace C N, Scholtz J M
机构信息
Department of Medical Biochemistry and Genetics, Texas A&M University, College Station 77843, USA.
出版信息
Protein Sci. 1998 Feb;7(2):383-8. doi: 10.1002/pro.5560070219.
Abstract
Trifluoroethanol (TFE) is often used to increase the helicity of peptides to make them usable as models of helices in proteins. We have measured helix propensities for all 20 amino acids in water and two concentrations of trifluoroethanol, 15 and 40% (v/v) using, as a model system, a peptide derived from the sequence of the alpha-helix of ribonuclease T1. There are three main conclusions from our studies. (1) TFE alters electrostatic interactions in the ribonuclease T1 helical peptide such that the dependence of the helical content on pH is lost in 40% TFE. (2) Helix propensities measured in 15% TFE correlate well with propensities measured in water, however, the correlation with propensities measured in 40% TFE is significantly worse. (3) Propensities measured in alanine-based peptides and the ribonuclease T1 peptide in TFE show very poor agreement, revealing that TFE greatly increases the effect of sequence context.
摘要
三氟乙醇（TFE）常用于增加肽的螺旋度，使其可用作蛋白质中螺旋结构的模型。我们以核糖核酸酶T1的α螺旋序列衍生的肽为模型系统，测量了20种氨基酸在水中以及两种浓度（15%和40%，v/v）的三氟乙醇中的螺旋倾向。我们的研究有三个主要结论。（1）TFE改变了核糖核酸酶T1螺旋肽中的静电相互作用，以至于在40%的TFE中，螺旋含量对pH的依赖性消失。（2）在15%的TFE中测得的螺旋倾向与在水中测得的倾向相关性良好，然而，与在40%的TFE中测得的倾向的相关性明显较差。（3）在基于丙氨酸的肽和TFE中的核糖核酸酶T1肽中测得的倾向显示出非常差的一致性，这表明TFE极大地增加了序列背景的影响。
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本文引用的文献
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Helix propensities are identical in proteins and peptides.螺旋倾向性在蛋白质和肽中是相同的。
Biochemistry. 1997 Sep 9;36(36):10923-9. doi: 10.1021/bi9707180.
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Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water.三氟乙醇诱导螺旋形成的机制：从三氟乙醇/水混合物外推肽在水中螺旋形成特性的框架。
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