折叠蛋白质氢交换模型。II。
Models for hydrogen exchange from folded proteins. II.
作者信息
Ellis L M
出版信息
Biophys J. 1978 Jul;23(1):79-87. doi: 10.1016/S0006-3495(78)85434-4.
Abstract
The kinetics of hydrogen exchange from folded proteins can be molded as a function of two continuous distributions of rate constants, kcx and kn, representing exchange from the folded and unfolded conformations, respectively. This model can account for the temperature dependence of soybean trypsin inhibitor at pH 3 and pH 6.5. The physical significance of this model, especially the shape and breadth of the kn distribution, are discussed.
摘要
折叠蛋白质中氢交换的动力学可以被构建为速率常数kcx和kn两个连续分布的函数，分别代表折叠态和非折叠态构象的交换。该模型可以解释大豆胰蛋白酶抑制剂在pH 3和pH 6.5时的温度依赖性。本文讨论了该模型的物理意义，特别是kn分布的形状和宽度。
相似文献
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Models for hydrogen exchange from folded proteins. II.折叠蛋白质氢交换模型。II。
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Hydrogen exchange and the dynamic structure of proteins.氢交换与蛋白质的动态结构
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本文引用的文献
1
On the kinetics of structural transition I of some pancreatic proteins.关于某些胰腺蛋白结构转变I的动力学
FEBS Lett. 1969 Apr;3(1):60-64. doi: 10.1016/0014-5793(69)80097-9.
2
Kinetic class analysis of hydrogen-exchange data.氢交换数据的动力学类别分析。
Biochemistry. 1970 Mar 31;9(7):1547-53. doi: 10.1021/bi00809a011.
3
Restrictions of sequence on the thickness of globular protein molecules.球状蛋白质分子厚度的序列限制。
Proc Natl Acad Sci U S A. 1971 Dec;68(12):2928-31. doi: 10.1073/pnas.68.12.2928.
4
Primary structure effects on peptide group hydrogen exchange.肽基氢交换的一级结构效应
Biochemistry. 1972 Jan 18;11(2):150-8. doi: 10.1021/bi00752a003.
5
Hydrogen exchange.氢交换
Annu Rev Biochem. 1972;41:903-24. doi: 10.1146/annurev.bi.41.070172.004351.
6
Measurement of structural and free energy changes in hemoglobin by hydrogen exchange methods.通过氢交换法测量血红蛋白的结构和自由能变化。
Ann N Y Acad Sci. 1975 Apr 15;244:10-27. doi: 10.1111/j.1749-6632.1975.tb41518.x.
7
Hydrogen-tritium exchange kinetics of soybean trypsin inhibitor (Kunitz). Solvent accessibility in the folded conformation.大豆胰蛋白酶抑制剂（Kunitz）的氢-氚交换动力学。折叠构象中的溶剂可及性。
Biochemistry. 1975 Jul 29;14(15):3413-9. doi: 10.1021/bi00686a019.
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