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A sequential model of nucleation-dependent protein folding: kinetic studies of ribonuclease A.

作者信息

Tsong T Y, Baldwin R L

出版信息

J Mol Biol. 1972 Feb 14;63(3):453-69. doi: 10.1016/0022-2836(72)90440-8.

DOI:10.1016/0022-2836(72)90440-8
PMID:5014928
Abstract
摘要

相似文献

1
A sequential model of nucleation-dependent protein folding: kinetic studies of ribonuclease A.
J Mol Biol. 1972 Feb 14;63(3):453-69. doi: 10.1016/0022-2836(72)90440-8.
2
A sequential model of nucleation-dependent protein folding: kinetic studies of ribonuclease A. Analysis of the steady-state approximation for the sequential model.一种依赖成核的蛋白质折叠的序列模型：核糖核酸酶A的动力学研究。对序列模型的稳态近似的分析。
J Mol Biol. 1972 Feb 14;63(3):469-75. doi: 10.1016/0022-2836(72)90441-x.
3
Test of the extended two-state model for the kinetic intermediates observed in the folding transition of ribonuclease A.对核糖核酸酶A折叠转变过程中观察到的动力学中间体的扩展两态模型的测试。
J Mol Biol. 1978 Jan 25;118(3):317-30. doi: 10.1016/0022-2836(78)90231-0.
4
Thermodynamics of protein denaturation. Effect of pressu on the denaturation of ribonuclease A.蛋白质变性的热力学。压力对核糖核酸酶A变性的影响。
Biochemistry. 1970 Feb 17;9(4):1038-47. doi: 10.1021/bi00806a045.
5
Calorimetric investigation of ribonuclease thermal denaturation.核糖核酸酶热变性的量热研究。
Int J Pept Protein Res. 1973;5(4):229-37. doi: 10.1111/j.1399-3011.1973.tb03457.x.
6
Recombination of S-peptide with S-protein during folding of ribonuclease S. I. Folding pathways of the slow-folding and fast-folding classes of unfolded S-protein.
J Mol Biol. 1979 Nov 25;135(1):231-44. doi: 10.1016/0022-2836(79)90349-8.
7
Kinetic and equilibrium studies on the interaction of ribonuclease A and 2'1-deoxyuridine 3'-phosphate.核糖核酸酶A与2'-脱氧尿苷3'-磷酸相互作用的动力学及平衡研究
Biochemistry. 1971 May 25;10(11):2156-62. doi: 10.1021/bi00787a031.
8
Pathways of folding of reduced bovine pancreatic ribonuclease.还原型牛胰核糖核酸酶的折叠途径
Biochemistry. 1974 Aug 13;13(17):3421-31. doi: 10.1021/bi00714a001.
9
pH dependence of the thermal unfolding of ribonuclease A.
Biochemistry. 1972 Feb 29;11(5):879-83. doi: 10.1021/bi00755a029.
10
The state of the tyrosines of bovine pancreatic ribonuclease in urea-sulfate solutions.牛胰核糖核酸酶酪氨酸在尿素 - 硫酸盐溶液中的状态
Biochemistry. 1969 Nov;8(11):4550-9. doi: 10.1021/bi00839a048.

引用本文的文献

1
Selection for cooperativity causes epistasis predominately between native contacts and enables epistasis-based structure reconstruction.选择协同作用主要导致天然接触之间的上位性，并使基于上位性的结构重建成为可能。
Proc Natl Acad Sci U S A. 2021 Apr 20;118(16). doi: 10.1073/pnas.2010057118.
2
Evolution of a protein folding nucleus.蛋白质折叠核心的进化
Protein Sci. 2016 Jul;25(7):1227-40. doi: 10.1002/pro.2848. Epub 2015 Dec 10.
3
Structural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics.
通过荧光能量转移动力学揭示的细胞色素c'折叠中间体的结构特征
Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14778-82. doi: 10.1073/pnas.192574099. Epub 2002 Oct 29.
4
From discrete protein kinetics to continuous Brownian dynamics: a new perspective.从离散蛋白质动力学到连续布朗动力学：一种新视角。
Protein Sci. 2002 Jan;11(1):1-5. doi: 10.1110/ps.18902.
5
The calorimetric criterion for a two-state process revisited.重新审视双态过程的量热判据。
Protein Sci. 1999 May;8(5):1064-74. doi: 10.1110/ps.8.5.1064.
6
Protein folding: matching theory and experiment.蛋白质折叠：理论与实验的匹配
Biophys J. 1998 Jul;75(1):428-34. doi: 10.1016/S0006-3495(98)77530-7.
7
Comparison of kinetics of formation of helices and hydrophobic core during the folding of staphylococcal nuclease from acid.葡萄球菌核酸酶从酸性条件下折叠过程中螺旋和疏水核心形成动力学的比较。
Biophys J. 1994 Jan;66(1):40-5. doi: 10.1016/S0006-3495(94)80771-4.
8
Both the fast and slow refolding reactions of ribonuclease A yield native enzyme.核糖核酸酶A的快速和慢速重折叠反应均产生天然酶。
Proc Natl Acad Sci U S A. 1973 Dec;70(12):3347-51. doi: 10.1073/pnas.70.12.3347.
9
Nuclear magnetic resonance study of the thermal denaturation of ribonuclease A: implications for multistate behavior at low pH.核糖核酸酶A热变性的核磁共振研究：低pH下多态行为的意义。
Proc Natl Acad Sci U S A. 1973 Mar;70(3):914-8. doi: 10.1073/pnas.70.3.914.
10
Properties of the refolding and unfolding reactions of ribonuclease A.核糖核酸酶A复性与变性反应的特性
Proc Natl Acad Sci U S A. 1972 Jul;69(7):1809-12. doi: 10.1073/pnas.69.7.1809.