Recombination of S-peptide with S-protein during folding of ribonuclease S. II. Kinetic characterization of a stable folding intermediate shown by S-protein at pH 1.7.

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作者信息

Labhardt A M, Baldwin R L

出版信息

J Mol Biol. 1979 Nov 25;135(1):245-54. doi: 10.1016/0022-2836(79)90350-4.

DOI:10.1016/0022-2836(79)90350-4

PMID:43399

Abstract

摘要

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Recombination of S-peptide with S-protein during folding of ribonuclease S. II. Kinetic characterization of a stable folding intermediate shown by S-protein at pH 1.7.

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Stabilization of the ribonuclease S-peptide alpha-helix by trifluoroethanol.用三氟乙醇稳定核糖核酸酶S肽的α螺旋结构

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引用本文的文献

Folding and association of proteins.蛋白质的折叠与缔合

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Hydrophobic basis of packing in globular proteins.球状蛋白质中堆积的疏水基础。

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Kinetic circular dichroism shows that the S-peptide alpha-helix of ribonuclease S unfolds fast and refolds slowly.动力学圆二色性表明，核糖核酸酶S的S-肽α-螺旋快速展开并缓慢重新折叠。

Proc Natl Acad Sci U S A. 1984 Dec;81(24):7674-8. doi: 10.1073/pnas.81.24.7674.

Is there a single pathway for the folding of a polypeptide chain?多肽链的折叠有单一途径吗？

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Protein fragments as probes in the study of protein folding mechanisms: differential effects of dihydrofolate reductase fragments on the refolding of the intact protein.蛋白质片段作为研究蛋白质折叠机制的探针：二氢叶酸还原酶片段对完整蛋白质重折叠的不同影响。

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