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肽糖基化的构象影响:糖基化对蛋白质折叠速率影响的一种可能模型。

Conformational influences of glycosylation of a peptide: a possible model for the effect of glycosylation on the rate of protein folding.

作者信息

Live D H, Kumar R A, Beebe X, Danishefsky S J

机构信息

Laboratory for Nucleic Acid and Protein Structure, Sloan-Kettering Institute for Cancer Research, New York, NY 10021, USA.

出版信息

Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12759-61. doi: 10.1073/pnas.93.23.12759.

Abstract

Improved strategies for synthesis make it possible to expand the range of glycopeptides available for detailed conformational studies. The glycopeptide 1 was synthesized using a new solid phase synthesis of carbohydrates and a convergent coupling to peptide followed by deprotection. Its conformational properties were subjected to NMR analysis and compared with a control peptide 2 prepared by conventional solid phase methods. Whereas peptide 2 fails to manifest any appreciable secondary structure, the glycopeptide 1 does show considerable conformational bias suggestive of an equilibrium between an ordered and a random state. The implications of this ordering effect for the larger issue of protein folding are considered.

摘要

改进的合成策略使得扩大可用于详细构象研究的糖肽范围成为可能。糖肽1是通过一种新的碳水化合物固相合成法、与肽的收敛偶联然后脱保护来合成的。对其构象性质进行了核磁共振分析,并与通过传统固相方法制备的对照肽2进行了比较。肽2未能表现出任何明显的二级结构,而糖肽1确实显示出相当大的构象偏向,表明在有序状态和随机状态之间存在平衡。考虑了这种有序效应对于更大的蛋白质折叠问题的影响。

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本文引用的文献

1
Sequence-Specific Peptide-Carbohydrate Interactions in an Asparagine-Linked Glycopeptide.
J Org Chem. 1996 Jun 26;61(13):4198-4199. doi: 10.1021/jo960590c.
3
Structural comparison of a 15 residue peptide from the V3 loop of HIV-1IIIb and an O-glycosylated analogue.
FEBS Lett. 1996 Sep 16;393(2-3):280-6. doi: 10.1016/0014-5793(96)00912-x.
5
Conformational implications of asparagine-linked glycosylation.天冬酰胺连接的糖基化的构象影响。
Proc Natl Acad Sci U S A. 1995 Jan 3;92(1):97-101. doi: 10.1073/pnas.92.1.97.
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Acquisition of three-dimensional structure of proteins.蛋白质三维结构的获取。
Annu Rev Biochem. 1973;42:135-58. doi: 10.1146/annurev.bi.42.070173.001031.

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