Conformational influences of glycosylation of a peptide: A possible model for the effect of glycosylation on the rate of protein folding
Conformational influences of glycosylation of a peptide: A possible model for the effect of glycosylation on the rate of protein folding
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DOI：
10.1073/pnas.93.23.12759
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发表时间：
1996-11-12
影响因子：
11.1
通讯作者：
Danishefsky, SJ
中科院分区：
文献类型：
--
作者：
Live, DH;Kumar, RA;Danishefsky, SJ
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 I 是使用碳水化合物的新固相合成方法以及与肽的聚合偶联然后脱保护来合成的。对其构象性质进行NMR分析，并与常规固相方法制备的对照肽2进行比较。虽然肽 2 未能表现出任何明显的二级结构，但糖肽 1 确实显示出相当大的构象偏差，表明有序状态和随机状态之间的平衡。考虑了这种排序效应对蛋白质折叠这一更大问题的影响。
Improved strategies for synthesis make it possible to expand the range of glycopeptides available for detailed conformational studies. The glycopeptide I 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.