Live D H, Kumar R A, Beebe X, Danishefsky S J
Laboratory for Nucleic Acid and Protein Structure, Sloan-Kettering Institute for Cancer Research, New York, NY 10021, USA.
Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12759-61. doi: 10.1073/pnas.93.23.12759.
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.
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。
