在多肽和蛋白质的结构及功能研究中 ,天冬酰胺 (Asn)备受关注。在 α-螺旋结构的肽链中 ,天冬酰胺往往处于 C-末端 ,通过其侧链形成的氢键限制构象任意改变 ,使螺旋结构稳定 [1]。-CH2 CONH2 侧链还可作为糖肽的键合点 [2 ] ,后者在细胞识别方面起着重要作用。近来又发现天冬酰 Asn is of interest in the structural and functional studies of peptides and proteins. In the α-helical structure of the peptide chain, asparagine often in the C-terminal, through the formation of hydrogen bonds in its side chain to restrict any conformational changes, the helical structure stability [1]. The -CH2 CONH2 side chain also serves as a bonding site for glycopeptides [2], which plays an important role in cell recognition. Asparagine has recently been found