Dill K, Carter R D, Lacombe J M, Pavia A A
Carbohydr Res. 1986 Sep 1;152:217-28. doi: 10.1016/s0008-6215(00)90301-x.
Natural-abundance 13C nuclear magnetic resonance (13C-n.m.r.) was used to study the effect of monoglycosylation on the structure and dynamics of a pentapeptide related to the N-terminus of glycophorin AM. The results of this study indicate that a single point of glycosylation, on the pentapeptide, can significantly affect its structure. Moreover, glycosylation of this pentapeptide also affects its dynamic motion in solution. This study further defines the role that the carbohydrate residue plays in determining the structure about the N-terminus of glycophorin AM.
利用天然丰度的13C核磁共振（13C - n.m.r.）研究了单糖基化对与血型糖蛋白AM N端相关的五肽结构和动力学的影响。该研究结果表明，五肽上的单个糖基化位点可显著影响其结构。此外，该五肽的糖基化还会影响其在溶液中的动态运动。这项研究进一步明确了碳水化合物残基在确定血型糖蛋白AM N端结构中所起的作用。
