Yoshida M, Nakai T, Fukuhara K, Saitoh S, Yoshikawa W, Kobayashi Y, Nakamura H
Protein Engineering Research Institute, Osaka.
J Biochem. 1990 Aug;108(2):158-65. doi: 10.1093/oxfordjournals.jbchem.a123175.
The three-dimensional structure of an alpha-amylase inhibitor, HAIM, composed of 78 amino acids, was analyzed by two-dimensional NMR techniques. Sequence-specific assignments were made for the amino acid residues from Ile-6 to Cys-72. Distance geometry analysis of the interresidue NOEs revealed that the HAIM molecule consists of two beta-sheets, as is the case in a homologous alpha-amylase inhibitor, Tendamistat, though one of its beta-strands is much shorter than that of Tendamistat. The combination of molecular modeling from Tendamistat and distance geometry analysis was confirmed to be useful for our purpose.
采用二维核磁共振技术分析了由78个氨基酸组成的α-淀粉酶抑制剂HAIM的三维结构。对从Ile-6到Cys-72的氨基酸残基进行了序列特异性归属。对残基间NOE的距离几何分析表明，HAIM分子由两个β-折叠组成，这与同源α-淀粉酶抑制剂Tendamistat的情况相同，不过其β-链之一比Tendamistat的β-链短得多。结果证实，结合Tendamistat的分子建模和距离几何分析对我们的研究目的很有用。
