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Three-dimensional structure of an alpha-amylase inhibitor HAIM as determined by nuclear magnetic resonance methods
M Yoshida1, T Nakai, K Fukuhara
1Protein Engineering Research Institute, Osaka.
Journal of Biochemistry
|August 1, 1990
Abstract:
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.