The Study of Higher Order Structure of Biologically Active Macromolecules by Means of High-Resolution NMR

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The biologically active macromolecules take a variety of higher-order structures according to the circumstances. This research project is being aimed to establish the higher-order structure of biologically active macromolecules in solutions and in solid states by means of high-resolution NMR spectroscopy. This project was carried out for three years from 1987 to 1989 on the three main research subjects,(1)glycoproteins,(2)enzymes and artificial enzymes, and (3)protein models. In the first subject, conformations and interaction between the sugar and peptide moieties were investigated for several O-glycosylated threonine containing oligopeptides which were models of antifreeze glycoprotein(Chujo & Inoue). In the second subject, enzyme-like activity of artificial enzyme, that is, histamine-modified cyclodextrin(Toda), and the role of branch in the molecular-inclusion function of branched cyclodextrins(Yamamoto) were investigated on the basis of structural information obtained from NMR. A hybrid protein between metapyrocatechase and binding protein A was produced by recombinant DNA techniques,and applicability of expressed fusion protein for enzyme immunoassay was investigated(Aizawa). In the last subject, the role of side-chain/side-chain interaction in the stabilization of higher-order structure of poly (gamma-benzyl glutamate)(Abe) and the effect of counterions on the structure of polyglutamate in solution(Komiyama) were investigated. The structure of potassium salt of carboxylic polyether, which is the model of natural ionophore,was studied in aqueous solution(Nakahama). The higher order structures or polypeptides and tropomyosine were also investigated in the solid state as well as in solution(Ando).