1H NMR STUDIES OF INSULIN ASSIGNMENT OF PHENYLANINE RESONANCES AND THEIR SIDE CHAIN CONFORMATIONS
胰岛素的核磁共振研究——苯丙氨酸共振峰的确定与测链构象

The assignment of the aromatic 1H NMR resonance of three important pheny-lalanine residues B1, B24, B25 in pig zinc-free insulin are established by double resonance techniques, two-dimensional correlated spectroscopy(COSY) and examination of Des-(B23-B30)-insulin(DOI).The side chain conformations of phenylalanines B1, B24, B25 have been studied at different pH. Bigest changes in side chain conformation of Phe B25 occur at high pH.