Journal article

SOLUTION STRUCTURE OF THE B-CHAIN OF INSULIN AS DETERMINED BY H-1-NMR SPECTROSCOPY - COMPARISON WITH THE CRYSTAL-STRUCTURE OF THE INSULIN HEXAMER AND WITH THE SOLUTION STRUCTURE OF THE INSULIN MONOMER

B HAWKINS, K CROSS, D CRAIK

INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH | MUNKSGAARD INT PUBL LTD | Published : 1995

Abstract

The solution structure of the isolated B-chain of bovine insulin has been determined by 1H NMR spectroscopy combined with simulated annealing calculations. Complete sequence-specific assignments for the proton resonances are reported together with a set of 309 NOEs used in the structure calculations. Chemical-shift variations from random coil values provide support for the existence of helical regions in the polypeptide chain, as do a characteristic series of d alpha beta(i, i + 3) NOEs from residues B8 to B17. While there is some evidence for a limited degree of conformational averaging over the helical region, in general the helix is relatively well defined and corresponds closely to the h..

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University of Melbourne Researchers