Article
A new B-chain mutant of insulin: comparison with the insulin crystal structure and role of sulfonate groups in the B-chain structure.
The journal of peptide research : official journal of the American Peptide Society - 1 Jul 2002
Dupradeau F-Y, Richard T, Le Flem G, Oulyadi H, Prigent Y, Monti J-P
Abstract excerpt
The solution structure of a new B-chain mutant of bovine insulin, in which the cysteines B7 and B19 are replaced by two serines, has been determined by circular dichroism, 2D-NMR and molecular modeling. This structure is compared with that of the oxidized B-chain of bovine insulin [Hawkins et al. (1995) Int. J. Peptide Protein Res.46, 424-433]. Circular dichroism spectroscopy showed in particular that a higher...
Topics
- Amino Acid Sequence
- Animals
- Cattle
- Circular Dichroism
- Insulin
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Folding
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Sulfonic Acids