Article
1H NMR spectrum of the native human insulin monomer. Evidence for conformational differences between the monomer and aggregated forms.
The Journal of biological chemistry - 5 Apr 1990
Roy M, Lee R W, Brange J, Dunn M F
Abstract excerpt
The effects of high dilution on the 1H Fourier transform NMR spectrum of native human insulin at pH* 8.0 and 9.3 have been examined at 500 MHz resolution. The dependence of the spectrum on concentration and comparison with the spectrum of a biologically highly potent monomeric insulin mutant (SerB9----Asp) establish that at 36 microM (pH* 9.3) or 18 microM (pH* 8) and no added buffer or salts, human insulin is...
Topics
- Aspartic Acid
- Circular Dichroism
- Fourier Analysis
- Humans
- Hydrogen-Ion Concentration
- Insulin
- Macromolecular Substances
- Magnetic Resonance Spectroscopy
- Molecular Conformation
- Mutation
- Serine