Article
Structural and dynamic properties of the homodimeric hemoglobin from Scapharca inaequivalvis Thr-72-->Ile mutant: molecular dynamics simulation, low temperature visible absorption spectroscopy, and resonance Raman spectroscopy studies.
Biophysical journal - 1 Nov 1998
Falconi M, Desideri A, Cupane A, Leone M, Ciccotti G, Peterson E S, Friedman J M, Gambacurta A, Ascoli F
Abstract excerpt
Molecular dynamics simulations, low temperature visible absorption spectroscopy, and resonance Raman spectroscopy have been performed on a mutant of the Scapharca inaequivalvis homodimeric hemoglobin, where residue threonine 72, at the subunit interface, has been substituted by isoleucine. Molecu...
Topics
- Animals
- Carbon Monoxide
- Dimerization
- Heme
- Hemoglobins
- Mollusca
- Mutation
- Protein Binding
- Spectrophotometry
- Spectrum Analysis, Raman
- Temperature
- Water