Article
A myoglobin variant with a polar substitution in a conserved hydrophobic cluster in the heme binding pocket.
Biochimica et biophysica acta - 15 Aug 1997
Maurus R, Overall C M, Bogumil R, Luo Y, Mauk A G, Smith M, Brayer G D
Abstract excerpt
Well-ordered internal amino acids can contribute significantly to the stability of proteins. To investigate the importance of the hydrophobic packing interface between helices G and H in the proximal heme pocket of horse heart myoglobin, the highly conserved amino acid, Leu104, was substituted wi...
Topics
- Animals
- Asparagine
- Binding Sites
- Circular Dichroism
- Electron Spin Resonance Spectroscopy
- Escherichia coli
- Heme
- Horses
- Leucine
- Molecular Sequence Data
- Mutation
- Myocardium
- Myoglobin
- Nucleic Acid Conformation
- Protein Conformation
- Protein Structure, Secondary
- Recombinant Proteins
- Spectrophotometry