Article
Hemoglobin Porto Alegre forms a tetramer of tetramers superstructure.
Protein science : a publication of the Protein Society - 1 Jan 2002
Baudin-Creuza Véronique, Fablet Christophe, Zal Franck, Green Brian N, Promé Danielle, Marden Michael C, Pagnier Josée, Wajcman Henri
Abstract excerpt
The effects of the mutation beta9(A6)Ser --> Cys on the interactions between the human hemoglobin molecules were investigated, and comparisons were made with other variants having an additional cysteine residue. In hemoglobin Porto Alegre (PA), the beta9 mutation induces polymerization by forming...
Topics
- Chromatography, Gel
- Cysteine
- Dimerization
- Disulfides
- Hemoglobins, Abnormal
- Humans
- Kinetics
- Microscopy, Electron
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation