Article
Site-directed mutagenesis in hemoglobin: functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37 beta and 145 beta mutations.
Biochemistry - 31 Mar 1992
Ishimori K, Imai K, Miyazaki G, Kitagawa T, Wada Y, Morimoto H, Morishima I
Abstract excerpt
In order to clarify the functional and structural role of intra- and intersubunit hydrogen bonds in human hemoglobin (Hb A), we prepared two artificial beta chain mutant hemoglobins by site-directed mutagenesis. The mutant Hb Phe-37 beta, in which Trp-37 beta is replaced by Phe to remove the intersubunit hydrogen bond between Asp-94 alpha and Trp-37 beta at the alpha 1-beta 2 interface in deoxy Hb A, showed a...
Topics
- Amino Acid Sequence
- Aspartic Acid
- Hemoglobin A
- Humans
- Hydrogen Bonding
- Magnetic Resonance Spectroscopy
- Mutagenesis, Site-Directed
- Mutation
- Oxygen
- Protein Conformation