Article
Quaternary structure sensitive tyrosine interactions in hemoglobin: a UV resonance Raman study of the double mutant rHb (beta99Asp-->Asn, alpha42Tyr-->Asp).
Biochemistry - 20 May 1997
Huang S, Peterson E S, Ho C, Friedman J M
Abstract excerpt
Two interactions involving tyrosines have been implicated in the communication pathway that links ligand binding to quaternary state changes in hemoglobin. Tyr alpha(1)42 stabilizes the alpha1beta2 T state interface through the formation of a hydrogen bond to Asp beta(2)99. The side chains of the...
Topics
- Allosteric Regulation
- Carboxyhemoglobin
- Hemoglobins
- Humans
- Hydrogen Bonding
- Mass Spectrometry
- Mutation
- Protein Conformation
- Recombinant Proteins
- Sequence Analysis
- Spectrum Analysis, Raman
- Tyrosine
- Ultraviolet Rays