Article
Hemoglobin site-mutants reveal dynamical role of interhelical H-bonds in the allosteric pathway: time-resolved UV resonance Raman evidence for intra-dimer coupling.
Journal of molecular biology - 16 Jul 2004
Balakrishnan Gurusamy, Tsai Ching-Hsuan, Wu Qiang, Case Martin A, Pevsner Alex, McLendon George L, Ho Chien, Spiro Thomas G
Abstract excerpt
The dynamical effect of eliminating specific tertiary H-bonds in the hemoglobin (Hb) tetramer has been investigated by site-directed mutagenesis and time-resolved absorption and ultraviolet resonance Raman (UVRR) spectroscopy. The Trp alpha 14...Thr alpha 67 and Trp beta 15...Ser beta 72 H-bonds...
Topics
- Absorption
- Allosteric Regulation
- Amino Acid Substitution
- Carboxyhemoglobin
- Dimerization
- Escherichia coli
- Genetic Variation
- Heme
- Hemoglobin A
- Humans
- Hydrogen Bonding
- Hydrogen-Ion Concentration
- Kinetics
- Ligands