Role of Interhelical H-Bonds (Wα14−Tα67 and Wβ15−Sβ72) in the Hemoglobin Allosteric Reaction Path Evaluated by UV Resonance Raman Spectroscopy of Site-Mutants
- 19 November 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 121 (48) , 11197-11203
- https://doi.org/10.1021/ja992228w
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Structure Changes in Hemoglobin upon Deletion of C-Terminal Residues, Monitored by Resonance Raman SpectroscopyBiochemistry, 1998
- Tyrosine and Tryptophan Structure Markers in Hemoglobin Ultraviolet Resonance Raman Spectra: Mode Assignments via Subunit-Specific Isotope Labeling of Recombinant ProteinBiochemistry, 1997
- Contribution of Surface Histidyl Residues in the α-Chain to the Bohr Effect of Human Normal Adult Hemoglobin: Roles of Global Electrostatic EffectsBiochemistry, 1997
- Hemoglobin Allostery: Resonance Raman Spectroscopy of Kinetic IntermediatesScience, 1995
- Nanosecond Dynamics of the R→T Transition in Hemoglobin: Ultraviolet Raman StudiesScience, 1994
- Tryptophan Raman bands sensitive to hydrogen bonding and side‐chain conformationJournal of Raman Spectroscopy, 1989
- The crystal structure of human deoxyhaemoglobin at 1.74 Å resolutionJournal of Molecular Biology, 1984
- Structure of human oxyhaemoglobin at 2·1resolutionJournal of Molecular Biology, 1983
- Dimeric and tetrameric hemoglobins from the mollusc Scapharca inaequivalvisJournal of Molecular Biology, 1981
- The structure of human carbonmonoxy haemoglobin at 2.7 Å resolutionJournal of Molecular Biology, 1980