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
Author:
Affiliation:
1. Contribution from the Department of Chemistry, Princeton University, Princeton, New Jersey 08544, and Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja992228w
Reference28 articles.
1. Hemoglobin R.fwdarw.T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals
2. Nanosecond Dynamics of the R→T Transition in Hemoglobin: Ultraviolet Raman Studies
3. Hemoglobin Allostery: Resonance Raman Spectroscopy of Kinetic Intermediates
4. Nanosecond Step-Scan FTIR Spectroscopy of Hemoglobin: Ligand Recombination and Protein Conformational Changes
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