Fourier Transform Infrared Evidence against Asp β99 Protonation in Hemoglobin: Nature of the Tyr α42−Asp β99 Quaternary H-Bond
Author:
Affiliation:
1. Department of Chemistry, Princeton University, Princeton, New Jersey 08544
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi9805644
Reference27 articles.
1. Site-directed mutagenesis in haemoglobin
2. Hemoglobin R.fwdarw.T structural dynamics from simultaneous monitoring of tyrosine and tryptophan time-resolved UV resonance Raman signals
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1. Intersubunit Interactions Associated with Tyr42α Stabilize the Quaternary-T Tetramer but Are Not Major Quaternary Constraints in Deoxyhemoglobin,;Biochemistry;2005-02-16
2. Time-resolved Absorption and UV Resonance Raman Spectra Reveal Stepwise Formation of T Quaternary Contacts in the Allosteric Pathway of Hemoglobin;Journal of Molecular Biology;2004-07
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