Histidine proton resonances of carbonmonoxyhaemoglobins A and Cowtown in chloride-free buffer

A re-examination of the C-2 histidine proton resonances of haemoglobins A and Cowtown (His HC3(146)β → Leu) in chloride-free Hepes buffer has shown that all the resonances present in haemoglobin A are present in haemoglobin Cowtown, so that the p K a of His HC3(146)β cannot be determined by nuclear...

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Published inJournal of molecular biology Vol. 195; no. 2; pp. 453 - 455
Main Authors Shih, Daniel T.-b., Perutz, Max F., Gronenborn, Angela M., Clore, G.Marius
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 20.05.1987
Elsevier
Subjects
Biological and medical sciences
Carboxyhemoglobin
Fundamental and applied biological sciences. Psychology
Hemoglobin A
Hemoglobins, Abnormal
Histidine
Humans
Magnetic Resonance Spectroscopy
Molecular biophysics
Physico-chemical properties of biomolecules
Protons
Hemoglobin A
Histidine
Bohr effect
Hemoglobin
Proton
Carboxyhemoglobin
Nuclear magnetic resonance
Aqueous solution
Buffer solution
Comparative study
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Summary:A re-examination of the C-2 histidine proton resonances of haemoglobins A and Cowtown (His HC3(146)β → Leu) in chloride-free Hepes buffer has shown that all the resonances present in haemoglobin A are present in haemoglobin Cowtown, so that the p K a of His HC3(146)β cannot be determined by nuclear magnetic resonance in this buffer.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0022-2836
1089-8638
DOI:10.1016/0022-2836(87)90666-8