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Dynamic Allosteric Mechanism of Modulation of Oxygen-Affinity in Human Hemoglobin

โœ Scribed by Yonetani, Takashi

Book ID
122124640
Publisher
Biophysical Society
Year
2013
Tongue
English
Weight
43 KB
Volume
104
Category
Article
ISSN
0006-3495

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Allosteric effectors do not alter the ox
Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals
โœ Andrea Mozzarelli; Claudio Rivetti; Gian Luigi Rossi; William A. Eaton; Eric R. ๐Ÿ“‚ Article ๐Ÿ“… 2008 ๐Ÿ› Cold Spring Harbor Laboratory Press ๐ŸŒ English โš– 581 KB

In solution, the oxygen affinity of hemoglobin in the T quaternary structure is decreased in the presence of allosteric effectors such as protons and organic phosphates. To explain these effects, as well as the absence of the Bohr effect and the lower oxygen affinity of T-state hemoglobin in the cry