Confirmation of a unique intra-dimer cooperativity in the human hemoglobin ?1?1half-oxygenated intermediate supports the symmetry rule model of allosteric regulation-Reference-Cited by-同舟云学术

Confirmation of a unique intra-dimer cooperativity in the human hemoglobin ?1?1half-oxygenated intermediate supports the symmetry rule model of allosteric regulation

Published:2000 Issue:S4 Volume:41 Page:23-43
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Ackers Gary K.,Holt Jo M.,Huang Yingwen,Grinkova Yelena,Klinger Alexandra L.,Denisov Ilia

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference104 articles.

1. Deciphering the Molecular Code of Hemoglobin Allostery

2. Analytical Gel Chromatography of Proteins

3. Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates

4. Direct and indirect pathways of functional coupling in human hemoglobin are revealed by quantitative low-temperature isoelectric focusing of mutant hybrids

5. Molecular Code for Cooperativity in Hemoglobin

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