Changes of tyrosine and tryptophan residues in human hemoglobin by oxygen binding: near- and far-UV circular dichroism of isolated chains and recombined hemoglobin-Reference-Cited by-同舟云学术

Changes of tyrosine and tryptophan residues in human hemoglobin by oxygen binding: near- and far-UV circular dichroism of isolated chains and recombined hemoglobin

Published:2000-11 Issue:1-4 Volume:82 Page:93-101
ISSN:0162-0134
Container-title:Journal of Inorganic Biochemistry
language:en
Short-container-title:Journal of Inorganic Biochemistry

Author:

Li R,Nagai Y,Nagai M

Publisher

Elsevier BV

Subject

Inorganic Chemistry,Biochemistry

Reference28 articles.

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2. Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism

3. Site-directed mutagenesis in haemoglobin

4. Homoglobin Rouen (α-140 (HC2) Tyr→His): alteration of the α-chain C-terminal region and moderate increase in oxygen affinity

5. Hemoglobin Hirose, a human hemoglobin variant with a substitution at the alpha1beta2 interface. Subunit dissociation and the equilibria and kinetics of ligand binding.

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