Site-directed mutations of human hemoglobin at residue 35β: A residue at the intersection of the α1β1, α1β2, and α1α2 interfaces-Reference-Cited by-同舟云学术

Site-directed mutations of human hemoglobin at residue 35β: A residue at the intersection of the α1β1, α1β2, and α1α2 interfaces

Published:2001-09 Issue:9 Volume:10 Page:1847-1855
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Sci.

Author:

Kavanaugh Jeffrey S.,Weydert Jamie A.,Rogers Paul H.,Arnone Arthur,Hui Hilda L.,Wierzba Anita M.,Kwiatkowski Laura D.,Paily Paul,Noble Robert W.,Bruno Stefano,Mozzarelli Andrea

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference41 articles.

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4. Molecular stability of Hb Philly (α2β2 35[C1] Tyr → Phe): The relationship of hemoglobin stability to ligand state as defined by heat and mechanical shaking tests;Asakura;Hemoglobin,1981

5. Functional properties of carboxypeptidase-digested hemoglobin;Bonaventura;J. Mol. Biol.,1974

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