The 2.7 Å crystal structure of deoxygenated hemoglobin from the sea lamprey (Petromyzon marinus): Structural basis for a lowered oxygen affinity and Bohr effect

Structure

Volumn 7, Issue 5, 1999, Pages 517-526

  Heaslet, Holly A ^a,b   Royer Jr , William E ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b CLARK UNIVERSITY   (United States)

Author keywords

Bohr effect; Cooperativity; Hemoglobin; Ligand linked oligomerization

Indexed keywords

HEMOGLOBIN; DEOXYHEMOGLOBIN; OXYGEN;

ARTICLE; BINDING AFFINITY; BOHR EFFECT; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; LAMPREY; LIGAND BINDING; NONHUMAN; OLIGOMERIZATION; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; ANIMAL; BLOOD; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; METABOLISM; X RAY CRYSTALLOGRAPHY;

MOLLUSCA; PETROMYZON MARINUS; PETROMYZONTIDAE;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HEMOGLOBINS; LAMPREYS; MODELS, MOLECULAR; OXYGEN; PROTEIN CONFORMATION;

EID: 34548520171     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80068-9     Document Type: Article

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