High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the root effect

Proteins: Structure, Function and Genetics

Volumn 65, Issue 2, 2006, Pages 490-498

  Mazzarella, Lelio ^a,b   Vergara, Alessandro ^a,b   Vitagliano, Luigi ^b   Merlino, Antonello ^a   Bonomi, Giovanna ^a   Scala, Sonia ^a   Verde, Cinzia ^c   Di Prisco, Guido ^c  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b CNR   (Italy)

^c INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Cooperativity; High resolution; Histidine; pH modulation; Root effect

Indexed keywords

ASPARTIC ACID; DEOXYHEMOGLOBIN; HISTIDINE;

ARTICLE; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; FISH; HYDROGEN BOND; NONHUMAN; OXYGEN AFFINITY; PH; PKA; PRIORITY JOURNAL; PROTEIN STRUCTURE; TREMATOMUS BERNACCHII;

AMINO ACID MOTIFS; ANIMALS; CRYSTALLOGRAPHY, X-RAY; HEMOGLOBINS; HISTIDINE; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; PERCIFORMES; PROTEIN STRUCTURE, TERTIARY;

TREMATOMUS BERNACCHII;

EID: 33748996221     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21114     Document Type: Article

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