Positive and negative cooperativities at subsequent steps of oxygenation regulate the allosteric behavior of multistate sebacylhemoglobin

Biochemistry

Volumn 35, Issue 11, 1996, Pages 3418-3425

  Bucci, Enrico ^a   Razynska, Anna ^a   Kwansa, Herman ^a   Gryczynski, Zygmunt ^a   Collins, John H ^b   Fronticelli, Clara ^a   Unger, Ron ^c   Braxenthaler, Michael ^c   Moult, John ^c   Ji, Xinhua ^c   Gilliland, Gary ^c  

^a UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF MARYLAND   (United States)

^c UNIVERSITY OF MARYLAND BIOTECHNOLOGY INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN DERIVATIVE; SEBACYLHEMOGLOBIN; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HUMAN; MOLECULAR INTERACTION; MOLECULAR MODEL; OXYGEN AFFINITY; OXYGEN DISSOCIATION CURVE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN CROSS LINKING;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; CROSS-LINKING REAGENTS; CRYSTALLOGRAPHY, X-RAY; DECANOIC ACIDS; HEMOGLOBINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXYGEN; OXYHEMOGLOBINS; PEPTIDE MAPPING; PEPTIDES; PROTEIN CONFORMATION; SALICYLIC ACIDS; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 0040267932     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952446b     Document Type: Article

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