Hemoglobin Einstein: Semisynthetic deletion in the B-helix of the α-chain

Protein Science

Volumn 13, Issue 5, 2004, Pages 1266-1275

  Srinivasulu, Sonati ^a   Manjula, Belur N ^a   Nagel, Ronald L ^a   Tsai, Ching Hsuan ^b   Ho, Chien ^b   Prabhakaran, Muthuchidambaran ^a   Acharya, Seetharama A ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b CARNEGIE MELLON UNIVERSITY   (United States)

Author keywords

1H NMR spectroscopy; Molecular modeling; Oxygen affinity; Shortened B helix; Stuctural plasticity; Subunit interfaces; Thermodynamic stability

Indexed keywords

HEMOGLOBIN A; HEMOGLOBIN ALPHA CHAIN; HEMOGLOBIN BETA CHAIN;

ARTICLE; BOHR EFFECT; HUMAN; HUMAN CELL; MOLECULAR MODEL; PLASTICITY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; THERMODYNAMICS;

HEMOGLOBIN A; HEMOGLOBINS, ABNORMAL; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; MODELS, MOLECULAR; OXYGEN; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; SEQUENCE DELETION; THERMODYNAMICS;

EID: 1942537545     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03567804     Document Type: Article

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