Normal coordinate structural decomposition of the heme distortions of hemoglobin in various quaternary states and bound to allosteric effectors

Molecular Diversity

Volumn 7, Issue 1, 2003, Pages 15-23

  Laberge, Monique ^a   Yonetani, Takashi ^b   Fidy, Judit ^a  

^a SEMMELWEIS UNIVERSITY   (Hungary)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Allosteric effectors; Cooperativity; Hemoglobin; Normal coordinate structural decomposition

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; GLYCOSYLATED HEMOGLOBIN; HEME; HEME DERIVATIVE; HEMOGLOBIN A; HEMOGLOBIN A2; HEMOGLOBIN BETA CHAIN; PHYTIC ACID; PROTEIN SUBUNIT;

ALLOSTERISM; ARTICLE; COOPERATION; DECOMPOSITION; ENERGY; EXTRACTION; HUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; REGULATORY MECHANISM; SCIENTIFIC LITERATURE; SEGREGATION DISTORTION; STRUCTURE ANALYSIS;

ALLOSTERIC SITE; COMPUTER SIMULATION; DIMERIZATION; HEME; HEMOGLOBIN A; MODELS, MOLECULAR;

EID: 0345825851     PISSN: 13811991     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MODI.0000006532.16981.e8     Document Type: Article

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