High pressure reveals that the stability of interdimeric contacts in the R- and T-state of HbA is influenced by allosteric effectors: Insights from computational simulations

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 3, 2006, Pages 516-521

  Kovesi I ^a   Schay, G ^a   Yonetani, T ^b   Laberge, M ^a,b   Fidy, J ^a  

^a SEMMELWEIS UNIVERSITY   (Hungary)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Dimer interface; Hb allostery; Heterotropic effector; High pressure; Human hemoglobin; MD simulation

Indexed keywords

DIMER; HEMOGLOBIN A; WATER;

ALLOSTERISM; ARTICLE; DATA ANALYSIS; EXPERIMENT; HYPERBARISM; MOLECULAR MODEL; MOLECULE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ANALYSIS;

ALLOSTERIC REGULATION; COMPUTER SIMULATION; HEMOGLOBIN A; HUMANS; MODELS, MOLECULAR; PRESSURE; PROTEIN CONFORMATION;

EID: 33645957933     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.12.002     Document Type: Article

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