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Volumn 49, Issue 40, 2010, Pages 8766-8778

A biosensor study indicating that entropy, electrostatics, and receptor glycosylation drive the binding interaction between interleukin-7 and its receptor

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC MECHANISMS; BINDING AFFINITIES; BINDING INTERACTION; BINDING INTERFACE; BIOPHYSICAL STUDIES; CHARGE INTERACTIONS; ELECTROSTATIC COMPONENTS; ENTHALPY CHANGE; ENTROPY CHANGES; EXTRACELLULAR DOMAINS; GLYCOSYLATED; HEAT CAPACITY CHANGE; INTERLEUKIN-7; N-GLYCAN; N-GLYCANS; N-LINKED GLYCOSYLATION; REACTION PATHWAYS; SALT CONCENTRATION; SURFACE PLASMON RESONANCE SPECTROSCOPY; T CELLS; TRANSITION-STATE; TRANSITION-STATE BINDING; TWO-STEP REACTIONS; VAN'T HOFF ANALYSIS;

EID: 77957683633     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101050h     Document Type: Article
Times cited : (14)

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