Kinetic analysis of the mass transport limited interaction between the tyrosine kinase lck SH2 domain and a phosphorylated peptide studied by a new cuvette-based surface plasmon resonance instrument

Analytical Biochemistry

Volumn 279, Issue 1, 2000, Pages 61-70

  De Mol, Nico J ^a   Plomp, Emke ^a   Fischer, Marcel J E ^a   Ruijtenbeek, Rob ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DIFFUSION; DISSOCIATION; KINETICS; LINEARIZATION; OPTICAL INSTRUMENTS; PEPTIDES; PLASMONS; RATE CONSTANTS;

ASSOCIATION RATE CONSTANTS; BINDING CAPACITIES; BINDING ISOTHERMS; DISSOCIATION RATE CONSTANT; MASS TRANSPORT LIMITATION; PEPTIDE-PROTEIN INTERACTIONS; PHOSPHORYLATED PEPTIDES; SECOND ORDER KINETICS;

SURFACE PLASMON RESONANCE;

PHOSPHOPROTEIN; PROTEIN TYROSINE KINASE;

ARTICLE; BINDING AFFINITY; CHEMICAL REACTION KINETICS; DIFFUSION; DISSOCIATION CONSTANT; MATHEMATICAL MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN IMMOBILIZATION; PROTEIN INTERACTION; SURFACE PLASMON RESONANCE; VISCOSITY;

IBIS;

EID: 0034066682     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.1999.4464     Document Type: Article

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