Using surface plasmon resonance to directly measure slow binding of low-molecular mass inhibitors to a VanX chip

Analytical Biochemistry

Volumn 359, Issue 1, 2006, Pages 63-71

  Chang, Yi Pin ^a   Tseng, Min Jen ^a   Chu, Yen Ho ^a  

^a NATIONAL CHUNG CHENG UNIVERSITY   (Taiwan)

Author keywords

Inhibitor; Substrate; Surface plasmon resonance; Vancomycin; VanX enzyme

Indexed keywords

BACTERIA; BINDING ENERGY; DRUG PRODUCTS; ENZYMES; PEPTIDES; PLASMONS; RESONANCE; SUBSTRATES;

AROMATIC INTERACTIONS; BINDING INTERACTION; COMBINATORIAL SEARCH; CONFORMATIONAL ISOMERIZATION; INHIBITOR; NATURAL SUBSTRATES; PATHOGENIC BACTERIUM; VANCOMYCIN;

SURFACE PLASMON RESONANCE;

DIPEPTIDE; ENZYME; GENE PRODUCT; PHOSPHONIC ACID DERIVATIVE; VANCOMYCIN;

ANALYTIC METHOD; ARTICLE; BINDING KINETICS; BINDING SITE; CHEMICAL STRUCTURE; COMBINATORIAL CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; GEOMETRY; INHIBITION KINETICS; ISOLATION PROCEDURE; ISOMERIZATION; MEASUREMENT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN SYNTHESIS; QUANTITATIVE ANALYSIS; STRUCTURE ANALYSIS; SURFACE PLASMON RESONANCE;

EID: 33750614316     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.08.009     Document Type: Article

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