Conformation Coupled Enzyme Catalysis:  Single-Molecule and Transient Kinetics Investigation of Dihydrofolate Reductase

Ensemble kinetics and single-molecule fluorescence microscopy were used to study conformational transitions associated with enzyme catalysis by dihydrofolate reductase (DHFR). The active site loop of DHFR was labeled with a fluorescence quencher, QSY35, at amino acid position 17, and the fluorescent...

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Veröffentlicht in:Biochemistry (Easton) 2005-12, Vol.44 (51), p.16835-16843
Hauptverfasser: Antikainen, Nina M, Smiley, R. Derike, Benkovic, Stephen J, Hammes, Gordon G
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Sprache:eng
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