Speaker
Mrs
Edona Karakaçi
(1.Adolphe Merkle Institute, University of Fribourg)
Description
The work presented here demonstrates that plasmonic optical tweezers can reveal insights into the conformational dynamics of native proteins that so far have not been investigated on a single molecule level. We examined citrate synthase , an enzyme of the Krebs cycle, which consists of two identical subunits with one active site per subunit. Previous studies show that during catalysis, each subunit of the enzyme independently closes upon substrate binding and opens for product release and renewed substrate binding. Our approach reveals that during the enzymatic cycle, the subunits of citrate synthase populate a previously unknown, intermediate conformation that is crucial for enzyme activity.
Authors
Mrs
Edona Karakaçi
(1.Adolphe Merkle Institute, University of Fribourg)
Dr
Cuifeng Ying
(1.Adolphe Merkle Institute, University of Fribourg ; 2.Advanced Optics and Photonics Lab, Department of Engineering, Nottingham Trent University, United Kingdom.)
Dr
Alessandro Ianiro
(1.Adolphe Merkle Institute, University of Fribourg)
Dr
Esteban Bernudez Urena
(1.Adolphe Merkle Institute, University of Fribourg ; 3.Centro de investigación en Ciencia e Ingeniería de Materiales and Escuela de Física, Universidad de Costa Rica)
Prof.
Reuven Gordon
(4.Department of Electrical and Computer Engineering, University of Victoria)
Prof.
Michael Mayer
(1.Adolphe Merkle Institute, University of Fribourg)