This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
All submissions of the EM system will be redirected to Online Manuscript Submission System. Authors are requested to submit articles directly to Online Manuscript Submission System of respective journal.
A biosensor is a key and important technique not only for drug screening, but also for detections of protein association
between bio-molecules. For example, inhaled anesthetic agents interact with many proteins and we can learn underlying
principles from such studies. Nevertheless, it is not generally simple to detect such association or conformational change by
conventional spectroscopy. Several techniques that can detect protein binding have been developed as a biosensor, and some of
them are commercially available now. Surface plasmon resonance (SPR) method is one of highly sensitive methods. The principle
of this technique is based on the refractive index change by the protein-protein binding and the refractive index dependence
of the wavenumber for the surface plasmon excitation. A target protein is fixed on a metal surface and an analyte molecule is
introduced on the surface. There have been reported many applications using this method. However, there are some inherent
shortcomings for this method. For example, the target protein should be fixed on metal surface and it usually takes several tens
minutes to accumulate proteins on the surface for detection. If one can detect the protein binding in solution phase with much
shorter time, it could be complementary to the SPR method. Here, I will show that the diffusion detection of proteins by the
laser induced transient grating (TG) method can be a suitable alternative way for detecting not only protein-protein binding but
also protein-drug interaction. This technique is based on the time-resolved detection of the refractive index change by the biomolecular
interaction and detects the diffusion coefficients, which represent physical and chemical nature of the species. Some
typical examples will be shown.
M.Terazima has completed his Ph.D from Kyoto University in Japan. He became an Assistant Professor at the Faculty of Science, Tohoku University at Sendai in 1986. He joined the Faculty of Science, Kyoto University in 1990 and was promoted to be a full professor. His current research interests include development of new methods to study reaction mechanisms of biological proteins, and for direct detection of energy and conformation of reactive species in time-domain. He authored more than 250 scientific papers.
Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals