• Twitter
  • Facebook
  • Google+
  • LinkedIn

Institute Lectures on Fluorescence Correlation Spectroscopy (FCS) by Prof. Sudipta Maiti

Topic: Fluorescence Correlation Spectroscopy: A Basic Minimum Course

Venue: Room 350, 2nd floor, Chemistry Annex

Date: May 3 to May 6, 2019

Time: 15:00 to 16:00 and 16:30 to 17:30

Abstract:

FCS provides diffusion coefficients rather easily. This technique has been used widely to study protein folding, fibrillation etc. Commonly, FCS is employed in optical microscopy, in particular, confocal microscopy or two photon excitation microscopy. In these techniques, light is focused on a sample and the measured fluorescence intensity fluctuations (due to diffusion, physical or chemical reactions, aggregation, etc.) are analyzed using the temporal autocorrelation. Because the measured property is essentially related to the magnitude and/or the amount of fluctuations, there is an optimum measurement regime at the level when individual species enter or exit the observation volume (or turn on and off in the volume). When too many entities are measured at the same time the overall fluctuations are small in comparison to the total signal and may not be resolvable – in the other direction, if the individual fluctuation-events are too sparse in time, one measurement may take prohibitively too long. FCS is in a way the fluorescent counterpart to dynamic light scattering, which uses coherent light scattering, instead of (incoherent) fluorescence.

About the speaker:

Prof. Sudipta Maiti is currently a Professor in the Department of Chemical Sciences at TIFR (Tata Institute of Fundamental Research). His area of research includes protein misfolding/aggregation and vesicular neurotransmission. He got his Doctoral Degree in 1994 from the University of Pennsylvania, Philadelphia, PA, USA and has also got some postdoctoral experience at Cornell University, New York, USA. He has published a lot of research papers in his field which includes research on Label-free Ratiometric Imaging of Serotonin in Live Cells, on Major Reaction Coordinates Linking Transient Amyloid-Beta Oligomers to Fibrils Measured at Atomic Level, etc.