Baron Chanda

Baron Chanda
Associate Professor, Department of Neuroscience
(608) 265-3936


Ph.D. National Centre for Biological Sciences, India

Research Focus:

Structural Mechanisms underlying Voltage-dependent Gating of Ion Channels

Research Strengths:

Membrane Excitability and Synaptic Transmission; Molecular Neuroscience

Research Description:

Ion channels are a class of membrane proteins that are essential for electrical signaling and information processing in the central nervous system. Research in my laboratory focuses on understanding how the structure and structural dynamics of voltage-dependent ion channels determine their function. These studies provide insights into fundamental mechanisms that determine and modulate electrical excitability in the central nervous system.

In response to a stimulus, voltage-dependent ion channels undergo a series of conformational transitions. These transitions involve early movements of the voltage-sensing domain followed by conformational changes in the pore domain of the ion channel. We are using a combination of spectroscopic (mainly fluorescence), biochemical and electrophysiological approaches to obtain insights into the structures of these transient states that are generated when the channel undergoes conformational change. The fluorescence technique allows us to take rapid snapshots of the ion channel molecule as it transits through various functional states. We are currently focused on understanding how the movement of the voltage-sensing domain is coupled to the conformational changes in the pore domain of the sodium channel. One project in the lab involves studying how molecules like local anesthetics that bind to the pore domain of the sodium channel affect the conformational changes in the voltage-sensing domain. We are expanding these studies to delineate the molecular determinants that are involved in coupling the movement of the voltage-sensor to the pore domain. The other area of interest in the lab is to study the structure-function relationships of the TRPV ion channel. Members of this family are the primary transducers of temperature stimuli. Temperature appears to dramatically affect the voltage-dependent activity of these channels. We are interested understanding the structural basis of high temperature sensitivity of TRPV channels.


Please see PubMed for most recent publications