Baron Chanda

Associate Professor

Picture of Baron ChandaWisconsin Institute for Medical Research (WIMR II)
Room 9457
1111 Highland Ave
Madison, WI, 53705
Phone: (608) 265-3936
Email: chanda@wisc.edu
Overview · Publications · Lab Website

Education

B.S., 1991, University of Delhi, India
M.S., 1993, University of Poona, India
Ph.D., 2000, National Center for Biological Sciences, Bangalore, India
Postdoctoral, 2000-06, University of California, Los Angeles

Areas of Study

Biomolecular Folding & Interactions
Membrane Dynamics & Proteins
Metals in Biology
Quantitative Biology
Structural Biology

Research Overview

We study the structure and dynamics of voltage-activated ion channels (VGICs). These molecules are primarily responsible for electrical excitability and sensory transduction in the human body. Graduate students in the Chanda lab have access to an array of biophysical techniques that includes but limited to electrophysiology, fluorescence spectroscopy, single-molecule methods and crystallography to address the fundamental mechanisms that underlie structure and activity of these physiologically important membrane proteins

One broad area of research in the Chanda lab is to understand the origin of molecular forces that drive conformational changes responsible for coupling a sensing domain to the ion pore. A protein is described as a complex meshwork of interactions where only some of which are involved in conformational coupling. We have recently described a set of mathematical equations that allow us to calculate activation and coupling energies in a model-independent manner. These analytical tools have enabled us to undertake a large scale analysis of interaction energies that underlie activation gating of voltage-and ligand-activated ion channels. Early work from Chanda lab resulted in identification of the molecular determinants of conformational coupling in voltage-activated sodium channels (see Figure 1).

image of Voltage-clamp fluorimetry to identify mutants that are involved in coupling voltage-sensor to pore opening in two interfaces (marked boxes).  This approach simultaneously tracks channel opening and voltage-sensor movement in response to voltage jumps.

Figure 1. Voltage-clamp fluorimetry to identify mutants that are involved in coupling voltage-sensor to pore opening in two interfaces (marked boxes).  This approach simultaneously tracks channel opening and voltage-sensor movement in response to voltage jumps. (Adapted from Muroi et. al. (2010) Nature Structural and Molecular Biology 17(2):217-230).

Some members of this superfamily are exquisitely sensitive to temperature stimulus and are considered to be the primary thermosensors in the human body. We want to understand the physiochemical basis of temperature-sensitivity of these ion channels. We have recently described the design principles of a heat-sensitive and a cold-sensitive ion channels. We are currently testing the hypothesis that the temperature-sensitivity in natural channels is not limited to specific modular domains but is distributed throughout the protein structure.

Image of Design of a temperature-sensitive ion channel

Figure 2. Design of a temperature-sensitive ion channel from Chowdhury et. al. (2014) Cell 158, 1148-1158.