Baron Chanda

Position title: Professor


Phone: (608) 265-3936

9457 Wisconsin Institute for Medical Research
111 Highland Ave. Madison, WI 53705

Baron Chanda

• BS 1991, University of Delhi, India
• MS 1993, University of Poona, India
• PhD 2000, National Center for Biological Sciences, Bangalore, India (M.K. Mathew)
• Postdoctoral, 2000-06, University of California, Los Angeles (Francisco Bezanilla)

Honors & Awards

• Scientist Development Grant, American Heart Association, 2005
• Shaw Scientist Award, 2008
• UW-Madison Vilas Associate Award, 2012
• Cranefield Award, Society of General Physiologists, 2013
• UW-Madison Romnes Award, 2015

Research Interests

The voltage-activated ion channel superfamily (VGICs) constitutes a large class of membrane proteins that are primarily responsible for sensory transduction and electrical signaling. The members of this superfamily respond to a variety of stimuli that range from voltage and temperature on one hand to calcium, cyclic nucleotides and phosphoinositides, on the other. Our goal is to understand at a fundamental level how the interplay of structure and dynamics determines the function of these ion channels and ultimately defines electrical excitability of biomembranes. We employ an array of biophysical techniques that includes but limited to electrophysiology, fluorescence spectroscopy, single-molecule methods and crystallography to address the molecular mechanisms of gating and modulation. Along with these experimental approaches, we are also developing analytical tools to quantify and measure energetics of ion channel activation.

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 enables us to calculate activation and coupling energies in a model-independent manner. Early work from Chanda lab resulted in identification of the molecular determinants of conformational coupling in voltage-activated sodium channels (see Figure 1).


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).

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


Publications of Note

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• Alvarez-Baron CP, Klenchin VA, Chanda B (2018) Minimal molecular determinants of isoform-specific differences in efficacy in the HCN channel family. J. Gen. Physiol. 150(8):1203-1213 (PMC6080897)

• Fernández-Mariño AI, Harpole TJ, Oelstrom K, Delemotte L, Chanda B (2018) Gating interaction maps reveal a noncanonical electromechanical coupling mode in the Shaker K channel. Nat. Struct. Mol. Biol. 25(4):320-326

• Bao H, Das D, Courtney NA, Jiang Y, Briguglio JS, Lou X, Roston D, Cui Q, Chanda B, Chapman ER (2018) Dynamics and number of trans-SNARE complexes determine nascent fusion pore properties. Nature 554(7691):260-263 (PMC5808578)

• Goldschen-Ohm MP, Chanda B (2017) SnapShot: Channel Gating Mechanisms. Cell 170(3):594-594.e1

• Zhao Y, Goldschen-Ohm MP, Morais-Cabral JH, Chanda B, Robertson GA (2017) The intrinsically liganded cyclic nucleotide-binding homology domain promotes KCNH channel activation. J. Gen. Physiol. 149(2):249-260 (PMC5299623)

• Goldschen-Ohm MP, White DS, Klenchin VA, Chanda B, Goldsmith RH (2017) Observing Single-Molecule Dynamics at Millimolar Concentrations. Angew. Chem. Int. Ed. Engl. 56(9):2399-2402

• Goldschen-Ohm MP, Klenchin VA, White DS, Cowgill JB, Cui Q, Goldsmith RH, Chanda B (2016) Structure and dynamics underlying elementary ligand binding events in human pacemaking channels. Elife 5: (PMC5115869)

• Oelstrom K, Chanda B (2016) Congruent pattern of accessibility identifies minimal pore gate in a non-symmetric voltage-gated sodium channel. Nat Commun 7:11608 (PMC4873679)

• Ahern CA, Payandeh J, Bosmans F, Chanda B (2016) The hitchhiker’s guide to the voltage-gated sodium channel galaxy. J. Gen. Physiol. 147(1):1-24 (PMC4692491)

• Bao H, Goldschen-Ohm M, Jeggle P, Chanda B, Edwardson JM, Chapman ER (2016) Exocytotic fusion pores are composed of both lipids and proteins. Nat. Struct. Mol. Biol. 23(1):67-73 (PMC4756907)

•Goldschen-Ohm MP, Chanda B (2015) How to open a proton pore-more than S4? Nat. Struct. Mol. Biol. 22(4):277-8

• Chowdhury S, Haehnel BM, Chanda B (2014) A self-consistent approach for determining pairwise interactions that underlie channel activation. J. Gen. Physiol. 144(5):441-55 (PMC4210424)

• Chowdhury S, Haehnel BM, Chanda B (2014) Interfacial gating triad is crucial for electromechanical transduction in voltage-activated potassium channels. J. Gen. Physiol. 144(5):457-67 (PMC4210428)

• Chowdhury S, Jarecki BW, Chanda B (2014) A molecular framework for temperature-dependent gating of ion channels. Cell 158(5):1148-58 (PMC4405168)

• Goldschen-Ohm MP, Chanda B (2014) Probing gating mechanisms of sodium channels using pore blockers. Handb Exp Pharmacol 221:183-201

• Oelstrom K, Goldschen-Ohm MP, Holmgren M, Chanda B (2014) Evolutionarily conserved intracellular gate of voltage-dependent sodium channels. Nat Commun 5:3420 (PMC3959192)