To gain a molecular level understanding of the transduction machinery, it is necessary to determine the energetic contributions of amino acid chains to various processes. To determine the relative contributions of a particular side chain to structural stability vis-a-vis energy transduction, my group has developed a set of analytical tools to directly measuring coupling energies and pairwise interactions that underlie this process. We showed that measuring conjugate displacements associated with a stimulus allows us to compute these interactions for multi-state processes without making any assumption about the underlying model. This work gained a lot of attention in the field.
- Chowdhury S, Chanda B. Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation. J Gen Physiol. 2012 Jan;139(1):3-17. PubMed PMID: 22155736; PubMed Central PMCID: PMC3250103.
- Chowdhury S, Chanda B. Free-energy relationships in ion channels activated by voltage and ligand. J Gen Physiol. 2013 Jan;141(1):11-28. PubMed PMID: 23250866; PubMed Central PMCID: PMC3536522.
- Chowdhury S, Haehnel BM, Chanda B. A self-consistent approach for determining pairwise interactions that underlie channel activation. J Gen Physiol. 2014 Nov;144(5):441-55. PubMed PMID: 25311637; PubMed Central PMCID: PMC4210424.
- Chowdhury S, Haehnel BM, Chanda B. Interfacial gating triad is crucial for electromechanical transduction in voltage-activated potassium channels. J Gen Physiol. 2014 Nov;144(5):457-67. PubMed PMID: 25311635; PubMed Central PMCID: PMC4210428.
Check out commentaries by Chris Miller (JGP (2012) Pgs:1-2) and Ofer Yifrach (JGP (2013) Pgs:3-9)
See Sandipan’s video abstract
See Dan Sigg (our collaborator’s) video abstract