Dr. Sujoy Mukherjee
Current Research Interest
The overall goal of this lab is to study the structure and dynamics of proteins undergoing conversion to amyloid fibrils as well as to understand the mechanism of signal transduction by membrane proteins using solution and solid-state NMR spectroscopy. Some of the ongoing as well as recently initiated research topics include: -
- High resolution studies on the aggregation of proteins to form amyloid fibrils.
- Mechanism of signal transduction by G-protein coupled receptors: structural and dynamic studies
- Investigating the structure and dynamics of amyloid fibrils using solid-state NMR.
Names of the group members including regular staff with designation and research fellows :
- Mr. Gopa Mahesh (JRF, DST INSPIRE FELLOW)
- Mr. Jitendra K Das (JRF, CSIR)
- Mr. Shyam S. Mall (JRF, ICMR)
- Ms. Juhi A. Rasquinha (JRF, UGC).
Students from any branch of science and engineering with NET (CSIR/UGC) are welcome to apply by sending email mukherjee.lab AT gmail DOT com. Fellows having an interest in physical chemistry, including the use of computational tools, are encouraged to apply. For further details, please visit group website.
Position is also open for a research assistant / postdoctoral fellow to perform postdoctoral research. Candidates with experience in biomolecular NMR or with high yield expression and purification of membrane proteins using eukaryotic cell cultures are encouraged to apply.
List of important Publications:
8.Mukherjee, S.; Pondaven, S. P.; Jaroniec, C. P., Conformational Flexibility of a Human Immunoglobulin Light Chain Variable Domain by Relaxation Dispersion Nuclear Magnetic Resonance Spectroscopy: Implications for Protein Misfolding and Amyloid Assembly Biochemistry 2011, 50, 5845-5857.
7. Jedidi, I.; Zhang, F.; Qiu, H.; Stahl, S. J.; Palmer, I.; Kaufman, J. D.; Nadaud, P. S.; Mukherjee, S.; Wingfield, P. T.; Jaroniec, C. P.; Hinnebusch, A. G., Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX domain, to recruit Mediator to target genes in vivo. J. Biol. Chem. 2010, 285, (4), 2438-2455.
6.Mukherjee, S.; Pondaven, S.; Jaroniec, C., Backbone and side-chain 1H, 13C and 15N resonance assignments for the κIV light-chain, variable domain of a recombinant, human immunoglobulin κIV light-chain variable domain. Biomol. NMR Assign. 2009, 3, (2), 255-259.
5.Mukherjee, S.; Huang, C.; Guerra, F.; Wang, K.; Oldfield, E., Thermodynamics of Bisphosphonates Binding to Human Bone: A Two-Site Model. J. Am. Chem. Soc. 2009, 131, (24), 8374-8375.
4. Zhang, Y.; Cao, R.; Yin, F.; Hudock, M.P.; Wang, H.; Guo, R.T.; Krysiak, K.; Mukherjee, S.; Gao, Y.; Robinson, H.; Song, Y.; No, J.H.; Bergan, K.; Leon, A.; Cass, L.; Goddard, A.; Chang, T.K.; Lin, F.Y.; Van Beek, E.V.; Papapoulos, S.; Wang, A.H.J.; Kubo, T.; Ochi, M.; Morita, C.T.; Oldfield, E., Lipophilic Bisphosphonates as Dual Farnesyl/Geranylgeranyl Diphosphate Synthase Inhibitors: An X-ray and NMR Investigation. J. Am. Chem. Soc. 2009, 131, (14), 5153–516. This article has been favorably reviewed in several news reports, including the following :-
3.Mukherjee, S.; Song, Y.; Oldfield, E., NMR Investigations of the Static and Dynamic Structures of Bisphosphonates on Bone: a Molecular Model. J. Am. Chem. Soc.2008, 130, (4), 1264-1273.
2. Mao, J. H.; Mukherjee, S.; Zhang, Y.; Cao, R.; Sanders, J. M.; Song, Y. C.; Zhang, Y. H.; Meints, G. A.; Gao, Y. G.; Mukkamala, D.; Hudock, M. P.; Oldfield, E., Solid-state NMR, crystallographic, and computational investigation of Bisphosphonates and farnesyl diphosphate synthase-bisphosphonate complexes. J. Am. Chem. Soc. 2006, 128, (45), 14485-1449.
1. Zhang, Y.; Mukherjee, S.; Oldfield, E., Zn-67 NMR chemical shifts and electric field gradients in zinc complexes: A quantum chemical investigation. J. Am. Chem. Soc.2005, 127, (8), 2370-2371