Laboratory of Biomolecular Structure, Dynamics and Function

Research Interests

Host-Microbe Interactions

Microbes hijack the host machinery to their own advantage. During infection, several host defense mechanisms are destabilized by the microbes using the ubiquitin-proteasome pathway. We study the interactions between microbial factors and host proteins to understand this process.

Protein Quality Control

Misfolding of proteins can lead to accimulation of toxic aggregates. It is assumed that higher energy intermediates along the protein folding landscape seed the formation of toxic aggregates. Protein quality control systems like the Ubiquitin-proteasome pathway ensures that these potentially toxic species are degraded. We are interested to get insights into the structure of higher energy intermediates. We also investigate how misfolded proteins targeted by the ubiquitin-proteasome pathway.

 

 

 

 

 

 

Positions: We are actively looking for postdocs with a Phd in protein-chemistry/protein-Xray-crystallography/protein-NMR and Virology. Please apply with a detailed CV to rana@ncbs.res.in. Your CV should reflect your expertise and research interest.

Students interested in Phd are requested to apply through the NCBS-PhD program. There are no summer/winter positions available.

Recent Publications

Mohanty P, Agrata R, Habibullah BI, Geetha Surendran A, Das R. (2019), Deamidation disrupts native and transient contacts to weaken the interaction between UBC13 and RING-finger E3 ligases, eLife 8:e492238.

Tripathi V, Chatterjee KS, Das R. (2019), Casein kinase-2 mediated phosphorylation increases the SUMO-dependent activity of the cytomegalovirus transactivator IE2, J Biol Chem. 294(40):14546-14561.

Chatterjee KS, Tripathi V, Das R, (2019) A conserved and buried edge-to-face aromatic interaction in Small Ubiquitin-like Modifier (SUMO) has a role in SUMO stability and function, J Biol Chem. 294(17):6772-6784.

Nandwani N, Surana P, Negi H, Mascarenhas NM, Udgaonkar JB*, Das R*, Gosavi S*, (2019) A five-residue motif for the design of domain swapping in proteins, Nature Communications. 10(1):452. *Corresponding authors.

Nandwani N#, Surana P#, Udgaonkar JB*, Das R*, Gosavi S.*, (2017) Amino-acid composition after loop deletion drives domain swapping, Protein Sci. 26(10):1994-2002. #Equal Contribution, *Corresponding authors.

Sengupta I, Bhate S, Das R*, Udgaonkar J*, (2017), Salt-Mediated Oligomerization of the Mouse Prion Protein Monitored by Real-Time NMR, J. Mol. Biol., 429(12): 1852-1872. *Corresponding authors.

Chakrabarti KS, Li J, Das R*, Byrd RA*, (2017), Conformational Dynamics and Allostery in E2:E3 Interactions Drive Ubiquitination: gp78 and Ube2g2., Structure, 25(5):794-805. *Corresponding authors.