Publications
26. Veerpal Kaur; Surbhi Garg*; Sabyasachi Rakshit*(2023); Chem Commun., Polyprotein synthesis: a journey from the traditional pre-translational method to modern post-translational approaches for single-molecule force spectroscopy. https://pubs.rsc.org/en/content/articlelanding/2023/CC/D3CC01756G
25. Veerpal Kaur; Sanat Ghosh; Tripta Bhatia; Sabyasachi Rakshit(2023); Biochemistry. Redefining the structure of tip-links in hair-cells.
24. Pritam Saha, Vishavdeep Vashisht, Ojas Singh, Gaurav Bhati, Surbhi Garg, Sabyasachi Rakshit. (2023); Research Square . Heterogeneity in conformational state space enhances the force-tolerance of mechanosensory proteins. https://doi.org/10.21203/rs.3.rs-2677234/v1
23. Nisha Arora, Jagadish P. Hazra, Sandip Roy, Gaurav K. Bhati, Sarika Gupta, K. P. Yogendran, Abhishek Chaudhuri, Amin Sagar, Sabyasachi Rakshit. (2024); Nature Commun. Emergence of slip-ideal-slip behavior in tip-links serve as force filters of sound in hearing.
22. Silky Bedi, Gaurav Kumar, S. M. Rose, Sabyasachi Rakshit* and Sharmistha Sinha. (2022); Chem Comm. Barrier-free liquid condensates of nanocatalysts as effective concentrators of catalysis. https://doi.org/10.1039/D2CC03111F
21. Veerpal Kaur, Surbji Garg, Sabyasachi Rakshit. (2022); Soft Matter. Instantaneous splice and excise of inteins to synthesize polyproteins on a substrate with tunable linkers,18, 602-608 .
20. Sai Srinivas*, Gayathri S. Singaraju*, Veerpal Kaur*, Sayan Das, Sabyasachi Rakshit (2023)Commun. Biol. Transient interactions drive the lateral clustering of Cadherin-23 on membrane (BIORXIV/2022/475209).
19. Nisha Arora, Jagadish Prasad Hazra*, Sabyasachi Rakshit* (Commun. Biol.); Anisotropy in mechanical unfolding of protein upon partner-assisted pulling and handle-assisted pulling (https://doi.org/10.1038/s42003-021-02445-y).
18. Tanuja Joshi, Surbhi Garg, Alejandro Estaña, Juan Cortes, Pau Bernadó, Sayan Das, Anjana R. Kammath, Amin Sagar*, Sabyasachi Rakshit* (BBRC, 2021); Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins.
Highlights
>Random-coil linkers (-polyGly here) maintain the domain independence in polyproteins of Immunoglobulin repeats.
>Linkers (-RS here) that facilitate interdomain contacts may alter the energy landscape of individual domains cooperatively.
>A simple tripeptide-based modeling approach captures the inter-domain orientations across the IDLs.
17. Surbhi Garg1, Amin Sagar1, Gayathri S. Singaraju1, Rahul Dani, Naimat K. Bari, Athi N. Naganathan*, Sabyasachi Rakshit* (2020); Biochem. J., Weakening of Interaction Networks with Aging in Tip-Link Proteins Induces Hearing Loss., 550, 43-48.
Therapeutic remedy to Age-related hearing-loss (ARHL) still remains myth in absence of biophysical models for aging. We, in search of biophysical model for ARHL, traced a single-point mutation, serine to proline, in tip-link protein that aggressively progresses the hearing-loss at early ages. We report a loss in the circular cross-correlated motions among intradomain β-strands that restore proteins from conformational deformations from sound stimuli with mutation, and may trigger ARHL with normal aging.
16. Ankush Garg, Jagadish Prasad Hazra, Malay Kumar Sannigrahi, Sabyasachi Rakshit*,Sharmistha Sinha* (2019); Biophys. J., Variable Mutations at the p53-R273 Oncogenic Hotspot Position Leads to Altered Properties.
15. Jagadish P. Hazra,Amin Sagar, Nisha Arora, Debadutta Deb, Simerpreet Kaur, and Sabyasachi Rakshit. (2019); BioChem. J. (Open Access) Broken force dispersal network in tip-links by the mutations at the Ca2+ -binding residues induces hearing-Loss. 476 (16): 2411-2425.
Mutations at the Ca2+ binding linker regions alter the force-propagation through the tip-links and promote the force-induced dissociation.
14. G. S. Singaraju, A. Kumar, J. S. Samuel, A. Sagar, J. P. Hazra, M. K. Sannigrahi, R. M. Yennamalli, Ashish and S. Rakshit. (2019); FEBS J.(Open Access) Structural basis of the strong cell‐cell junction formed by cadherin‐23. (BioRchiv; SneakPeak, 10.1111/febs.15141 )
A cartoon representation of cadherin-23 (CDH23) proteins that interact from opposing cell-surfaces and mediate the cell-cell junction. To highlight the difference in the interaction conformation from classical cadherins, we also represented the interaction conformation for classical E-cadherin.
13. Malay K. Sannigrahi, Sai Srinivas, Nilesh Deokate and Sabyasachi Rakshit. (2019); Mol. Oncology. Strong Aggregation-propensity of Cadherin-23 inhibit cell migration.
Cadherin-23 is uniformly expressed at the cell-boundaries of various tissues
Cadherin-23 mediated cell-cell junction hinders cancer cell-migration
12. Malay Kumar Sannigrahi, Sai Srinivas and Sabyasachi Rakshit. (2018), Advances in Experimental Medicine and Biology (Springer Books). The prospects of Cadherin-23 as a mediator of homophillic cell-cell adhesion. 1112:99-105.
Cadherin-23, a long non-classical cadherin is uniformly expressed in normal tissues and down-regulated in cancer.
11. Jagadish P. Hazra, Nisha Arora, Amin Sagar, Shwetha Srinivasan, Abhishek Chaudhuri, and Sabyasachi Rakshit. (2018); Biochem. J. (Cover Page) Force-activated catalytic pathway accelerates bacterial-adhesion against flow. 475 (16): 2611-2620.
Publications from Collaborations
4. S Rani, B Dasgupta, GK Bhati, K Tomar, S Rakshit, S Maiti . (2020), ChemBioChem. , Superior Proton Transfer Catalytic Promiscuity of Cytochrome C in Self‐organized Media.
3. Mandeep Singh,Ana Guzman-Aranguez, Afzal Hussain, Cheerneni S Srinivas, Indu P Kaur. (2019), Nanomedicine , Solid lipid nanoparticles for ocular delivery of isoniazid: evaluation, proof of concept and in vivo safety & kinetics.
2. Naimat K. Bari, G. Kumar, A. Bhatt, J.P.Hazra, A. Garg, Md. Ehsan Ali and Sharmistha Sinha. (2018) , ACS catal. (Just Accepted) Nanoparticle fabrication on Bacterial Microcompartment surface for the development of hybrid enzyme-inorganic catalyst.
1. Naimat K.Bari, Shaswat Barua, Ankush Garg, Malay K.Sannigrahi, Sharmistha Sinha. (2018) Cellulose-metallothionein matrix for metal binding. Carb. Pol. 192, 126-134.