Department of Biotechnology | Indian Institute Of Technology Madras , Chennai
team

Athi N. Naganathan

Professor

Ph.D., University of Maryland, USA

B.Tech., Anna University, Chennai

Block 2, BT 115

044 2257 4140

athi[at]iitm[.]ac[.]in

Lab: Block 2, BT 113

Lab: 044 2257 5120

Lab Website
Scopus
Google Scholar

  • Experimental Characterization of Protein Conformational Behavior
  • Modeling and Predicting Folding Landscapes using Statistical Models
  • Understanding Protein Folding and Dynamics through Coarse-Grained and All-Atom Molecular Simulations
  • Multi-Scale Exploration of Protein Conformational Ensembl

  1. Kannan, A., & Naganathan, A. N (2024). "Engineering the native ensemble to tune protein function: Diverse mutational strategies and interlinked molecular mechanisms", Current opinion in structural biology, 89, pp. 102940, DOI: 10.1016/j.sbi.2024.102940.
  2. Rajendran, D., Goyal, S., Chaurasiya, D. K., & Naganathan, A. N (2024). "Determinants of Unfolding Cooperativity and Binding Are Decoupled in a DNA Binding Domain", The journal of physical chemistry. B, 128(39), pp. 9341–9352, DOI: 10.1021/acs.jpcb.4c03895.
  3. Natarajan, L., De Sciscio, M. L., Nardi, A. N., Sekhar, A., Del Giudice, A., D'Abramo, M., & Naganathan, A. N (2024). "A finely balanced order-disorder equilibrium sculpts the folding-binding landscape of an antibiotic sequestering protein", Proceedings of the National Academy of Sciences of the United States of America, 121(20), pp. e2318855121, DOI: 10.1073/pnas.2318855121.
  4. Lukose, B., Maruno, T., Faidh, M. A., Uchiyama, S., & Naganathan, A. N (2024). "Molecular and thermodynamic determinants of self-assembly and hetero-oligomerization in the enterobacterial thermo-osmo-regulatory protein H-NS", Nucleic acids research, 52(5), pp. 2157–2173, DOI: 10.1093/nar/gkae090.
  5. Kannan, A., Chaurasiya, D. K., & Naganathan, A. N (2023). "Conflicting Interfacial Electrostatic Interactions as a Design Principle to Modulate Long-Range Interdomain Communication", ACS bio & med chem Au, 4(1), pp. 53–67, DOI: 10.1021/acsbiomedchemau.3c00047.