publications
2024
- Varghese, C. N., Jaladeep, A., & Sekhar, A. (2024). Measuring Hydroxyl Exchange Rates in Glycans Using a Synergistic Combination of Saturation Transfer and Relaxation Dispersion NMR. Journal of the American Chemical Society.
- Jain, S., & Sekhar, A. (2024). Transient excited states of the metamorphic protein Mad2 and their implications for function. Proteins: Structure, Function, and Bioinformatics.
- Kumar, A., Madhurima, K., Naganathan, A. N., Vallurupalli, P., & Sekhar, A. (2023). Probing excited state 1Hα chemical shifts in intrinsically disordered proteins with a triple resonance-based CEST experiment: Application to a disorder-to-order switch. Methods, 218, 198-209.
- Khandave, N. P., Sekhar, A., & Vallurupalli, P. (2023). Studying micro to millisecond protein dynamics using simple amide 15N CEST experiments supplemented with major-state R 2 and visible peak-position constraints. Journal of Biomolecular NMR, 77(4), 165-181.
- Madhurima, K., Nandi, B., Munshi, S., Naganathan, A. N., & Sekhar, A. (2023). Functional regulation of an intrinsically disordered protein via a conformationally excited state. Science advances, 9(26), eadh4591.
- Sekhar, A., & Vallurupalli, P. (2023). 15 Chemical Exchange. Two‐Dimensional (2D) NMR Methods, 435-460.
- Rajendran, D., Mitra, S., Oikawa, H., Madhurima, K., Sekhar, A., Takahashi, S., & Naganathan, A. N. (2022). Quantification of entropic excluded volume effects driving crowding-induced collapse and folding of a disordered protein. The journal of physical chemistry letters, 13(13), 3112-3120.
- Narayanan, V., Bobbili, K. B., Sivaji, N., Jayaprakash, N. G., Suguna, K., Surolia, A., & Sekhar, A. (2022). Structure and carbohydrate recognition by the nonmitogenic lectin horcolin. Biochemistry, 61(6), 464-478.
- Jain, S., & Sekhar, A. (2022). Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy. Journal of magnetic resonance open, 10, 100034.
- Jaladeep, A., Varghese, C. N., & Sekhar, A. (2021). Measuring radiofrequency fields in NMR spectroscopy using offset-dependent nutation profiles. Journal of Magnetic Resonance, 330, 107032.
- Madhurima, K., Nandi, B., & Sekhar, A. (2021). Metamorphic proteins: the Janus proteins of structural biology. Open biology, 11(4), 210012.
- Kumar, A., Narayanan, V., & Sekhar, A. (2019). Characterizing post-translational modifications and their effects on protein conformation using NMR spectroscopy. Biochemistry, 59(1), 57-73.
- Sekhar, A., & Kay, L. E. (2019). An NMR view of protein dynamics in health and disease. Annual review of biophysics, 48, 297-319.
- Munshi, S., Subramanian, S., Ramesh, S., Golla, H., Kalivarathan, D., Kulkarni, M., ... & Naganathan, A. N. (2019). Engineering order and cooperativity in a disordered protein. Biochemistry, 58(19), 2389-2397.
Representative publications (before IISc)
(these should give you an idea of the NMR methods we routinely employ in the lab)
1) Rosenzweig R*, Sekhar A*, Nagesh J and Kay L E "Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles" (2017) eLife, 6, e28030. (* equal contributors and joint corresponding authors) Link
2) Sekhar A, Rumfeldt J A O, Broom H R, Doyle C M, Sobering R E, Meiering E M and Kay L E "Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR Spectroscopy" (2016) Proc. Natl. Acad. Sci. U.S.A., 113, E6939-E6945. Link
3) Sekhar A*, Rosenzweig R*, Bouvignies G and Kay L E "Hsp70 biases the folding pathways of client proteins" (2016) Proc. Natl. Acad. Sci. U.S.A., 113, E2794-E2801. (* equal contributors) Link
4) Sekhar A*, Rosenzweig R*, Bouvignies G and Kay L E "Mapping the conformation of a client protein through the Hsp70 functional cycle" (2015) Proc. Natl. Acad. Sci. U.S.A., 112, 10395-10400. (* equal contributors and joint corresponding authors) Link
5) Sekhar A, Rumfeldt J A O, Broom H R, Doyle C M, Bouvignies G, Meiering E M and Kay L E "Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways" (2015) eLife, 4, e07296. (joint corresponding author) Link
6) Sekhar A and Kay L E "NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformations" (2013) Proc. Natl. Acad. Sci. U.S.A., 110, 12867-12874. (Review) Link
7) Sekhar A*, Vallurupalli P* and Kay L E "Defining a length scale for millisecond-timescale protein conformational exchange" (2013) Proc. Natl. Acad. Sci. U.S.A., 110, 11391-11396. (* joint corresponding authors) Link
For Ashok's full list of publications, please click here.
Link to Ashok's google scholar profile.
