Supriya Pratihar
Affiliations: | Max Planck Institute for Biophysical Chemistry, Göttingen, Göttingen, Niedersachsen, Germany |
Area:
Protein Dynamics, NMR, Biomolecular NMRGoogle:
"Supriya Pratihar"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| Ramakrishna V. Hosur | grad student | 2010-2012 | TIFR |
| Christian Griesinger | grad student | 2015-2021 | Max Planck Institute for Biophysical Chemistry |
| Hashim M. Al-Hashimi | post-doc | 2022- | Columbia |
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Publications
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| Luo Y, Pratihar S, Horste EH, et al. (2023) mRNA interactions with disordered regions control protein activity. Biorxiv : the Preprint Server For Biology |
| Chakrabarti KS, Olsson S, Pratihar S, et al. (2022) A litmus test for classifying recognition mechanisms of transiently binding proteins. Nature Communications. 13: 3792 |
| Reddy JG, Pratihar S, Ban D, et al. (2017) Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments. Journal of Biomolecular Nmr |
| Pratihar S, Sabo TM, Ban D, et al. (2016) Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G. Angewandte Chemie (International Ed. in English) |
| Chakrabarti KS, Ban D, Pratihar S, et al. (2016) High-power (1)H composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 269: 65-69 |
| Smith CA, Ban D, Pratihar S, et al. (2016) Allosteric switch regulates protein-protein binding through collective motion. Proceedings of the National Academy of Sciences of the United States of America |
| Smith CA, Ban D, Pratihar S, et al. (2015) Population shuffling of protein conformations. Angewandte Chemie (International Ed. in English). 54: 207-10 |
| Michielssens S, Peters JH, Ban D, et al. (2014) A designed conformational shift to control protein binding specificity. Angewandte Chemie (International Ed. in English). 53: 10367-71 |
| Chakraborty S, Pratihar S, Hosur RV. (2012) NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assembly. Plos One. 7: e30109 |