19FNMR relaxation of buried tryptophan side chains suggest anisotropic rotational diffusion of the protein RfaH
Md Khushnood Alam , R. Aishwarya Bhuvaneshwari and Ishita Sengupta
J.Biomolecular NMR, 2024
Insights into the Structure and Dynamics of Proteins from19F Solution NMR Spectroscopy
Ishita Sengupta
Biochemistry,2024
Lineshape Analysis of19F NMR Monitored Chemical Denaturation of a Fold Switching Protein RfaH Reveals its Slow Folding Dynamics
R. Aishwarya Bhuvaneshwari, Anish Shivamani and Ishita Sengupta
J. Phys. Chem. B2024, 128, 2, 465-471
Illustrating Elementary NMR Concepts through Simple Interactive Python Programs
Sengupta; Ishita.
J. Chem. Educ. 2021, 98, 1673–1680.
Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein
Ishita Sengupta and Jayant B. Udgaonkar,
eLife, 8, e44698 (2019)
Salt-mediated oligomerization of the mouse prion protein monitored by real-time NMR
Ishita Sengupta, Suhas H. Bhate, Ranabir Das, and Jayant B. Udgaonkar,
Journal of Molecular Biology, 429 (12), 1852-1872 (2017)
Protein Structure Determination with Paramagnetic Solid-State NMR Spectroscopy
Ishita Sengupta, Philippe S. Nadaud, and Christopher P. Jaroniec,
Accounts of Chemical Research, 46 (9), 2117–2126 (2013)
Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy
Ishita Sengupta, Philippe S. Nadaud, Jonathan J. Helmus, Charles D. Schwieters and Christopher P. Jaroniec
Nature Chemistry, 4, 410–417 (2012)