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Venkata S. Mandala

Oberlin College
Entry year: 2015

vmandala@mit.edu

Publications

1

G. W. Stull, M. J. Moore, V. S. Mandala, N. A. Douglas, H. R. Kates, X. Qi, S. F. Brockington, P. S. Soltis, D. E. Soltis, and M. A. Gitzendanner, “A targeted enrichment strategy for massively parallel sequencing of angiosperm plastid genomes”, Appl. Plant Sci. 1 (2), apps.1200497 (2013).

2

V. S. Mandala, S. J. Loewus, and M. A. Mehta, “Monintoring Cocrystal Formation via In Situ Solid-State NMR“, J. Phys. Chem. Lett. 5, 3340-3344 (2014).

3

V. S. Mandala, S. Liao, B. Kwon and M. Hong, “Structural Basis of Inward Rectification in the Influenza M2 Proton Channel from Solid-State NMR”,  J. Mol. Biol. 429, 2192-2210 (2017).

4

V. S. Mandala, J. K. Williams, and M. Hong, “Structure and Dynamics of Membrane Proteins from Solid-State NMR”, Annu. Rev. Biophys. 47, 201-222 (2018).

5

V. S. Mandala, M. D. Gelenter, M. Hong, “Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR”, J. Am. Chem. Soc.  140, 1514-1524 (2018).  doi: 10.1021/jacs.7b12464.

6

M.K. Roos$, V.S. Mandala$ and M. Hong, “Determination of Long-Range Distances by Fast Magic-Angle-Spinning Radiofrequency-Driven 19F-19F Dipolar Recoupling NMR”, J. Phys. Chem. B, 122 (40), 9302-9313 (2018). ($ indicates equal contribution)  

7

V.S. Mandala and M. Hong, “High-sensitivity protein solid-state NMR spectroscopy”, Curr. Opin. Struc. Biol., in press (2019).

8

V.S. Mandala, S.Y. Liao, M.D. Gelenter and M. Hong, “Backbone Conformation of the Influenza Virus B M2 Protein in Lipid Bilayers from Solid-State NMR”, Sci. Rep., 9, 3725 (2019).

9

A.A. Shcherbakov, V.S. Mandala and M. Hong, “High-Sensitivity Detection of Nanometer 1H-19F Distances for Protein Structure Determination by 1H-Detected Fast MAS NMR”, J. Phys Chem. B, 123, 4387-4391 (2019).

10

B. Kwon$, M. Roos$, V.S. Mandala, A.A. Shcherbakov, and M. Hong, “Elucidating Relayed Proton Transfer Through a His-Trp-His Triad of a Transmembrane Proton Channel by Solid-State NMR”, J. Mol. Biol., in press (2019).

11

M.D. Gelenter, K.J. Smith$, S.Y. Liao$, V.S. Mandala, A.J. Dregni, M.S. Lamm, Y. Tian, W. Xu, D.J. Pochan, T.J. Tucker, Y. Su, and M. Hong, “The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations”, Nat. Struct. Mol. Biol., 26, 592-598 (2019).

Featured in MIT NewsChemists discover structure of glucagon fibrils: Study may be a step toward shelf-stable versions of the hormone, which is used to control diabetes.

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