Jayant B. Udgaonkar
professor
Biochemistry, Biophysics and Bioinformatics
National Centre for Biological Sciences
India
Biography
Jayant B. Udgaonkar is a professor in the department of Biochemistry, Biophysics and Bioinformatics from the National Centre for Biological Sciences.
Research Interest
Their recent work on protein folding and unfolding include (1) the demonstration that multiple pathways are available for the folding and unfolding of monellin and that switching between alternative pathways can occur with a change in folding or unfolding conditions; (2) the demonstration that the native state of the prion protein undergoes unusually high fluctuations, which makes it extremely malleable to structural change; (3) the demonstration that protein unfolding reactions can occur through intermediates with non-native interactions; and (4) the demonstration that protein unfolding proceeds through dry and wet globules and a solvated transition state. Highlights of our recent work on protein misfolding and aggregation include (1) the structural characterization of oligomeric intermediates and worm-like fibrils formed by the mouse prion protein, and the demonstration that these aggregates can perturb membrane structure; (2) the temporal dissection of the structural changes that occur during fibril formation by the prion protein; and (3) the demonstration of a secondary pathway for fibril formation by the tau protein, and the delineation of structural changes that occur during fibril formation.
Publications
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Sabareesan, A.T., and Udgaonkar, J.B. (2016). Pathogenic Mutations within the Disordered Palindromic Region of the Prion Protein Induce Structure Therein and Accelerate the Formation of Misfolded Oligomers. J. Mol. Biol. 428, 3935–3947.
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Malhotra, P., and Udgaonkar, J.B. (2016). Secondary Structural Change Can Occur Diffusely and Not Modularly during Protein Folding and Unfolding Reactions. J. Am. Chem. Soc. 138, 5866–5878.
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Goluguri, R.R., and Udgaonkar, J.B. (2016). Microsecond Rearrangements of Hydrophobic Clusters in an Initially Collapsed Globule Prime Structure Formation during the Folding of a Small Protein. J. Mol. Biol. 428, 3102–3117.
