A5057549416- Protein Structure and Dynamics
- Enzyme Structure and Function
- Prion Diseases and Protein Misfolding
- Alzheimer's disease research and treatments
- Hemoglobin structure and function
- Neurological diseases and metabolism
- Trace Elements in Health
- Spectroscopy and Quantum Chemical Studies
- Protein Interaction Studies and Fluorescence Analysis
- RNA and protein synthesis mechanisms
- Proteins in Food Systems
- Photosynthetic Processes and Mechanisms
- Mass Spectrometry Techniques and Applications
- Advanced NMR Techniques and Applications
- Lipid Membrane Structure and Behavior
- Molecular spectroscopy and chirality
- Bacterial Genetics and Biotechnology
- Porphyrin Metabolism and Disorders
- Protein Kinase Regulation and GTPase Signaling
- Protein purification and stability
- DNA and Nucleic Acid Chemistry
- Heat shock proteins research
- Ion channel regulation and function
- Force Microscopy Techniques and Applications
- RNA Research and Splicing
Indian Institute of Science Education and Research Pune
2018-2024
Tata Institute of Fundamental Research
2013-2023
National Centre for Biological Sciences
2013-2023
Savitribai Phule Pune University
2018
University of California, Berkeley
2013
Indian Institute of Science Bangalore
1998-2012
University of Pennsylvania
2009
Stanford University
1990-2009
Stanford Medicine
1990-2009
Jawaharlal Nehru Centre for Advanced Scientific Research
1998
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThermodynamics of Denaturation Barstar: Evidence for Cold and Evaluation the Interaction with Guanidine HydrochlorideVishwas R. Agashe Jayant B. UdgaonkarCite this: Biochemistry 1995, 34, 10, 3286–3299Publication Date (Print):March 1, 1995Publication History Published online1 May 2002Published inissue 1 March 1995https://doi.org/10.1021/bi00010a019Request reuse permissionsArticle Views584Altmetric-Citations157LEARN ABOUT THESE METRICSArticle Views...
Pulsed hydrogen exchange (2H-1H) is used to characterize the folding process of ribonuclease A (disulfide bonds intact). The results show one principal early intermediate (I1), which formed rapidly after start and whose proton-exchange properties change with time folding. All probes that are bonded within beta-sheet native protected in I1. Thus, suggest cooperatively. initial protection factors between 10 100, but they increase exceed 1000 at 400 msec from only moderately stable when it...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSynthesis, photochemistry, and biological activity of a caged photolabile acetylcholine receptor ligandTracy Milburn, Norio Matsubara, Andrew P. Billington, Jayant B. Udgaonkar, Jeffery W. Walker, Barry K. Carpenter, Watt Webb, Jeffrey Marque, Winfried Denk, Cite this: Biochemistry 1989, 28, 1, 49–55Publication Date (Print):January 10, 1989Publication History Published online1 May 2002Published inissue 10 January...
The aggregation of the natively disordered protein, Tau, to form lesions called neurofibrillary tangles is a characteristic feature several neurodegenerative tauopathies. polyanion, heparin, commonly used as an inducer in studies Tau vitro, but there surprisingly no comprehensive model describing, quantitatively, all aspects heparin-induced reaction. In this study, rate constants and extents fibril formation by four repeat domain (Tau4RD) have been reproducibly determined over full range...
Little is known about how proteins begin to unfold. In particular, and when water molecules penetrate into the protein interior during unfolding, thereby enabling dissolution of specific structure, poorly understood. The hypothesis that native state expands initially a dry molten globule, in which tight packing interactions are broken, but whose hydrophobic core has not expanded sufficiently be able absorb molecules, very little experimental support. Here, we report our analysis earliest...
To investigate how the heterogeneity inherent in formation of worm-like amyloid fibrils by mouse prion protein is modulated a change aggregation conditions, as well to determine reaction leads structure, fibril at low pH was studied presence various salts. It shown that β-rich oligomers different sizes and structures are formed high NaCl concentrations, determined Fourier transfer infrared (FTIR) spectroscopy dynamic light scattering (DLS). The from concentrations also differ their internal...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTEquilibrium unfolding studies of barstar: Evidence for an alternative conformation which resembles a molten globuleRitu Khurana and Jayant B. UdgaonkarCite this: Biochemistry 1994, 33, 1, 106–115Publication Date (Print):January 11, 1994Publication History Published online1 May 2002Published inissue 11 January 1994https://pubs.acs.org/doi/10.1021/bi00167a014https://doi.org/10.1021/bi00167a014research-articleACS PublicationsRequest reuse...
The unfolding kinetics of many small proteins appears to be first order, when measured by ensemble-averaging probes such as fluorescence and circular dichroism. For one protein, monellin, it is shown here that hidden behind this deceptive simplicity a complexity becomes evident with the use experimental are able discriminate between different conformations in an ensemble structures. In study, monellin has been probed measurement changes distributions 4 intramolecular distances, using...
In the presence of acetylcholine, nicotinic acetylcholine receptor undergoes two rapid conformational changes: one in 1-ms time region, leading to formation a transmembrane channel and signal transmission between cells, other 100-ms an inactive "desensitized" form with altered ligand-binding properties. To determine properties that are relevant for opening transmission, we have developed cell-flow technique allows measurements be made cells prior desensitization. Here illustrate usefulness...
Designed stabilization of helix 2 the mouse prion protein is shown to lead an increase in global stability protein. Studies hydrogen exchange coupled mass spectrometry confirm that confined primarily 2, and it accounts for Importantly, such localized can completely inhibit its ability form oligomers slows down amyloid fibril formation.
Abstract Domain swapping is the process by which identical monomeric proteins exchange structural elements to generate dimers/oligomers. Although engineered domain a compelling strategy for protein assembly, its application has been limited due lack of simple and reliable design approaches. Here, we demonstrate that hydrophobic five-residue ‘cystatin motif’ (QVVAG) from domain-swapping Stefin B, when into solvent-exposed, tight surface loop between two β-strands prevents folding back upon...