A5070534724- X-ray Diffraction in Crystallography
- Crystallization and Solubility Studies
- Crystallography and molecular interactions
- Alzheimer's disease research and treatments
- Extracellular vesicles in disease
- Organic Chemistry Cycloaddition Reactions
- Synthesis and Catalytic Reactions
- Circular RNAs in diseases
- Protein Structure and Dynamics
- Molecular spectroscopy and chirality
- Natural product bioactivities and synthesis
- Chemical Synthesis and Analysis
- Gold and Silver Nanoparticles Synthesis and Applications
- Synthesis and properties of polymers
- Ginger and Zingiberaceae research
- Synthesis and Reactivity of Heterocycles
- Amino Acid Enzymes and Metabolism
- PARP inhibition in cancer therapy
- Tea Polyphenols and Effects
- Dermatoglyphics and Human Traits
- Research on Leishmaniasis Studies
- Machine Learning in Bioinformatics
- Biochemical and Structural Characterization
- Human Health and Disease
- Biopolymer Synthesis and Applications
Indian Institute of Chemical Biology
1992-2019
Council of Scientific and Industrial Research
2014-2019
A gold nanoparticle exhibits strong absorption and emission due to its unique physical geometry surface plasmon resonance phenomena.
The potential of β,γ-unsaturated α-ketothioesters participating in hetero-Diels–Alder reaction has remained unexplored. We report herein the first study a ZnI2-catalyzed highly diastereoselective inverse electron demand with olefins to access substituted 3,4-dihydro-2H-pyrans. All reactions proceed cis-selectivity moderate excellent yields. Under similar conditions, terminal alkynes undergo direct conjugate 1,4-addition yield δ,ε-acetylenic α-ketothioesters. Furthermore, utility these...
Lysozyme, like many other well-folded globular proteins, under stressful conditions produces nanoscale oligomer assembly and amyloid-like fibrillar aggregates. With engaging Raman microscopy, we made a critical structural analysis of structures lysozyme obtained from hen egg white provided quantitative estimation protein secondary structure in different states its fibrillation. A strong amide I band at 1660 cm–1 N–Cα–C stretching ∼930 clearly indicated the presence substantial amount...
An amyloidogenic region (AR) in a protein sequence plays significant role aggregation and amyloid formation. We have investigated the complexity of AR that is present intrinsically disordered human proteins. More than 80% proteins databases (DisProt+IDEAL) contained one or more ARs. With decrease disorder, content was decreased. A probability density distribution analysis discrete sequences showed ∼8% residue average 8 residues long. The were high it seldom overlapped with low regions (LCR),...
Amyloid β (Aβ) peptide is present as a major component in amyloid plaque that one of the hallmarks Alzheimer's disease. The contains single tyrosine residue and Aβ has implication pathology disease progression. Current investigation revealed side chain attained two different critical stereo orientations dissimilar conformational states peptide. extended α-helical structure observed an apolar solvent or methanol/water mixture became disordered aqueous medium radius gyration decreased. In...
The proline residue in a protein sequence generates constraints to its secondary structure as the associated torsion angles become part of heterocyclic ring. It becomes more significant when two consecutive residues link via amide linkage and produce additional configurational constraint protein's folding stability. In current manuscript we have illustrated conformation preference novel dipeptide, (R)-tert-butyl 2-((S)-2-(methoxycarbonyl)pyrrolidine-1-carbonyl)pyrrolidine-1-carboxylate....
The antitumour effect of tea plant root extract (TRE) has been evaluated against a 3-methylcholanthrene (3-MC) induced solid tumour model in ICR mice. TRE inhibited the tumur weight and tumours were found to be non-necrotic. Superoxide dismutase (SOD), free radical scavenger, sera treated bearing mice was significantly increased while SOD level untreated animals low. Moreover, enhanced thiobarbituric acid reactive substance (TBARS) normalized upon treatment. © 1998 John Wiley & Sons, Ltd.
Oligomers and fibrils of protein peptides are implicated in memory storage, neurotransmission formation amyloid diseases. It is believed that partially misfolded/folded states trapped a certain conformation it eventually leads to larger more stable fibrillar aggregates. Recently, our laboratory demonstrated AdK-aggregate could be disaggregated by cyclophilin CyP (LdCyP) an isomerase- independent fashion, resulting reactivation [Ref. 1]. We also observed the elongated when lysozyme was...
Abstract Hydropyrans are prepared from ketothioesters and olefins by a highly cis‐selective Diels—Alder cycloaddition using ZnI 2 as the catalyst.