A5032119214- Nanopore and Nanochannel Transport Studies
- Ion-surface interactions and analysis
- Microfluidic and Capillary Electrophoresis Applications
- RNA Research and Splicing
- RNA and protein synthesis mechanisms
- Advanced biosensing and bioanalysis techniques
- Engineering Technology and Methodologies
- thermodynamics and calorimetric analyses
- Electrostatics and Colloid Interactions
- Manufacturing Process and Optimization
- Advanced machining processes and optimization
- RNA modifications and cancer
- RNA Interference and Gene Delivery
- Fuel Cells and Related Materials
- Neurogenetic and Muscular Disorders Research
- Electrochemical Analysis and Applications
- Genomics and Chromatin Dynamics
- Lipid Membrane Structure and Behavior
- Experimental and Theoretical Physics Studies
- Geophysical and Geoelectrical Methods
- Advanced Thermodynamics and Statistical Mechanics
- Single-cell and spatial transcriptomics
- Carbon Nanotubes in Composites
- Advanced Proteomics Techniques and Applications
University of Illinois Urbana-Champaign
2019-2023
Indian Institute of Science Bangalore
2017
The chemical nature and precise position of posttranslational modifications (PTMs) in proteins or peptides are crucial for various severe diseases, such as cancer. State-of-the-art PTM diagnosis is based on elaborate costly mass-spectrometry immunoassay-based approaches, which limited selectivity specificity. Here, we demonstrate the use a protein nanopore to differentiate peptides─derived from human histone H4 protein─of identical mass according positions acetylated methylated lysine...
Proteins containing intrinsically disordered regions are integral parts of the cellular signaling pathways and common components biological condensates. Point mutations in protein sequence, genetic at birth or acquired through aging, can alter properties condensates, marking onset neurodegenerative diseases such as ALS dementia. While all-atom molecular dynamics method can, principle, elucidate conformational changes that arise from point mutations, applications this to condensate systems is...
Nanopore sensing has emerged as a versatile approach to detection and identification of biomolecules. Presently, researchers rely on experience intuition for choosing or modifying the nanopores detect target analyte. The field would greatly benefit from computational method that could relate atomic-scale geometry analytes blockade nanopore currents they produce. Existing methods are either computationally too expensive be used routinely in experimental laboratories not sensitive enough...
The detection of analytes and the sequencing DNA using biological nanopores have seen major advances over recent years. analysis proteins peptides with nanopores, however, is complicated by complex physicochemical structure polypeptides lack understanding mechanism capture recognition nanopores. In this work, we show that introducing aromatic amino acids at precise positions within lumen α-helical fragaceatoxin C (FraC) increased frequency largely improved discrimination among similar size....
Nanopore sequencing of nucleic acids has an illustrious history innovations that eventually made commercial nanopore possible. Nevertheless, the present technology leaves much room for improvement, especially with respect to accuracy raw reads and detection nucleotide modifications. Double-nanopore sequencing—an approach where a DNA molecule is pulled back forth by tug-of-war two nanopores—could potentially improve single-molecule read modification offering multiple same fragment. One...
Proteins containing intrinsically disordered regions are integral components of the cellular signaling pathways and common biological condensates. Point mutations in protein sequence, genetic at birth or acquired through aging, can alter properties condensates, marking onset neurodegenerative diseases such as ALS dementia. While all-atom molecular dynamics method can, principle, elucidate conformational changes responsible for aging condensate, applications this to condensate systems is...
Posttranslational modifications (PTMs) of proteins are crucial for cellular function but pose analytical problems, especially in distinguishing chemically identical PTMs at different nearby locations within the same protein. Current methods, such as liquid chromatography-tandem mass spectrometry, technically tantamount to de novo protein sequencing 1 . Nanopore techniques may provide a more efficient solution, applying concepts nanopore DNA strand still faces fundamental problems 2–4 Here,...