A5013775301- Nanopore and Nanochannel Transport Studies
- Ion-surface interactions and analysis
- Carbon Nanotubes in Composites
- Force Microscopy Techniques and Applications
- RNA and protein synthesis mechanisms
- Microfluidic and Capillary Electrophoresis Applications
- Enzyme Structure and Function
- Molecular Sensors and Ion Detection
- Membrane-based Ion Separation Techniques
- Electrochemical sensors and biosensors
- Molecular Spectroscopy and Structure
- Lipid Membrane Structure and Behavior
- Electrostatics and Colloid Interactions
- Protein Structure and Dynamics
- Spectroscopy and Quantum Chemical Studies
- Advanced Chemical Physics Studies
- DNA and Nucleic Acid Chemistry
- RNA Research and Splicing
- Fuel Cells and Related Materials
- stochastic dynamics and bifurcation
- Surface Chemistry and Catalysis
- Carbon and Quantum Dots Applications
- Advanced biosensing and bioanalysis techniques
Banaras Hindu University
2023-2024
Indian Institute of Technology BHU
2024
Northeastern University
2020-2023
University of Massachusetts Amherst
2021
University of Illinois Urbana-Champaign
2013
Significance Can localized electric fields drive the complete unfolding of a protein molecule? Protein prior to its translocation through nanopore constriction is an important step in transport across biological membranes and also nanopore-based sequencing. We studied here electric-field–driven behavior model (cyt c ) nanopores diameters ranging from 1.5 5.5 nm. These single-molecule measurements show that at can select both partially fully unfolded conformations. Zero-field free energy gaps...
Conformational transitions of proteins are governed by chemical kinetics, often toggled passage through an activated state separating two conformational ensembles. The time a protein the can be too fast to detected single-molecule experiments without aid viscogenic agents. Here, we use high-bandwidth nanopore measurements resolve microsecond-duration that occur between states individual molecules partly blocking pore current. We measure transition folded and unfolded two-state λ6-85 mutant...
Translocation of proteins is correlated with structural fluctuations that access conformational states higher in free energy than the folded state. We use electric fields at solid-state nanopore to control relative and occupancy different protein single-molecule level. The change conformations as a function field gives rise shifts measured distributions ionic current blockades residence times. probe statistics times for three mutants <mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML"...
Rosette nanotubes (RNTs) are a class of materials formed by molecular self-assembly fused guanine–cytosine base (G∧C base). An important feature these self-assembled is their precise atomic structure, intriguing for rational design and optimization as synthetic transmembrane porins. Here, we present experimental observations ion transport across 1.1 nm inner diameter RNT porins (RNTPs) various lengths in the range 5–200 nm. In typical experiment, custom lipophilic RNTPs were first inserted...
Nanopore translocation can discriminate the RNA fibers differing from one another in frequency of branches.
Creating an analytical probe to track extremely mutagenic picric acid (PA) is essential for human health and the environment. Here, we developed a straightforward quick fluorescence method utilizing 3-aminopropyltrimethoxysilane (3-APTMS)-functionalized curcumin carbon quantum dots (CQDs) fast selective detection of PA. Solvothermal carbonization functionalization with 3-APTMS were used create multifunctional CQDs, which then characterized using UV-vis spectroscopy, Fourier transform...
Local vibrational coupling models predict that intramolecular energy redistribution (IVR) is not completely statistical even at the dissociation limit of polyatomic molecules. Thus states protected from IVR and rapid form regular progressions can be assigned quantum numbers. We previously observed such in spectra molecule SCCl2, but a discrepancy density remained between theory experiment. Here we show gap closed by observing assigning additional transitions above carefully analyzing...
Knotted proteins are rare but important species, yet how their complex topologies affect physical properties is not fully understood. Here we combine single molecule nanopore experiments and all-atom MD simulations to study the electric-field-driven unfolding during translocation through a model pore of individual protein knots for methylating tRNA. One these shows an unusual behavior that resembles electrons hopping between two potential surfaces: as electric driving reaction increased,...
Abstract Many small proteins move across cellular compartments through narrow pores. In order to thread a protein constriction, free energy must be overcome either deform or completely unfold the protein. principle, diameter of pore, along with effective driving force for unfolding protein, as well its barrier translocation, should critical factors that govern whether process proceeds via squeezing, unfolding/threading, both. To probe this well-established system, we studied...
ABSTRACT We have investigated how a pair of oppositely charged macromolecules can be driven by an electric field to form polyelectrolyte complex inside nanopore. To observe and isolate individual pair, model protein nanopore, embedded in artificial phospholipid membrane, allowing compartmentalization ( cis / trans ) is employed. A polyanion the polycation compartments are subjected electrophoretic capture pore. find that measured ionic current across pore has distinguishable signature...