• Publications
  • Influence
VDAC‐2: Mitochondrial outer membrane regulator masquerading as a channel?
The voltage‐dependent anion channels (VDACs) are the workforce of mitochondrial transport and as such are required for cellular metabolism. The elaborate interplay between mitochondria and theExpand
  • 17
  • 3
Modulating lipid dynamics and membrane fluidity to drive rapid folding of a transmembrane barrel
Lipid-protein interactions, critical for the folding, stability and function of membrane proteins, can be both of mechanical and chemical nature. Mechanical properties of lipid systems can beExpand
  • 42
  • 2
N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry*
Human voltage-dependent anion channel-2 (hVDAC-2) functions primarily as the crucial anti-apoptotic protein in the outer mitochondrial membrane, and additionally as a gated bidirectional metaboliteExpand
  • 24
  • 1
Cysteine Residues Impact the Stability and Micelle Interaction Dynamics of the Human Mitochondrial β-Barrel Anion Channel hVDAC-2
The anti-apoptotic 19-stranded transmembrane human voltage dependent anion channel isoform 2 (hVDAC-2) β-barrel stability is crucial for anion transport in mitochondria. The role of the unusuallyExpand
  • 14
  • 1
  • PDF
Cyclic AMP receptor protein regulates cspE, an early cold-inducible gene, in Escherichia coli.
cspE, a member of the cspA family of cold shock proteins in Escherichia coli, is an early cold-inducible protein. The nucleic acid melting ability and transcription antiterminator activity of CspEExpand
  • 13
  • 1
Modulation of Human Mitochondrial Voltage-dependent Anion Channel 2 (hVDAC-2) Structural Stability by Cysteine-assisted Barrel-lipid Interactions*
Background: Human VDAC isoform 2 is crucial for apoptosis regulation and cell survival. Results: Cys-less mutant displays significantly lowered unfolding free energy despite greater barrel rigidity.Expand
  • 40
Influence of Protein – Micelle Ratios and Cysteine Residues on the Kinetic Stability and Unfolding Rates of Human Mitochondrial VDAC-2
Delineating the kinetic and thermodynamic factors which contribute to the stability of transmembrane β-barrels is critical to gain an in-depth understanding of membrane protein behavior. HumanExpand
  • 19
  • PDF
Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans
Structural and biophysical characterization of transmembrane proteins that require sufficiently pure protein in high amounts are usually generated in large-scale preparations as inclusion bodiesExpand
  • 11
  • PDF
Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities
Voltage‐dependent anion channels (VDACs) are the gateway to mitochondrial processes, interlinking the cytosolic and mitochondrial compartments. The mitochondrion acts as a storehouse for cytochromeExpand
  • 12
Control of human VDAC-2 scaffold dynamics by interfacial tryptophans is position specific
Membrane proteins employ specific distribution patterns of amino acids in their tertiary structure for adaptation to their unique bilayer environment. The solvent-bilayer interface, in particular,Expand
  • 6