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C K Mitra

Publications and source records attributed to C K Mitra.

9 recordsLinked to original sources
PubMed1999

Modeling the surface phenomena in carbon paste electrodes by low frequency impedance and double-layer capacitance measurements.

Impedance and capacitance studies have been performed with covalently coupled Glucose oxidase (GOD) enzyme, covalently coupled flavin adenine dinucleotide (FAD), reconstituted GOD enzyme and blank carbon paste electrodes to study the changes in the electrochemical interfacial properties. Impedance studies were performed using a low frequency impedance technique and the electrochemical surface capacitance was measured by a pulse technique. We have attempted to fit the experimental values to an equivalent circuit model. The Randles' cell circuit with Warburg impedance modeled well the experimental values and the behavior of the enzyme electrodes. The individual components of the model were calculated and the parameters were explained. The blank paste electrode showed a constant phase element behavior.

Carbon↗
PubMed1996

Pair-preferences: a quantitative measure of regularities in protein sequences.

We present here the results obtained by applying several different methods to quantitatively measure regularities in protein sequences based on pair-preferences. We have studied the distribution of amino acid residues, singly as well as in pairs in a large data base and have attempted this task. We confirmed the existence of well-defined pair-preferences in proteins which were shown to be remarkably absent in simulated random sequences of similar amino acid distribution. The analysis of the sequences from the SWISS-PROT data base using simple statistical tests. Fourier analysis, fractal analysis and statistical thermodynamical tests were used to derive parameters to define a natural sequence. As a consequence of the existence of pair-preferences, parameters like fractal dimension (D), spectral exponent (beta), scaling parameter (H) and entropy (statistical) were found to be characteristic for natural sequences. For a reference state we chose a randomised state devoid of any pair-preference. The pair-preferences qualified well to be used as quantitative measures of regularities in protein sequences.

Algorithms↗
PubMed1993

Electrogenic property of Na+, K(+)-ATPase through computer simulation.

A computer simulation of the electrogenic nature of the membrane-bound Na+, K(+)-ATPase is presented. The model involves coupling two simulation systems for passive and active transports, using a minimum of empirical parameters, and studies the contribution of the pump to the membrane potential. The simulation results indicate that electrogenic active transport accelerates the restoration of the resting electrochemical gradients and contributes approximately 0.44-1.1 mV to the resting potential of the membrane, depending on the Na:K coupling ratio. The effect of membrane potential and the physical positioning of the enzyme from the passive transporting channel on the enzyme function is also presented. The validity of the model is checked by comparing our results with reported literature values.

Biological Transport↗
PubMed1991

Selectivity of ionic channels: as seen through computer simulation.

A theoretical approach has been attempted to study the selectivity of ionic channels in membranes. We predict the channel to behave as an allosteric enzyme and have different conformational states that can bind strongly or weakly to a particular ion. The kinetic equation derived for the channel has few empirical parameters like the allostery factor, the probability factor, binding affinity factor and the transporting rate factor, the later two giving an idea of the ion-ion interactions and ion-channel interactions. The equation is programmed for an IBM compatible personal computer in MS-FORTRAN and the simulation data has been analysed to explain selectivity of the channels to particular ion. The simulation results show that the ions smaller than the permeable ions tend to act as inhibitors, the amplitude depending on the concentrations of the ions and comparative transport rate of the ion in the channel. The program helps easy study of the different parameters on the conducting rate of the permeable ion through the channel which otherwise would demand intricate experimental set-ups.

Computer Simulation↗
PubMed1991

Photoproduction of hydrogen from sewage by immobilized cells of Chromatium species IA.

Immobilized cells of two Chromatium species produced hydrogen continuously for more than 160 hr in 60% and 80% sewage. One strain showing high optimum range of sulfide tolerance (up to 9 mM) produced more hydrogen in 80% sewage while the less sulfide tolerating strain (up to 6 mM) showed hydrogen photoproduction in 60% sewage. Cells were immobilized in alginate and stable hydrogen photoproduction was observed for more than one week. Appropriate strategy necessary for the treatment of sewage and similar industrial effluents for energy reclamation is discussed.

Chromatium↗
PubMed1990

Computer simulation of the kinetics of the sodium pump.

A simple kinetic model for the membrane-bound enzyme, 'Na+, K(+)-ATPase', is presented. An equation for the efflux of Na+ and influx of K+ is derived. This also explains multiple ligand binding of homospecies of these cations and competition between heterospecies of these cations. The equation is computed by a small BASIC program and its validity is sought by comparing the results with a few experimental data.

Computer Simulation↗
PubMed1981

Left-handed deoxyribonucleic acid double helix in solution.

Magnetic shielding constants were calculated for the synthetic deoxyribonucleic acid (DNA) double helix poly(dG-dC).poly(dG-dC) from the x, y, and z coordinates of Z-DNA of Rich and co-workers [Wang, A. H-J., Quigley, G. J., Kolpak, F. J., Crawford, J. L., van Boom, J. H., van der Marel, G., & Rich, A. (1979) Nature (London) 282, 680-686)] and B-DNA of Arnott & Hukins [Arnott, S., & Hukins, D. W. L. (1972) Biochem. Biophys. Res. Commun. 47, 1504-1509], taking into account the contribution to shielding from ring current effects and effects from the diamagnetic and paramagnetic components of the atomic magnetic anisotropy. Comparison of the calculated shielding values with the experimentally observed nuclear magnetic resonance shift data for poly(dG-dC).poly(dG-dC) in high salt solution shows striking agreement for Z-DNA and considerable deviation for B-DNA, indicating that this synthetic DNA double helix is high salt solution can assume the spatial configuration of the left-handed Z-DNA double helix known to occur in crystals.

DNA↗
PubMed1980

Conformational flexibility of the 3' acceptor end of transfer ribonucleic acid.

The intimate details of the conformational features and dynamics of the trinucleoside diphosphates CpCpA and ApCpC in aqueous solution have been arrived at by the complete analysis of their proton magnetic resonance spectra. In addition to the right-handed stacked species in which the phosphodiester torsions conform to the gauche-gauche domains, sugar puckers 3E, C4'-C5 approximately equal to 60 degrees, C5'-O5' approximately 180 degrees, C3'-O3' approximately equal to 205 degrees, and chi CN approximately equal to 40 degrees, the trimers display a variety of spatial configurations, an important one being a bulged configuration in which the central nucleotide unit is bulged out, enabling stacking interactions between the end units. It is further shown that the 3' acceptor end of tRNA, CpCpA, displays considerable flexibility for the terminal adenine nucleotide unit. Theoretical NMR calculations demonstrate that the predominant solution conformation does not conform to the CCA terminus of tRNA as reported by four independent crystallographic studies of tRNAPhe. It is shown that the preferred intramolecular order of CCA in solution is such that chi 1 = chi 2 = chi 3 = 40 degrees, all the three sugars are in 3E, psi 1 = psi 2 = psi 3 = 60 degrees, phi 2 and phi 3 = 170 and 180 degrees, respectively, phi 1 = phi 2' = 205 degrees, and omega 1/omega 1 and omega 2/omega 2' = 240/205 degrees and 295/265 degrees, respectively.

Base Sequence↗