85 resultados para Electrostatics


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"Task 9R38-01-017-30. Contract DA 44-177-TC-652."

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Available on demand as hard copy or computer file from Cornell University Library.

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Originally published: Leipzig : B.C. Breitkopf, 1744.

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Mode of access: Internet.

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We give a theoretical treatment of the interaction of electronic excitations (excitions) in biomolecules and quantum dots with the surrounding polar solvent. Significant quantum decoherence occurs due to the interaction of the electric dipole moment of the solute with the fluctuating electric dipole moments of the individual molecules in the solvent. We introduce spin boson models which could be used to describe the effects. of decoherence on the quantum dynamics of biomolecules which undergo light-induced conformational change and on biomolecules or quantum dots which are coupled by Forster resonant energy transfer.

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We present a technique to measure the viscosity of microscopic volumes of liquid using rotating optical tweezers. The technique can be used when only microlitre (or less) sample volumes are available, for example biological or medical samples, or to make local measurements in complicated micro-structures such as cells. The rotation of the optical tweezers is achieved using the polarisation of the trapping light to rotate a trapped birefringent spherical crystal, called vaterite. Transfer of angular momentum from a circularly polarised beam to the particle causes the rotation. The transmitted light can then be analysed to determine the applied torque to the particle and its rotation rate. The applied torque is determined from the change in the circular polarisation of the beam caused by the vaterite and the rotation rate is used to find the viscous drag on the rotating spherical particle. The viscosity of the surrounding liquid can then be determined. Using this technique we measured the viscosity of liquids at room temperature, which agree well with tabulated values. We also study the local heating effects due to absorption of the trapping laser beam. We report heating of 50-70 K/W in the region of liquid surrounding the particle.

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Electrostatic interactions are of fundamental importance in determining the structure and stability of macromolecules. For example, charge-charge interactions modulate the folding and binding of proteins and influence protein solubility. Electrostatic interactions are highly variable and can be both favorable and unfavorable. The ability to quantify these interactions is challenging but vital to understanding the detailed balance and major roles that they have in different proteins and biological processes. Measuring pKa values of ionizable groups provides a sensitive method for experimentally probing the electrostatic properties of a protein.

pKa values report the free energy of site-specific proton binding and provide a direct means of studying protein folding and pH-dependent stability. Using a combination of NMR, circular dichroism, and fluorescence spectroscopy along with singular value decomposition, we investigated the contributions of electrostatic interactions to the thermodynamic stability and folding of the protein subunit of Bacillus subtilis ribonuclease P, P protein. Taken together, the results suggest that unfavorable electrostatics alone do not account for the fact that P protein is intrinsically unfolded in the absence of ligand because the pKa differences observed between the folded and unfolded state are small. Presumably, multiple factors encoded in the P protein sequence account for its IUP property, which may play an important role in its function.