Point-form relativistic quantum mechanics is applied to elastic electrondeuteron scattering. The deuteron is modeled using relativistic interactions that are scattering-equivalent to the nonrelativistic Argonne v 18 and Reid '93 interactions. A point-form spectator approximation (PFSA) is introduced to define a conserved covariant current in terms of single-nucleon form factors.The PFSA is shown to provide an accurate description of data up to momentum transfers of 0.5 GeV 2 , but falls below the data at higher momentum transfers. Results are sensitive to the nucleon form factor parameterization chosen, particularly to the neutron electric form factor.

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Background: KLF16 is the least characterized family member of recently described metabolic regulators.Results: We extensively characterize mechanisms of DNA binding and chromatin coupling used by KLF16 to regulate metabolic gene expression.Conclusion: KLF16 is a novel regulator of metabolic genes by regulatable coupling to Sin3-histone deacetylase complexes.Significance: This knowledge reveals key mechanisms used by KLF16 as a regulator of metabolic gene expression.

Computational methods designed to predict and visualize ligand protein binding interactions were used to characterize volatile anesthetic (VA) binding sites and unoccupied pockets within the known structures of VAs bound to serum albumin, luciferase, and apoferritin. We found that both the number of protein atoms and methyl hydrogen, which are within approximately 8 A of a potential ligand binding site, are significantly greater in protein pockets where VAs bind. This computational approach was applied to structures of calmodulin (CaM), which have not been determined in complex with a VA. It predicted that VAs bind to [Ca(2+)](4)-CaM, but not to apo-CaM, which we confirmed with isothermal titration calorimetry. The VA binding sites predicted for the structures of [Ca(2+)](4)-CaM are located in hydrophobic pockets that form when the Ca(2+) binding sites in CaM are saturated. The binding of VAs to these hydrophobic pockets is supported by evidence that halothane predominantly makes contact with aliphatic resonances in [Ca(2+)](4)-CaM (nuclear Overhauser effect) and increases the Ca(2+) affinity of CaM (fluorescence spectroscopy). Our computational analysis and experiments indicate that binding of VA to proteins is consistent with the hydrophobic effect and the Meyer-Overton rule.

We investigate the difference between those relativistic models based on interpreting a realistic nucleon-nucleon interaction as a perturbation of the square of a relativistic mass operator and those models that use the method of Kamada and Glöckle to construct an equivalent interaction to add to the relativistic mass operator. Although both models reproduce the phase shifts and binding energy of the corresponding non-relativistic model, they are not scattering equivalent. The example of elastic electron-deuteron scattering in the one-photon-exchange approximation is used to study the sensitivity of three-body observables to these choices. Our conclusion is that the differences in the predictions of the two models can be understood in terms of the different ways in which the relativistic and non-relativistic S-matrices are related. We argue that the mass squared method is consistent with conventional procedures used to fit the Lorentz-invariant cross section as a function of the laboratory energy.