Spectral Representation Theory for Dielectric Behavior of Nonspherical Cell Suspensions

Recent experiments revealed that the dielectric dispersion spectrum of fission yeast cells in a suspension was mainly composed of two sub-dispersions. The low-frequency sub-dispersion depended on the cell length, while the high-frequency one was independent of it. The cell shape effect was simulated by an ellipsoidal cell model but the comparison between theory and experiment was far from being satisfactory. Prompted by the discrepancy, we proposed the use of spectral representation to analyze more realistic cell models. We adopted a shell-spheroidal model to analyze the effects of the cell membrane. It is found that the dielectric property of the cell membrane has only a minor effect on the dispersion magnitude ratio and the characteristic frequency ratio. We further included the effect of rotation of dipole induced by an external electric field, and solved the dipole-rotation spheroidal model in the spectral representation. Good agreement between theory and experiment has been obtained.Comment: 19 pages, 5 eps figure

3.5Å cryoEM structure of hepatitis B virus core assembled from full-length core protein.

The capsid shell of infectious hepatitis B virus (HBV) is composed of 240 copies of a single protein called HBV core antigen (HBc). An atomic model of a core assembled from truncated HBc was determined previously by X-ray crystallography. In an attempt to obtain atomic structural information of HBV core in a near native, non-crystalline environment, we reconstructed a 3.5Å-resolution structure of a recombinant core assembled from full-length HBc by cryo electron microscopy (cryoEM) and derived an atomic model. The structure shows that the 240 molecules of full-length HBc form a core with two layers. The outer layer, composed of the N-terminal assembly domain, is similar to the crystal structure of the truncated HBc, but has three differences. First, unlike the crystal structure, our cryoEM structure shows no disulfide bond between the Cys61 residues of the two subunits within the dimer building block, indicating such bond is not required for core formation. Second, our cryoEM structure reveals up to four more residues in the linker region (amino acids 140-149). Third, the loops in the cryoEM structures containing this linker region in subunits B and C are oriented differently (~30° and ~90°) from their counterparts in the crystal structure. The inner layer, composed of the C-terminal arginine-rich domain (ARD) and the ARD-bound RNAs, is partially-ordered and connected with the outer layer through linkers positioned around the two-fold axes. Weak densities emanate from the rims of positively charged channels through the icosahedral three-fold and local three-fold axes. We attribute these densities to the exposed portions of some ARDs, thus explaining ARD's accessibility by proteases and antibodies. Our data supports a role of ARD in mediating communication between inside and outside of the core during HBV maturation and envelopment

Probing WL′WHW^\prime_L WH and WR′WHW^\prime_R W H Interaction at LHC

Many new physics models predict the existence of TeV-scale charged gauge boson $W^\prime$ together with Higgs boson(s). We study the $W^\prime WH$ interaction and explore the angular distribution of charged lepton to distinguish $W_R^\prime WH$ from $W_L^\prime WH$ in $pp\to HW\to b \bar b l \nu$ process at the LHC. It is found that a new type forward-backward asymmetry($A_{FB}$) relating to the angle between the direction of the charged lepton in $W$ rest frame and that of the reconstructed $W^\prime$ in laboratory frame is useful to investigate the properties of $W^\prime W H$ interaction. We analyze the Standard Model backgrounds and develop a set of cuts to highlight the signal and suppress the backgrounds at LHC. We find that $A_{FB}$ can reach 0.03(-0.07) for $W_R^\prime$($W_L^\prime$) production at $\sqrt{S}=14$ TeV