Attenuation of Noise and Vibration Caused by Underground Trains

Abstract Tunnels are used to convey transportation in dense urban areas, especially by underground trains. Underground trains radiate noise and vibration by airborne sound and by transmission of vibration through the rails to the surrounding ground. The acoustic wave propagates through the ground, being transmitted by soil-structure interactions to nearby buildings. The transportation induced vibrations add to the static and other types of loads, and their specific spectral features are well distinguished and perceived as nuisance to people. The disturbing effect caused by these solid borne vibrations can be significantly mitigated by soil replacement of the material under the rails. This technique, which was described in previous publications by the authors, is further developed and analyzed here by modeling and numerical analysis, for underground applications. Illustrative examples show through spectral analysis the role of soil replacement, avoiding sound bridges. In this context, the required thickness of the soil replacement layer was considered. It is shown that a 0.5 m thick layer may be sufficient for most practical purposes

The revival-collapse phenomenon in the quadrature field components of the two-mode multiphoton Jaynes-Cummings model

In this paper we consider a system consisting of a two-level atom in an excited state interacting with two modes of a radiation field prepared initially in $l$-photon coherent states. This system is described by two-mode multiphoton (, i.e., $k_1, k_2$) Jaynes-Cummings model (JCM). For this system we investigate the occurrence of the revival-collapse phenomenon (RCP) in the evolution of the single-mode, two-mode, sum and difference quadrature squeezing. We show that there is a class of states for which all these types of squeezing exhibit RCP similar to that involved in the corresponding atomic inversion. Also we show numerically that the single-mode squeezing of the first mode for $(k_1,k_2)=(3,1)$ provides RCP similar to that of the atomic inversion of the case $(k_1,k_2)=(1,1)$, however, sum and difference squeezing give partial information on that case. Moreover, we show that single-mode, two-mode and sum squeezing for the case $(k_1,k_2)=(2,2)$ provide information on the atomic inversion of the single-mode two-photon JCM. We derive the rescaled squeezing factors giving accurate information on the atomic inversion for all cases. The consequences of these results are that the homodyne and heterodyne detectors can be used to detect the RCP for the two-mode JCM.Comment: 18 pages, 6 figure

On being a good Bayesian

Bayesianism is fast becoming the dominant paradigm in archaeological chronology construction. This paradigm shift has been brought about in large part by widespread access to tailored computer software which provides users with powerful tools for complex statistical inference with little need to learn about statistical modelling or computer programming. As a result, we run the risk that such software will be reduced to the status of black boxes. This would be a dangerous position for our community since good, principled use of Bayesian methods requires mindfulness when selecting the initial model, defining prior information, checking the reliability and sensitivity of the software runs and interpreting the results obtained. In this article, we provide users with a brief review of the nature of the care required and offer some comments and suggestions to help ensure that our community continues to be respected for its philosophically rigorous scientific approach

Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels

Comparison of the crystal structures of the KcsA and MthK potassium channels suggests that the process of opening a K+ channel involves pivoted bending of the inner pore-lining helices at a highly conserved glycine residue. This bending motion is proposed to splay the transmembrane domains outwards to widen the gate at the “helix-bundle crossing”. However, in the inwardly rectifying (Kir) potassium channel family, the role of this “hinge” residue in the second transmembrane domain (TM2) and that of another putative glycine gating hinge at the base of TM2 remain controversial. We investigated the role of these two positions in heteromeric Kir4.1/Kir5.1 channels, which are unique amongst Kir channels in that both subunits lack a conserved glycine at the upper hinge position. Contrary to the effect seen in other channels, increasing the potential flexibility of TM2 by glycine substitutions at the upper hinge position decreases channel opening. Furthermore, the contribution of the Kir4.1 subunit to this process is dominant compared to Kir5.1, demonstrating a non-equivalent contribution of these two subunits to the gating process. A homology model of heteromeric Kir4.1/Kir5.1 shows that these upper “hinge” residues are in close contact with the base of the pore α-helix that supports the selectivity filter. Our results also indicate that the highly conserved glycine at the “lower” gating hinge position is required for tight packing of the TM2 helices at the helix-bundle crossing, rather than acting as a hinge residue

Selective Phosphorylation Modulates the PIP2 Sensitivity of the CaM-SK Channel Complex

Phosphatidylinositol bisphosphate (PIP2) regulates the activities of many membrane proteins including ion channels through direct interactions. However, the affinity of PIP2 is so high for some channel proteins that its physiological role as a modulator has been questioned. Here we show that PIP2 is an important cofactor for activation of small conductance Ca2+-activated potassium channels (SK) by Ca2+-bound calmodulin (CaM). Removal of the endogenous PIP2 inhibits SK channels. The PIP2-binding site resides at the interface of CaM and the SK C-terminus. We further demonstrate that the affinity of PIP2 for its target proteins can be regulated by cellular signaling. Phosphorylation of CaM T79, located adjacent to the PIP2-binding site, by Casein Kinase 2 reduces the affinity of PIP2 for the CaM-SK channel complex by altering the dynamic interactions among amino acid residues surrounding the PIP2-binding site. This effect of CaM phosphorylation promotes greater channel inhibition by G-protein-mediated hydrolysis of PIP2

Enantioselective Protein-Sterol Interactions Mediate Regulation of Both Prokaryotic and Eukaryotic Inward Rectifier K+ Channels by Cholesterol

Cholesterol is the major sterol component of all mammalian cell plasma membranes and plays a critical role in cell function and growth. Previous studies have shown that cholesterol inhibits inward rectifier K+ (Kir) channels, but have not distinguished whether this is due directly to protein-sterol interactions or indirectly to changes in the physical properties of the lipid bilayer. Using purified bacterial and eukaryotic Kir channels reconstituted into liposomes of controlled lipid composition, we demonstrate by 86Rb+ influx assays that bacterial Kir channels (KirBac1.1 and KirBac3.1) and human Kir2.1 are all inhibited by cholesterol, most likely by locking the channels into prolonged closed states, whereas the enantiomer, ent-cholesterol, does not inhibit these channels. These data indicate that cholesterol regulates Kir channels through direct protein-sterol interactions likely taking advantage of an evolutionarily conserved binding pocket

PIP2-Binding Site in Kir Channels: Definition by Multiscale Biomolecular Simulations†

Phosphatidylinositol bisphosphate (PIP(2)) is an activator of mammalian inwardly rectifying potassium (Kir) channels. Multiscale simulations, via a sequential combination of coarse-grained and atomistic molecular dynamics, enabled exploration of the interactions of PIP(2) molecules within the inner leaflet of a lipid bilayer membrane with possible binding sites on Kir channels. Three Kir channel structures were investigated: X-ray structures of KirBac1.1 and of a Kir3.1-KirBac1.3 chimera and a homology model of Kir6.2. Coarse-grained simulations of the Kir channels in PIP(2)-containing lipid bilayers identified the PIP(2)-binding site on each channel. These models of the PIP(2)-channel complexes were refined by conversion to an atomistic representation followed by molecular dynamics simulation in a lipid bilayer. All three channels were revealed to contain a conserved binding site at the N-terminal end of the slide (M0) helix, at the interface between adjacent subunits of the channel. This binding site agrees with mutagenesis data and is in the proximity of the site occupied by a detergent molecule in the Kir chimera channel crystal. Polar contacts in the coarse-grained simulations corresponded to long-lived electrostatic and H-bonding interactions between the channel and PIP(2) in the atomistic simulations, enabling identification of key side chains

Relationship between the atomic inversion and Wigner function for multiphoton multimode Jaynes-Cummings model

In this paper we consider multimode multiphoton Jaynes-Cummings model, which consists of a two-level atom, initially prepared in an excited atomic state, interacting with $N$ modes of electromagnetic field prepared in general pure quantum states. For this system we show that under certain conditions the evolution of the Wigner function at the phase space origin provides direct information on the corresponding atomic inversion. This relation is also valid even if the system includes Kerr-like nonlinearity, Stark shift effect, different types of the initial atomic state as well as moving atom. Furthermore, based on this fact we discuss for the single-mode case the possibility of detecting the atomic inversion by means of techniques similar to those used for Wigner function.Comment: 19 pages, 4 figure

TRAF4 is a novel phosphoinositide-binding protein modulating tight junctions and favoring cell migration

Tumor necrosis factor (TNF) receptor-associated factor 4 (TRAF4) is frequently overexpressed in carcinomas, suggesting a specific role in cancer. Although TRAF4 protein is predominantly found at tight junctions (TJs) in normal mammary epithelial cells (MECs), it accumulates in the cytoplasm of malignant MECs. How TRAF4 is recruited and functions at TJs is unclear. Here we show that TRAF4 possesses a novel phosphoinositide (PIP)-binding domain crucial for its recruitment to TJs. Of interest, this property is shared by the other members of the TRAF protein family. Indeed, the TRAF domain of all TRAF proteins (TRAF1 to TRAF6) is a bona fide PIP-binding domain. Molecular and structural analyses revealed that the TRAF domain of TRAF4 exists as a trimer that binds up to three lipids using basic residues exposed at its surface. Cellular studies indicated that TRAF4 acts as a negative regulator of TJ and increases cell migration. These functions are dependent from its ability to interact with PIPs. Our results suggest that TRAF4 overexpression might contribute to breast cancer progression by destabilizing TJs and favoring cell migration