Effect of Fat and Casein Particles in Milk on the Scattering of Elliptically Polarized Light

In this article, we present an experimental approach to determine the milk fat content using scattered light intensity profiles. The elements of the scattering (Mueller) matrix have been shown to provide valuable information about variation of the optical properties of scattering particles. The scattering behavior of fat and casein in terms of the scattering matrix elements was experimentally determined for milk with varying fat levels ranging from 0.05 wt% (skim) to 3.20 wt% (whole). Three of the scattering Mueller matrix elements, specifically S11, S12/S11, and S33/S11, were found to be sensitive to the number of fat particles in milk. These results indicate that it should be possible to develop a reliable sensor based on the measurement of these scattering elements, which will allow for the development of a robust, in-line sensor to be used in food processing. In addition, an attempt was made to model the phenomena using a relatively simple approach based on single scattering with a size distribution. The disagreement between the model and experiments suggests that a more comprehensive model is needed which can account for multiple scattering

The Peptidyl Prolyl Isomerase Rrd1 Regulates the Elongation of RNA Polymerase II during Transcriptional Stresses

Rapamycin is an anticancer agent and immunosuppressant that acts by inhibiting the TOR signaling pathway. In yeast, rapamycin mediates a profound transcriptional response for which the RRD1 gene is required. To further investigate this connection, we performed genome-wide location analysis of RNA polymerase II (RNAPII) and Rrd1 in response to rapamycin and found that Rrd1 colocalizes with RNAPII on actively transcribed genes and that both are recruited to rapamycin responsive genes. Strikingly, when Rrd1 is lacking, RNAPII remains inappropriately associated to ribosomal genes and fails to be recruited to rapamycin responsive genes. This occurs independently of TATA box binding protein recruitment but involves the modulation of the phosphorylation status of RNAPII CTD by Rrd1. Further, we demonstrate that Rrd1 is also involved in various other transcriptional stress responses besides rapamycin. We propose that Rrd1 is a novel transcription elongation factor that fine-tunes the transcriptional stress response of RNAPII

A three-Dimensional Human Trunk Model for the Analysis of Respiratory Mechanics

Over the past decade, road safety research and impact biomechanics have strongly stimulated the development of anatomical human numerical models using the finite element (FE) approach. The good accuracy of these models, in terms of geometric definition and mechanical response, should now find new areas of application. We focus here on the use of such a model to investigate its potential when studying respiratory mechanics. The human body FE model used in this study was derived from the RADIOSS® HUMOS model. Modifications first concerned the integration and interfacing of a user-controlled respiratory muscular system including intercostal muscles, scalene muscles, the sternocleidomastoid muscle, and the diaphragm and abdominal wall muscles. Volumetric and pressure measurement procedures for the lungs and both the thoracic and abdominal chambers were also implemented. Validation of the respiratory module was assessed by comparing a simulated maximum inspiration maneuver to volunteer studies in the literature. Validation parameters included lung volume changes, rib rotations, diaphragm shape and vertical deflexion, and intra-abdominal pressure variation. The HUMOS model, initially dedicated to road safety research, could be turned into a promising, realistic 3D model of respiration with only minor modifications. Internal abdominal pressure, respiratory mechanics, diaphragm, numerical mode

Differential interactions of the formins INF2, mDia1, and mDia2 with microtubules

Three mammalian formins, although binding microtubules with high affinity, differ dramatically in their microtubule-binding mechanisms. In addition, the ability of one formin (mDia2) to bind actin is strongly inhibited by microtubules, whereas the ability of another formin (INF2) to bind microtubules is strongly inhibited by actin monomers