Moscow State University

About: Moscow State University is a education organization based out in Moscow, Russia. It is known for research contribution in the topics: Laser & Population. The organization has 66747 authors who have published 123358 publications receiving 1753995 citations. The organization is also known as: MSU & Lomonosov Moscow State University.

Liquid-crystalline ordering in the solution of long persistent chains

Abstract: The orientational ordering in the solution of long persistent macromolecules is studied by means of the Onsager method. It is shown that the liquid-crystalline transition occurs at significantly higher concentrations and that the order parameter at the transition point is much smaller than for the model of freely-jointed segments. It is concluded that the orientational ordering in the solutions of semiflexible chains depends essentially on the flexibility distribution along the chain contour.

Observation of sequential Υ suppression in PbPb collisions

Abstract: The suppression of the individual Υ(nS) states in PbPb collisions with respect to their yields in pp data has been measured. The PbPb and pp data sets used in the analysis correspond to integrated luminosities of 150 μb^(-1) and 230 nb^(-1), respectively, collected in 2011 by the CMS experiment at the LHC, at a center-of-mass energy per nucleon pair of 2.76 TeV. The Υ(nS) yields are measured from the dimuon invariant mass spectra. The suppression of the Υ(nS) yields in PbPb relative to the yields in pp, scaled by the number of nucleon-nucleon collisions, R_(AA), is measured as a function of the collision centrality. Integrated over centrality, the R_(AA) values are 0.56±0.08(stat)±0.07(syst), 0.12±0.04(stat)±0.02(syst), and lower than 0.10 (at 95% confidence level), for the Υ(1S), Υ(2S), and Υ(3S) states, respectively. The results demonstrate the sequential suppression of the Υ(nS) states in PbPb collisions at LHC energies.

Kindling fluorescent proteins for precise in vivo photolabeling

Abstract: Photobleaching of green fluorescent protein (GFP) is a widely used approach for tracking the movement of subcellular structures and intracellular proteins1,2,3. Although photobleaching is a powerful technique, it does not allow direct tracking of an object's movement and velocity within a living cell. Direct tracking becomes possible only with the introduction of a photoactivated fluorescent marker. A number of previous studies have reported optically induced changes in the emission spectra of fluorescent proteins4,5,6,7. However, the ideal photoactivated fluorescent marker should be a nonfluorescent tag capable of “switching on” (i.e., becoming fluorescent) in response to irradiation by light of a particular wavelength, intensity, and duration. In this report, we generated a mutant of Anemonia sulcata chromoprotein asCP8. The mutant protein is capable of unique irreversible photoconversion from the nonfluorescent to a stable bright-red fluorescent form (“kindling”). This “kindling fluorescent protein” (KFP1) can be used for precise in vivo photolabeling to track the movements of cells, organelles, and proteins. We used KFP1 for in vivo cell labeling in mRNA microinjection assays to monitor Xenopus laevis embryo development and to track mitochondrial movement in mammalian cells.

Force production by disassembling microtubules.

Abstract: Microtubules (MTs) are important components of the eukaryotic cytoskeleton: they contribute to cell shape and movement, as well as to the motions of organelles including mitotic chromosomes. MTs bind motor enzymes that drive many such movements, but MT dynamics can also contribute to organelle motility. Each MT polymer is a store of chemical energy that can be used to do mechanical work, but how this energy is converted to motility remains unknown. Here we show, by conjugating glass microbeads to tubulin polymers through strong inert linkages, such as biotin-avidin, that depolymerizing MTs exert a brief tug on the beads, as measured with laser tweezers. Analysis of these interactions with a molecular-mechanical model of MT structure and force production shows that a single depolymerizing MT can generate about ten times the force that is developed by a motor enzyme; thus, this mechanism might be the primary driving force for chromosome motion. Because even the simple coupler used here slows MT disassembly, physiological couplers may modulate MT dynamics in vivo.