1,278 research outputs found

    Laser Cooling of TeV Muons

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    We show that Compton scattering can be used to cool TeV-scale muon beams, and we derive analytical expressions for the equilibrium transverse angular spread, longitudinal energy spread, and power requirements. We find that a factor of a few thousand reduction in emittance is possible for a 3 TeV muon collider.Comment: 5 pages, 1 figure, contributed to the NuFAct'00 International Worksho

    CS 241-04: Computer Programming - II

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    The CS 241 course is a continuation of CS 240. The emphasis in CS 241 is on solving more complex problems using object oriented programming. Prerequisite: CS240. Students must register for both lecture and one laboratory section. 4 credit hours

    CEG 2170-01: Introduction to C Programming for Engineers

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    Basic engineering problem solving using the C programming language. Topics include loops, selection, input/output, files, functions, arrays, complex variables, pointers, structures, and dynamic memory. Students will learn how to approach solving problems in engineering and science; how to develop algorithms, using advanced techniques such as recursion, searching, sorting and linked lists, to solve those problems; and how to implement those algorithms in the C language

    CEG 220-01: Introduction to C Programming for Engineers

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    This course provides a general introduction to computers as a problem-solving tool using the C programming language. Emphasis is on algorithms and techniques useful to engineers. Topics include data representation, debugging, and program verification. 4 credit hours. Prerequisite: MTH 229 (Calculus I) or EGR 101 (Engineering Mathematics). The course includes a scheduled laboratory section for which you must register

    CS 240-02: Computer Programming I

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    Basic concepts of programming and programming languages are introduced. Emphasis is on structured programming and stepwise refinement. Prerequisite: MTH 130 or MPL 5

    Using the Fermilab Proton Source for a Muon to Electron Conversion Experiment

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    The Fermilab proton source is capable of providing 8 GeV protons for both the future long-baseline neutrino program (NuMI), and for a new program of low energy muon experiments. In particular, if the 8 GeV protons are rebunched and then slowly extracted into an external beamline, the resulting proton beam would be suitable for a muon-to-electron conversion experiment designed to improve on the existing sensitivity by three orders of magnitude. We describe a scheme for the required beam manipulations. The scheme uses the Accumulator for momentum stacking, and the Debuncher for bunching and slow extraction. This would permit simultaneous operation of the muon program with the future NuMI program, delivering 10^20 protons per year at 8 GeV for the muon program at the cost of a modest (~10%) reduction in the protons available to the neutrino program.Comment: 18 pages, 7 figure

    ESR of spin-labeled bacteriophage M13 coat protein in mixed phospholipid bilayers.

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    Bacteriophage M13 major coat protein was spin-labeled with a nitroxide derivative of iodoacetamide, preferentially at the single methionine that is located in the hydrophobic region of the protein. The spin-labeled protein was incorporated at different lipid-to-protein ratios in phospholipid bilayers composed of dimyristoylphosphatidylglycerol (DMPG), dimyristoylphosphatidylcholine (DMPC), or the 1:1 molar mixture of these lipids. Both conventional and saturation transfer (ST) ESR studies were performed to investigate the rotational motions of the protein over a large dynamic range. The conventional ESR spectra indicate that the mobility of the spin labelled protein in the lipid gel phase decreases in the order: DMPG > DMPC/DMPG (1:1) > DMPC. In the liquid crystalline phase, the largest mobility is found in DMPC/DMPG (1:1, mol/mol) mixtures, but the mobility is still greater in DMPG than in DMPC. The results are interpreted in terms of different degrees of protein aggregation in the different lipids. Segmental motion with rotational correlation times on the order of tens of nanoseconds, motional anisotropy, and spectral overlap complicate the analysis of the STESR spectra. An estimate of the size of the protein aggregates is found to be in the region of 85 monomer units. Removing the polar tails from the protein by proteolytic digestion results in an enhanced aggregation in the gel phase. In the liquid crystalline phase, the segmental wobbling mobility of the protein is increased relative to the native protein, whereas the overall rotational diffusion is not changed greatly
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