The Tuning System for the HIE-ISOLDE High-Beta Quarter Wave Resonator

A new linac using superconducting quarter-wave resonators (QWR) is under construction at CERN in the framework of the HIE-ISOLDE project. The QWRs are made of niobium sputtered on a bulk copper substrate. The working frequency at 4.5 K is 101.28 MHz and they will provide 6 MV/m accelerating gradient on the beam axis with a total maximum power dissipation of 10 W on cavity walls. A tuning system is required in order to both minimize the forward power variation in beam operation and to compensate the unavoidable uncertainties in the frequency shift during the cool-down process. The tuning system has to fulfil a complex combination of RF, structural and thermal requirements. The paper presents the functional specifications and details the tuning system RF and mechanical design and simulations. The results of the tests performed on a prototype system are discussed and the industrialization strategy is presented in view of final production.Comment: 5 pages, The 16th International Conference on RF Superconductivity (SRF2013), Paris, France, Sep 23-27, 201

Multiplicity Distributions and Rapidity Gaps

I examine the phenomenology of particle multiplicity distributions, with special emphasis on the low multiplicities that are a background in the study of rapidity gaps. In particular, I analyze the multiplicity distribution in a rapidity interval between two jets, using the HERWIG QCD simulation with some necessary modifications. The distribution is not of the negative binomial form, and displays an anomalous enhancement at zero multiplicity. Some useful mathematical tools for working with multiplicity distributions are presented. It is demonstrated that ignoring particles with pt<0.2 has theoretical advantages, in addition to being convenient experimentally.Comment: 24 pages, LaTeX, MSUHEP/94071

Determination of Rapid-Equilibrium Kinetic Parameters of Ordered and Random Enzyme-Catalyzed Reaction A + B = P + Q

This article deals with the rapid-equilibrium kinetics of the forward and reverse reactions together for the ordered and random enzyme-catalyzed A + B = P + Q and emphasizes the importance of reporting the values of the full set of equilibrium constants. Equilibrium constants that are not in the rate equation can be calculated for random mechanisms using thermodynamic cycles. This treatment is based on the use of a computer to derive rate equations for three mechanisms and to estimate the kinetic parameters with the minimum number of velocity measurements. The most general of these three programs is the one to use first when the mechanism for A + B = P + Q is studied for the first time. This article shows the effects of experimental errors in velocity measurements on the values of the kinetic parameters and on the apparent equilibrium constant calculated using the Haldane relation

Determination of Kinetic Parameters of Enzyme-Catalyzed Reaction A + B + C → Products with the Minimum Number of Velocity Measurements

Rapid-equilibrium rate equations are derived for the five different mechanisms for the enzymatic catalysis of A + B + C → products using a computer. These rate equations are used to determine the minimum number of velocities required to estimate the values of the kinetic parameters. The rate equation for the completely ordered mechanism involves four kinetic parameters, and the rate equation for the completely random mechanism involves eight kinetic parameters. Therefore, the four to eight kinetic parameters can be estimated by determining four to eight velocities and solving four to eight simultaneous equations. General recommendations are made as to the choices of triplets of substrate concentrations {[A], [B], [C]} to be used to determine the velocities. The effects of 5% errors in the measured velocities, one at a time, are calculated and are summarized in tables. Calculations of effects of experimental errors are useful in choosing the triplets of substrate concentrations to be used to obtain the most accurate values of the kinetic parameters. When the kinetic parameters for A + B + C → products are to be determined for the first time, it is recommended that the program for the completely random mechanism be used because it can identify the mechanism and determine the kinetic parameters in one operation

Molecular dynamics simulations of the temperature-induced unfolding of crambin follow the Arrhenius equation

Molecular dynamics simulations have been used extensively to model the folding and unfolding of proteins. The rates of folding and unfolding should follow the Arrhenius equation over a limited range of temperatures. This study shows that molecular dynamic simulations of the unfolding of crambin between 500K and 560K do follow the Arrhenius equation. They also show that while there is a large amount of variation between the simulations the average values for the rate show a very high degree of correlation

Enabling Torts

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Detailed Enzyme Kinetics in Terms of Biochemical Species: Study of Citrate Synthase

The compulsory-ordered ternary catalytic mechanism for two-substrate two-product enzymes is analyzed to account for binding of inhibitors to each of the four enzyme states and to maintain the relationship between the kinetic constants and the reaction equilibrium constant. The developed quasi-steady flux expression is applied to the analysis of data from citrate synthase to determine and parameterize a kinetic scheme in terms of biochemical species, in which the effects of pH, ionic strength, and cation binding to biochemical species are explicitly accounted for in the analysis of the data. This analysis provides a mechanistic model that is consistent with the data that have been used support competing hypotheses regarding the catalytic mechanism of this enzyme

Calculation of the interfacial free energy of a fluid at a static wall by Gibbs–Cahn integration

This is the publisher's version, also available electronically from http://scitation.aip.org/content/aip/journal/jcp/132/20/10.1063/1.3428383.The interface between a fluid and a static wall is a useful model for a chemically heterogeneous solid-liquid interface. In this work, we outline the calculation of the wall-fluid interfacial free energy(γwf) for such systems using molecular simulation combined with adsorptionequations based on Cahn’s extension of the surface thermodynamics of Gibbs. As an example, we integrate such an adsorptionequation to obtain γwf as a function of pressure for a hard-sphere fluid at a hard wall. The results so obtained are shown to be in excellent agreement in both magnitude and precision with previous calculations of this quantity, but are obtained with significantly lower computational effort

The role of histidine residues in modulation of the rat P2X 2 purinoceptor by zinc and pH

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/65774/1/jphysiol.2001.013244.pd