The technical challenges of the Large Hadron Collider
The Large Hadron Collider (LHC) is a 27 km circumference hadron collider, built at CERN to explore the energy frontier of particle physics. Approved in 1994, it was commissioned and began operation for data taking in 2009. The design and construction of the LHC presented many design, engineering and logistical challenges which involved pushing a number of technologies well beyond their level at the time. Since the start-up of the machine, there has been a very successful 3-year run with an impressive amount of data delivered to the LHC experiments. With an increasingly large stored energy in the beam, the operation of the machine itself presented many challenges and some of these will be discussed. Finally, the planning for the next 20 years has been outlined with progressive upgrades of the machine, first to nominal energy, then to progressively higher collision rates. At each stage the technical challenges are illustrated with a few examples.
Dynamic aperture computation for the as-built CERN Large Hadron Collider
During the design phase of the CERN Large Hadron Collider the dynamic aperture, i.e., the domain in phase space where stable motion occurs, was used as figure-ofmerit to specify the field quality of the various classes of superconducting magnets. The programme of magnetic measurements performed within the framework of the magnets’ acceptance process has produced a large amount of information available, which can be used to estimate the value of the dynamic aperture for the actual machine. In this paper the results of massive numerical simulations based on the measured field quality, both for injection and top energy configurations, are presented and discussed in detail.
Cytoplsmic uridine phosphorylase of rat liver. Characterization and kinetics.
Abstract Uridine phosphorylase (uridine:orthophosphate ribosyltransferase, EC 2.4.2.3) of rat liver cytoplasm has been purified 1900-fold. Initial velocity patterns of the phosphorolysis of uridine or deoxyuridine and of the synthesis of uridine indicated a sequential mechanism. Product inhibition patterns with uracil or ribose 1-phosphate as inhibitors were consistent with an "ordered Bi Bi" reaction in which inorganic phosphate is the first substrate to bind to the enzyme and ribose 1-phosphate the last product to leave the enzyme. The most highly purified enzyme fractions still retained uridine-, deoxyuridine-, and thymidine-cleaving activities in the ratio of 10:7:1 at pH 7.4. The fractions separated into a major and a minor band of protein on electrophoresis in phosphate buffer. Aging of the enzyme with loss of activity resulted in an increase in the proportion of the minor band. The pH optimum of the enzyme for uridine cleavage was 8.2, for deoxyuridine cleavage, 6.5, and for uridine synthesis, 8.5. Uridine or deoxyuridine synthesis was inhibited 50% in the presence of 1 mm uracil. The enzyme did not catalyze the direct transfer of ribose from uridine to uracil in the absence of phosphate. Uridine protected the enzyme to a greater degree than phosphate against inhibition by o-iodosobenzoate. Thus, at least one sulfhydryl group and possibly three are present at or near the active site. Uridine cleavage, uridine synthesis, and deoxyuridine cleavage were inhibited by deoxyglucosylthymine. The phosphorolysis of deoxyuridine and thymidine by thymidine phosphorylase, also purified from rat liver cytoplasm, was not inhibited by deoxyglucosylthymine. The molecular weights of both uridine and thymidine phosphorylases were estimated to be 110,000.