Your search for "M Padrta" returned 5 results

The Compact Muon Solenoid (CMS) detector is described. The detector operates at the Large Hadron Collider (LHC) at CERN. It was conceived to study proton-proton (and lead-lead) collisions at a centre-of-mass energy of 14 TeV (5.5 TeV nucleon-nucleon) and at luminosities up to 10³⁴ cm⁻² s⁻¹ (10²⁷ cm⁻² s⁻¹). At the core of the CMS detector sits a high-magnetic-field and large-bore superconducting solenoid surrounding an all-silicon pixel and strip tracker, a lead-tungstate scintillating-crystals electromagnetic calorimeter, and a brass-scintillator sampling hadron calorimeter. The iron yoke of the flux-return is instrumented with four stations of muon detectors covering most of the 4π solid angle. Forward sampling calorimeters extend the pseudorapidity coverage to high values (|η| ⩽ 5) assuring very good hermeticity. The overall dimensions of the CMS detector are a length of 21.6 m, a diameter of 14.6 m and a total weight of 12500 t.

Muons are among the decay products of many new particles that may be discovered at the CERN Large Hadron Collider. At the first trigger level the identification of muons and the determination of their transverse momenta and location are performed by the Drift Tube Trigger Track Finder in the central region of the CMS (Compact Muon Solenoid) experiment, using track segments detected in the Drift Tube muon chambers. Track finding is performed both in pseudorapidity and azimuth. Track candidates are ranked and sorted, and the best four are delivered to the subsequent stage, the Global Muon Trigger, which combines them with candidates found in the two complementary muon systems of CMS, the Resistive Plate Chambers and the Cathode Strip Chambers. The concept, design, control and simulation software as well as tests and the expected performance of the Drift Tube Trigger Track Finder system are described.

The electronics of the First Level Global Trigger (GT) for the CMS experiment is described. It is the last stage of the Level-1 trigger system and decides for every LHC bunch crossing whether to reject or to accept a physics event for further evaluation by the High Level Trigger. The Global Trigger receives trigger objects from the Global Calorimeter Trigger and the Global Muon Trigger and applies in parallel up to 128 physics trigger requirements, so-called 'Algorithms'. In addition, up to 64 so-called 'Technical Trigger' signals can be used to either accept or reject events. The Algorithm and Technical Trigger bits are then combined to a Final_OR signal to start the readout procedure of an event.

The Large Hadron Collider will deliver up to 32 million physics collisions per second. This rate is far too high to be processed by present-day computer farms, let alone stored on disk by the experiments for offline analysis. A fast selection of interesting events must therefore be made. In the CMS experiment, this is implemented in two stages: the Level-1 Trigger of the CMS experiment uses custom-made, fast electronics, while the experiment's high-level trigger is implemented in computer farms. The Level-1 Global Trigger electronics has to receive signals from the subdetector systems that enter the trigger (mostly from muon detectors and calorimeters), synchronize them, determine if a pre-set trigger condition is fulfilled, check if the various subsystems are ready to accept triggers based on information from the Trigger Throttling System and on calculations of possible dead-times, and finally distribute the trigger decision (``Level-1 Accept'') together with timing signals to the subdetectors over the so-called ``Trigger, Timing and Control'' distribution tree of the experiment. These functions are fulfilled by several specialized, custom-made VME modules, most of which are housed in one crate. The overall control is exerted by the central ``Trigger Control System'', which is described in this paper. It consists of one main module and several ancillary boards for input and output functions.

The key achievements and the potential of NMR spectroscopy for weakly aligned biomolecules are considered. Due to weak alignment, it becomes possible to determine a number of NMR parameters dependent on the orientation of biomolecules, which are averaged to zero in usual isotropic media. The addition of new orientational constraints to standard procedures of 3D structure determination markedly increases the achievable accuracy. The possibility of structure determination for biomolecules using only orientation-dependent parameters without invoking other NMR data is discussed. The methods of orientation, experimental techniques, and calculation methods are systematised. The main results obtained and the prospects of using NMR spectroscopy of weakly aligned systems to study different classes of biomolecules and to solve various problems of molecular biology are analysed. Examples of biomolecules whose structures have been determined using orientation-dependent parameters are given. The bibliography includes 508 references.