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The ratio of the yields of antiprotons to protons in pp collisions has been measured by the ALICE experiment at sqrt[s]=0.9 and 7 TeV during the initial running periods of the Large Hadron Collider. The measurement covers the transverse momentum interval 0.45

The production of π + , π − , K + , K − , p, and p at mid-rapidity has been measured in proton-proton collisions at √ s = 900 GeV with the ALICE detector. Particle identification is performed using the specific energy loss in the inner tracking silicon detector and the time projection chamber. In addition, time-of-flight information is used to identify hadrons at higher momenta. Finally, the distinctive kink topology of the weak decay of charged kaons is used for an alternative measurement of the kaon transverse momentum (p t ) spectra. Since these various particle identification tools give the best separation capabilities over different momentum ranges, the results are combined to extract spectra from p t = 100 MeV/c to 2.5 GeV/c. The measured spectra are further compared with QCD-inspired models which yield a poor description. The total yields and the mean p t are compared with previous measurements, and the trends as a function of collision energy are discussed.t Deceased.

The pseudorapidity density and multiplicity distribution of charged particles produced in proton-proton collisions at the LHC, at a centre-of-mass energy √ s = 7 TeV, were measured in the central pseudorapidity region |η| < 1. Comparisons are made with previous measurements at √ s = 0.9 TeV and 2.36 TeV. At √ s = 7 TeV, for events with at least one charged particle in |η| < 1, we obtain dN ch /dη = 6.01 ± 0.01(stat.) +0.20 −0.12 (syst.). This corresponds to an increase of 57.6% ± 0.4%(stat.) +3.6 −1.8 %(syst.) relative to collisions at 0.9 TeV, significantly higher than calculations from commonly used models. The multiplicity distribution at 7 TeV is described fairly well by the negative binomial distribution.

The molecular chaperone αB-crystallin, the major player in maintaining the transparency of the eye lens, prevents stress-damaged and aging lens proteins from aggregation. In nonlenticular cells, it is involved in various neurological diseases, diabetes, and cancer. Given its structural plasticity and dynamics, structure analysis of αB-crystallin presented hitherto a formidable challenge. Here we present a pseudoatomic model of a 24-meric αB-crystallin assembly obtained by a triple hybrid approach combining data from cryoelectron microscopy, NMR spectroscopy, and structural modeling. The model, confirmed by cross-linking and mass spectrometry, shows that the subunits interact within the oligomer in different, defined conformations. We further present the molecular architectures of additional well-defined αB-crystallin assemblies with larger or smaller numbers of subunits, provide the mechanism how "heterogeneity" is achieved by a small set of defined structural variations, and analyze the factors modulating the oligomer equilibrium of αB-crystallin and thus its chaperone activity.T he most prominent member of the small heat-shock protein (sHsp) family, α-crystallin, is expressed at high concentrations in the vertebrate eye lens (1) where it plays a major role in maintaining lens transparency (2). Moreover, it protects lens epithelial cells from environmental stress by preventing aggregation of stress-damaged proteins (3). In the low protein turnover milieu of the eye lens, proteins gradually deteriorate throughout the lifespan due to posttranslational modifications and become increasingly prone to aggregation leading to opacity. Thus, the chaperone action of α-crystallin is vital for maintaining the eye lens transparency. Lenticular α-crystallin is composed of two homologous polypeptides, αA-and αB-crystallin, which comprise 173 and 175 amino acid residues, respectively (1, 4). Both proteins possess a three-domain organization consisting of the α-crystallin domain (ACD), a consensus sequence of approximately 90 amino acids common to all sHsps, flanked by a diverse N-terminal region and a moderately conserved C-terminal extension (5, 6).Of the two constituents of α-crystallin, αB-crystallin is the more widespread chaperone with versatile functions: Besides the eye lens, it is abundantly expressed in other tissues (7) and upregulated by various stresses (8). There is growing evidence for its implications in several neuropathological diseases (9) including Parkinson disease, Alzheimer's disease, and multiple sclerosis (10, 11) as well as in cancer (12). In vitro, αB-crystallin prevents the stress-induced aggregation of partially folded polypeptides (3, 13).The αB-crystallin assembles into homooligomers with a variable number of subunits, primarily 24-32 (14-16), and the subunits exchange between homooligomers (17). These properties have hampered high-resolution structural studies on the functionally assembled, full-length protein. An earlier cryoelectron microscopy (cryo-EM) study (18) presented at low resolution (3...