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Träfflista för sökning "WFRF:(Wolfenstein L.) srt2:(2005-2009)"

Sökning: WFRF:(Wolfenstein L.) > (2005-2009)

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1.
  • Amsler, C., et al. (författare)
  • Review of particle physics
  • 2008
  • Ingår i: Physics Letters. Section B: Nuclear, Elementary Particle and High-Energy Physics. - : Elsevier BV. - 0370-2693 .- 1873-2445. ; 667:1-5, s. 1-1
  • Forskningsöversikt (refereegranskat)abstract
    • This biennial Review summarizes much of particle physics. Using data from previous editions., plus 2778 new measurements from 645 papers, we list, evaluate, and average measured properties of gauge bosons, leptons, quarks, mesons, and baryons. We also summarize searches for hypothetical particles such as Higgs bosons, heavy neutrinos, and supersymmetric particles. All the particle properties and search limits are listed in Summary Tables. We also give numerous tables, figures, formulae, and reviews of topics such as the Standard Model, particle detectors., probability, and statistics. Among the 108 reviews are many that are new or heavily revised including those on CKM quark-mixing matrix, V-ud & V-us, V-cb & V-ub, top quark, muon anomalous magnetic moment, extra dimensions, particle detectors, cosmic background radiation, dark matter, cosmological parameters, and big bang cosmology.
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2.
  • Yao, W-M, et al. (författare)
  • Review of Particle Physics
  • 2006
  • Ingår i: Journal of Physics G: Nuclear and Particle Physics. - : IOP Publishing. - 0954-3899 .- 1361-6471. ; 33:1, s. 1-1
  • Tidskriftsartikel (refereegranskat)
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3.
  • Yoshizaki, Lucila, et al. (författare)
  • Calliandra selloi Macbride trypsin inhibitor : isolation, characterization, stability, spectroscopic analyses
  • 2007
  • Ingår i: Phytochemistry. - : Elsevier BV. - 0031-9422 .- 1873-3700. ; 68:21, s. 2625-2634
  • Tidskriftsartikel (refereegranskat)abstract
    • A trypsin inhibitor was purified from Calliandra selloi Macbride seeds (CSTI). SDS-PAGE under non-reducing conditions showed a single band of approximately 20,000Da, while under reducing conditions two bands of 16,000 and 6000Da were observed, indicating that CSTI consists of two polypeptide chains. Molecular masses of 20,078 and 20,279 were obtained by mass spectrometry, although only one pI of 4.0 was observed and one peak was obtained by reversed phase chromatography. Amino-terminal sequence analysis showed homology to Kunitz-type inhibitors. CSTI was able to inhibit trypsin (K(i) 2.21x10(-7)M), alpha-chymotrypsin (K(i) 4.95x10(-7)M) and kallikrein (K(i) 4.20x10(-7)M) but had no effect on elastase. Trypsin inhibitory activity was stable over a wide range of pH and temperature. CSTI was particularly susceptible to DTT treatment, followed by addition of iodoacetamide. Far-UV circular dichroism measurements revealed that CSTI is a beta-II protein. Thermal unfolding showed a two-state transition with a midpoint at 68 degrees C. Far-UV CD spectra of CSTI at pH extremes showed little changes, while more pronounced differences in near-UV CD spectra were detected. Remarkably, treatment with 1mM DTT caused very slight changes in the far-UV CD spectrum, and only after carbamidomethylation was there was a marked loss observed in secondary structure.
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