1,190 research outputs found
Latitudinal variation of diversity in European freshwater animals is not concordant across habitat types
Mass Spectrometric Characterization of Oligomers in Pseudomonas aeruginosa Azurin Solutions
We have employed laser-induced liquid bead ion desorption mass spectroscopy (LILBID MS) to study the solution behavior of Pseudomonas aeruginosa azurin as well as two mutants and corresponding Re-labeled derivatives containing a Re(CO)_(3)(4,7-dimethyl-1,10-phenanthroline)^+ chromophore appended to a surface histidine. LILBID spectra show broad oligomer distributions whose particular patterns depend on the solution composition (pure H_(2)O, 20−30 mM NaCl, 20 and 50 mM NaP_i or NH_(4)P_i at pH = 7). The distribution maximum shifts to smaller oligomers upon decreasing the azurin concentration and increasing the buffer concentration. Oligomerization is less extensive for native azurin than its mutants. The oligomerization propensities of unlabeled and Re-labeled proteins are generally comparable, and only Re126 shows some preference for the dimer that persists even in highly diluted solutions. Peak shifts to higher masses and broadening in 20−50 mM NaP_i confirm strong azurin association with buffer ions and solvation. We have found that LILBID MS reveals the solution behavior of weakly bound nonspecific protein oligomers, clearly distinguishing individual components of the oligomer distribution. Independently, average data on oligomerization and the dependence on solution composition were obtained by time-resolved anisotropy of the Re-label photoluminescence that confirmed relatively long rotation correlation times, 6−30 ns, depending on Re−azurin and solution composition. Labeling proteins with Re-chromophores that have long-lived phosphorescence extends the time scale of anisotropy measurements to hundreds of nanoseconds, thereby opening the way for investigations of large oligomers with long rotation times
Hydration and Mobility of Oxidized Phospholipid Bilayer: Fluorescence Solvent Relaxation and Fluorescence Correlation Spectroscopy Study
Dworkin's argument revisited: point processes, dynamics, diffraction, and correlations
The paper studies the relationship between diffraction and dynamics for
uniformly discrete ergodic point processes in real spaces. This relationship
takes the form of an isometric embedding of two L^2 spaces. Diffraction (or
equivalently the 2-point correlations) usually cannot determine the dynamics
entirely, but we prove that knowledge of all the higher correlations (2-point,
3-point, ...) does. A square-mean form of the Bombieri-Taylor conjecture is
proved. A quantitative relation between autocorrelation, diffraction, and
epsilon dual characters is derived. Most results of the paper are proved in the
setting of multi-colour points and assignable scattering strengths.Comment: 49 page
Optical Near-Field Electron Microscopy
Imaging dynamical processes at interfaces and on the nanoscale is of great
importance throughout science and technology. While light-optical imaging
techniques often cannot provide the necessary spatial resolution,
electron-optical techniques damage the specimen and cause dose-induced
artefacts. Here, Optical Near-field Electron Microscopy (ONEM) is proposed, an
imaging technique that combines non-invasive probing with light, with a high
spatial resolution read-out via electron optics. Close to the specimen, the
optical near-fields are converted into a spatially varying electron flux using
a planar photocathode. The electron flux is imaged using low energy electron
microscopy, enabling label-free nanometric resolution without the need to scan
a probe across the sample. The specimen is never exposed to damaging electrons
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