Euclidean ramsey theorems. I

The general Ramsey problem can be described as follows: Let A and B be two sets, and R a subset of A × B. For a?A denote by R(a) the set {b?B | (a, b) ?R}. R is called r-Ramsey if for any r-part partition of B there is some a?A with R(a) in one part. We investigate questions of whether or not certain R are r-Ramsey where B is a Euclidean space and R is defined geometrically.     

Colorimetrie

Ohne Zusammenfassung     

Die Bestimmung des Nickels bei Gegenwart von Zink und Eisen

Ohne Zusammenfassung     

On the choice of the test structure for the electrical characterization of dielectrics for silicon solar cells

Surface passivation of Si solar cells is typically achieved by deposition of a dielectric layer. Via the investigation of Al₂O₃ passivation layers, we show that care must be taken when performing capacitance–voltage (C –V) measurements in order to obtain results that are meaningful at solar cell level. The passivation properties of a dielectric are not only affected by post‐deposition treatments but also by the presence and the nature of a metal covering the dielectric. Consequently, this Letter emphasizes how important it is to perform C –V measurements on a device structure that resembles as closely as possible that of the finished solar cell, using the same metal, deposition technique and thermal budget. (© 2010 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)     

Subpicosecond protein backbone changes detected during the green-absorbing proteorhodopsin primary photoreaction

Recent studies demonstrate that photoactive proteins can react within several picoseconds to photon absorption by their chromophores. Faster subpicosecond protein responses have been suggested to occur in rhodopsin-like proteins where retinal photoisomerization may impulsively drive structural changes in nearby protein groups. Here, we test this possibility by investigating the earliest protein structural changes occurring in proteorhodopsin (PR) using ultrafast transient infrared (TIR) spectroscopy with approximately 200 fs time resolution combined with nonperturbing isotope labeling. PR is a recently discovered microbial rhodopsin similar to bacteriorhodopsin (BR) found in marine proteobacteria and functions as a proton pump. Vibrational bands in the retinal fingerprint (1175-1215 cm(-1)) and ethylenic stretching (1500-1570 cm(-1)) regions characteristic of all-trans to 13-cis chromophore isomerization and formation of a red-shifted photointermediate appear with a 500-700 fs time constant after photoexcitation. Bands characteristic of partial return to the ground state evolve with a 2.0-3.5 ps time constant. In addition, a negative band appears at 1548 cm(-1) with a time constant of 500-700 fs, which on the basis of total-15N and retinal C15D (retinal with a deuterium on carbon 15) isotope labeling is assigned to an amide II peptide backbone mode that shifts to near 1538 cm(-1) concomitantly with chromophore isomerization. Our results demonstrate that one or more peptide backbone groups in PR respond with a time constant of 500-700 fs, almost coincident with the light-driven retinylidene chromophore isomerization. The protein changes we observe on a subpicosecond time scale may be involved in storage of the absorbed photon energy subsequently utilized for proton transport.