Pointing of the 16 foot antenna

Comprehensive pointing theory for 16 ft antenna including servo encoder reading

The linear polarization of lunar thermal emission at 3.1 mm wavelength

Several observations of the distribution of linearly polarized lunar thermal emission were made at a wavelength of 3.1 mm with 4.88 m parabolic reflector from February to March 1971. A shadow corrected rough surface thermal emission model was least squares fitted to the data. Results indicate an effective lunar dielectric constant of 1.34 + or -.08 with surface roughness characterized by a standard deviation of surface slopes of 18 deg + or - 2 deg. A comparison of these results with previously published values at other wavelengths suggests that the effective lunar dielectric constant decreases with decreasing wavelength

Planetary observations at millimeter wavelengths

Observations of the Sun, Moon, Mercury, Venus, Mars, Jupiter, and Saturn were made at 3.1 mm and 8.6 mm wavelengths with a 16-foot radio telescope between March and August, 1971. Absolute brightness temperature data are given. All errors are one standard deviation and include uncertainties in antenna gain calibration. The solar and lunar temperatures are in excellent agreement with published observations. The planetary measurements at 3.1 mm are consistently higher than previous results. The implications of higher temperatures with respect to existing atmospheric and surface models are discussed

The use of Gaussian functions in radio astronomy source measurements

Gaussian distribution analysis of radio source observatio

STUDY ON THE STRUCTURAL BASIS OF PERIPHERAL LIGHT HARVESTING COMPLEXES (LH2) IN PURPLE NON-SULPHUR PHOTOSYNTHETIC BACTERIA

ABSTRACT Photosynthesisprovides an example of a natural process that has been optimized during evolution to harness solar energy efficiently and safely, and finally to use it to produce a carbon-based fuel. Initially, solar energy is captured by the light harvesting pigment-protein complexes. In purple bacteria these antenna complexes are constructed on a rather simple modular basis. Light absorbed by these antenna complexes is funnelled downhill to reaction centres, where light drives a trans-membraneredox reaction. The light harvesting proteins not only provide the scaffolding that correctly positions the bacteriochlorophylla and carotenoid pigments for optimal energy transfer but also creates an environment that can modulate the wavelengthat which different bacteriochlorophyllmolecules absorb light thereby creating the energy funnel. How these proteins can modulate the absorption spectra of the bacteriochlorophyllswill be discussedin this review. INTRODUCTION Keywords: photosynthesis, peripheral light harvesting complex, H-bonding, energy transfe

An improved crystal structure of C-phycoerythrin from the marine cyanobacterium Phormidium sp. A09DM

C-Phycoerythrin (PE) from Phormidium sp. A09DM has been crystallized using different conditions and its structure determined to atomic resolution (1.14 Å). In order for the pigment present, phycoerythrobilin (PEB), to function as an efficient light-harvesting molecule it must be held rigidly (Kupka and Scheer in Biochim Biophys Acta 1777:94–103, 2008) and, moreover, the different PEB molecules in PE must be arranged, relative to each other, so as to promote efficient energy transfer between them. This improved structure has allowed us to define in great detail the structure of the PEBs and their binding sites. These precise structural details will facilitate theoretical calculations of each PEB’s spectroscopic properties. It was possible, however, to suggest a model for which chromophores contribute to the different regions of absorption spectrum and propose a tentative scheme for energy transfer. We show that some subtle differences in one of these PEB binding sites in two of the 12 subunits are caused by crystal contacts between neighboring hexamers in the crystal lattice. This explains some of the differences seen in previous lower resolution structures determined at two different pH values (Kumar et al. in Photosyn Res 129:17–28, 2016)

Nature does not rely on long-lived electronic quantum coherence for photosynthetic energy transfer

During the first steps of photosynthesis, the energy of impinging solar photons is transformed into electronic excitation energy of the light-harvesting biomolecular complexes. The subsequent energy transfer to the reaction center is commonly rationalized in terms of excitons moving on a grid of biomolecular chromophores on typical timescales [Formula: see text]100 fs. Today's understanding of the energy transfer includes the fact that the excitons are delocalized over a few neighboring sites, but the role of quantum coherence is considered as irrelevant for the transfer dynamics because it typically decays within a few tens of femtoseconds. This orthodox picture of incoherent energy transfer between clusters of a few pigments sharing delocalized excitons has been challenged by ultrafast optical spectroscopy experiments with the Fenna-Matthews-Olson protein, in which interference oscillatory signals up to 1.5 ps were reported and interpreted as direct evidence of exceptionally long-lived electronic quantum coherence. Here, we show that the optical 2D photon echo spectra of this complex at ambient temperature in aqueous solution do not provide evidence of any long-lived electronic quantum coherence, but confirm the orthodox view of rapidly decaying electronic quantum coherence on a timescale of 60 fs. Our results can be considered as generic and give no hint that electronic quantum coherence plays any biofunctional role in real photoactive biomolecular complexes. Because in this structurally well-defined protein the distances between bacteriochlorophylls are comparable to those of other light-harvesting complexes, we anticipate that this finding is general and directly applies to even larger photoactive biomolecular complexes

Fluorescence-excitation and emission spectroscopy on single FMO complexes

In green-sulfur bacteria sunlight is absorbed by antenna structures termed chlorosomes, and transferred to the RC via the Fenna-Matthews-Olson (FMO) complex. FMO consists of three monomers arranged in C3 symmetry where each monomer accommodates eight Bacteriochlorophyll a (BChl a) molecules. It was the first pigment-protein complex for which the structure has been determined with high resolution and since then this complex has been the subject of numerous studies both experimentally and theoretically. Here we report about fluorescence-excitation spectroscopy as well as emission spectroscopy from individual FMO complexes at low temperatures. The individual FMO complexes are subjected to very fast spectral fluctuations smearing out any possible different information from the ensemble data that were recorded under the same experimental conditions. In other words, on the time scales that are experimentally accessible by single-molecule techniques, the FMO complex exhibits ergodic behaviour