RESUMEN
We report on the design and fabrication of an Er(3+):Yb(3+) triple clad fiber and on the power scaling of a single frequency fiber amplifier at 1.5 µm based on that fiber. In addition, we report on mode content measurements in order to reveal the overlap of the amplifier output with the TEM(00) mode. The triple clad design was used to enable high output power levels, a good slope efficiency and an excellent beam quality. A maximum single frequency output power of 61 W at 1.5 µm could be achieved with the aid of the co-seeding method, which was used to suppress parasitic processes at 1.0 µm. With a scanning ring cavity the mode content of the amplifier output was analyzed with respect to the TEM modes. For all output power levels the TEM(00) content was above 90%.
RESUMEN
In this study quantum mechanical calculations of force constants and normal mode analysis are used to elucidate the factors that influence the C=C and C=N stretching frequencies in polyenes and in protonated Schiff bases. The C=N stretching frequency is found to depend on both the C=N stretching force constant and the C=N-H bending force constant. Due to the contributions of these two modes, the C=N stretching frequency is particularly sensitive to the magnitude of the Schiff base counterion interactions and to the hydrogen bonding environment of the Schiff base nitrogen. Models for chromophore-protein interactions in the retinal binding site and for the photochemical transformations of bacteriorhodopsin and rhodopsin are evaluated in light of these results.
Asunto(s)
Bacteriorodopsinas , Pigmentos Retinianos , Rodopsina , Sitios de Unión , Enlace de Hidrógeno , Unión Proteica , Conformación Proteica , Retinaldehído , Bases de Schiff , Espectrometría RamanRESUMEN
Fourier-transform infrared difference spectroscopy has been used to detect the vibrational modes in the chromophore and protein that change in position or intensity between rhodopsin and the photoproducts formed at low temperature (70 K), bathorhodopsin and isorhodopsin. A method has been developed to obtain infrared difference spectra between rhodopsin and bathorhodopsin, bathorhodopsin and isorhodopsin, and rhodopsin and isorhodopsin. To aid in the identification of the vibrational modes, we performed experiments on deuterated and hydrated films of native rod outer segments and rod outer segments regenerated with either retinal containing 13C at carbon 15 or 15-deuterioretinal. Our infrared measurements provide independent verification of the resonance Raman result that the retinal in bathorhodopsin is distorted all-trans. The positions of the C = N stretch in the deuterated pigment and the deuterated pigments regenerated with 11-cis-15-deuterioretinal or 11-cis-retinal containing 13C at carbon 15 are indicative that the Schiff-base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin. Furthermore, the C = N stretching frequency occurs at the same position in all three species. The data indicate that the protonated Schiff base has a C = N trans conformation in all three species. Finally, we present evidence that, even in these early stages of the rhodopsin photosequence, changes are occurring in the opsin and perhaps the associated lipids.