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We investigate the photostability of a set of organic semiconductor blends comprising a conjugated polymer as the donor and a fullerene as the acceptor using electron spin resonance (ESR). In the absence of oxygen, all blends show excellent stability. Even after several hundred hours of exposure to solar or UV radiation, the ESR spectra and the recombination of photoinduced charges recorded at low temperature are found to be unchanged. By contrast, the presence of oxygen leads to a fast light-induced degradation rendering the ability of the donor/acceptor system to form photoinduced charge carriers. Our findings suggest that conjugated polymer–fullerene blends exhibit very good photostability and that oxygen needs to be excluded in optoelectronic applications. Our findings also suggest that at low temperature, a universal recombination process of long-lived photoinduced charges is active, which does not depend on the electronic structure or the morphology of the investigated materials.
The complete covalent structure of a novel boar
DQH sperm surface protein resistant to many classical procedures
of enzymatic fragmentation was determined. The relative
molecular mass of the major form of this protein determined
by ESI-MS and MALDI-MS was 13,065.2 ± 1.0 and 13,065.1,
respectively. However, additional peaks differing by 162
Da (i.e., minus hexose), 365 Da (i.e., minus hexose and
N-acetylhexosamine), 146 Da (i.e., plus deoxyhexose), and
291 Da (i.e., plus sialic acid) indicated the heterogeneity
due to differences in glycosylation. The complete covalent
structure of the protein was determined using automated
Edman degradation, MALDI-MS, and post-source decay (PSD)
MALDI-MS, and shown to consist of N-terminal O-glycosylated
peptide followed by two fibronectin type II repeats. The
carbohydrates are O-glycosidically linked to threonine
10, as confirmed by PSD MALDI-MS of the isolated N-terminal
glycopeptide. Eight cysteine residues of the protein form
four disulfide bridges, the positions of which were assigned
from MALDI-MS and Edman degradation data. We conclude that
mass spectral techniques provide an indispensable tool
for the detailed analysis of the covalent structure of
proteins, especially those that are refractory to standard
approaches of protein chemistry.
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