Search results for "Trimer"
showing 6 items of 76 documents
1984
The decomposition reactions of the lithiated dimer, trimer, and tetramer of methyl methacrylate (MMA) in THF at 25°C were investigated. The decomposition of the lithiated dimer proceeds via depolymerization to lithiated monomer and MMA, addition of MMA to residual lithiated dimer, resulting the trimer (“disproportionation” of the dimer), and subsequent autocondensation of the products. The lithiated trimer almost exclusively undergoes cyclo-autocondensation, whereas for the lithiated tetramer both reactions proceed simultaneously to a remarkable degree. It is shown that the relative rate of autocondensation, which is highly dependent on the degree of polymerization of the oligomer, controls…
(E,E,E)-4,4′-Distyrylstilbenes – Synthesis, Photophysics, Photochemistry and Phase Behavior
2008
The fluorescence quantum yields F(n) of oligo[2,5-bis(propyloxy)-1,4-phenylenevinylene]s (1b) reach for the trimer (n = 3) in solution a maximum of 86 %, which is almost twice as high as for the monomer (n = 1) and the octamer or undecamer (n = 8, 11). The latter represent the convergence limit of 46 %. 4-Mono-, 3,4-di- or 3,4,5-trisubstituted terminal phenyl rings in the trimers 6a–f do not lead to calamitic or phasmidic liquid crystals; however, 2,3,4-trisubstitution with hexyloxy groups (6h) and even with OCH3 groups (6g) effects LC formation. Irradiation with energy-rich UV light provokes a crosslinking of the originally conjugated chains. In the case of 6c, a chemo- and stereoselective…
Light-dependent CK2-mediated phosphorylation of centrins regulates complex formation with visual G-protein.
2008
AbstractCentrins are Ca2+-binding EF-hand proteins. All four known centrin isoforms are expressed in the ciliary apparatus of photoreceptor cells. Cen1p and Cen2p bind to the visual G-protein transducin in a strictly Ca2+-dependent way, which is thought to regulate light driven movements of transducin between photoreceptor cell compartments. These relatively slow motile processes represent a novel paradigm in light adaptation of photoreceptor cells.Here we validated specific phosphorylation as a novel regulator of centrins in photoreceptors. Centrins were differentially phosphorylated during photoreceptor dark adaptation. Inhibitor treatments revealed protein kinase CK2 as the major protein…
Modeling of the N-terminal Section and the Lumenal Loop of Trimeric Light Harvesting Complex II (LHCII) by Using EPR
2015
The major light harvesting complex II (LHCII) of green plants plays a key role in the absorption of sunlight, the regulation of photosynthesis, and in preventing photodamage by excess light. The latter two functions are thought to involve the lumenal loop and the N-terminal domain. Their structure and mobility in an aqueous environment are only partially known. Electron paramagnetic resonance (EPR) has been used to measure the structure of these hydrophilic protein domains in detergent-solubilized LHCII. A new technique is introduced to prepare LHCII trimers in which only one monomer is spin-labeled. These heterogeneous trimers allow to measure intra-molecular distances within one LHCII mon…
Notes on Shore Flies (Diptera: Ephydridae) from Finland and north-western Russia
2015
The recent checklist of the Ephydridae of Finland by Zatwarnicki and Kahanpää (2014) mentioned 13 ephydrid species as new for Finland without further details. This paper presents detailed records for those species and a few other species of interest. Four species are recorded for the first time from Russia. Trimerina indistincta Krivosheina, 2004 is herein considered as a new junior synonym of Trimerina microchaeta Hendel, 1932, syn. nov.
Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines.
1998
ABSTRACT We have used viruslike particles (VLPs) of human papillomaviruses to study the structure and assembly of the viral capsid. We demonstrate that mutation of either of two highly conserved cysteines of the major capsid protein L1 to serine completely prevents the assembly of VLPs but not of capsomers, whereas mutation of all other cysteines leaves VLP assembly unaffected. These two cysteines form intercapsomeric disulfides yielding an L1 trimer. Trimerization comprises about half of the L1 molecules in VLPs but all L1 molecules in complete virions. We suggest that trimerization of L1 is indispensable for the stabilization of intercapsomeric contacts in papillomavirus capsids.