172,276 research outputs found
Dezider Scheer Collection 1940-2002 Bulk dates: 1940-1991
No full textThe Dezider Scheer Collection documents select periods throughout the life and career of Dezider Scheer. The collection consists of correspondence, legal and identification documents, original and photocopied photographs, clippings, Sosúa reunion documents and a scrapbook. Scheer’s correspondence consists of typed, photocopied and hand-written correspondence with a variety of correspondents in several languages. The Scheer Family series includes Dezider Scheer’s passport, original photographs of the Scheer family children, typed accounts of Scheer family Holocaust survivors and righteous Gentiles, and typed and handwritten memoirs. Also included are photocopied Scheer family trees, deportation lists, and photographs with notations identifying Scheer family relatives. Series III: Jewish settlement in Sosua contains Sosúa-related press clippings in English and Spanish, as well as documents and a scrapbook related to the Sosúa reunions and settlers.Dezider Scheer was born in Slovakia c. 1918. On August 29, 1939, He left Slovakia with a small group of young men to travel to Palestine illegally, but they were interned in an Italian camp in St. Bertononeo near Salerno. In 1940, Mr. Thorne, a representative from the Dominican Republic Settlement Association (DORSA) came to the camp in Italy and selected potential settlers among the young refugees for a Jewish refugee settlement in Sosúa, Dominican Republic. He selected Dezider Scheer and others.Dezider Scheer arrived in Sosúa in October 1940 and eventually acquired a farm with 25 cows. He also became principal of the local school. In 1950 he decided to leave the Sosúa settlement to join his brother in Canada. He paid his debts to DORSA and settled in Montreal, Quebec.Historical Note:In July 1938 the Évian Conference was convened at the initiative of US President Franklin D. Roosevelt to discuss the issue of increasing numbers of Jewish refugees from Central Europe. In the end the Dominican Republic was the only country willing to accept a large number of Jews, offering citizenship for up to 100,000 refugees.Itemized container list on fileProcesseddigitize
Effect of protein environment and the excitonic coupling on the excited-state properties of the bilinchromophores in C-Phycocyanin
No full textEnergy transfer calculations for two C-phycocyanins based on refined x-ray crystal structure coordinates of chromophores
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Energy transfer in 'native' and chemically modified C-phyocyanin trimers and the constituent subunits
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Dissociating effect of chromophore modifications on C-phycocyanin heterohexamers
No full textThe bilin chromophores of the α or β subunit of C-phycocyanin (PC) from Mastigocladus laminosus were modified, and subsequently recombined with the respective complementary unmodified chromophores. The modifications consisted of photobleaching (350 nm) or reversible reduction of the verdin- to rubin-type chromophore(s). Recombination led to heterodimers (αβ)1, but the heterohexameric aggregation state (αβ)3 could not be obtained with the modified chromophores. Autoxidation of the reduced α-84 chromophore in such a hybrid, which occurred on standing under aerobic conditions, induced reaggregation to heterohexamers. Chemical re-oxidation of the reduced chromophores did not produce reaggregation, and it was not promoted by a 22 kDa linker peptide fragment (Gottschalk et al., Photochem. Photobiol., 54 (1991) 283), which in unmodified samples stabilized heterohexameric aggregates. Binding of the mercurial p-chloromercury-benzenesulphonate to the single free cysteine of PC near (approximately 0.4 nm) the β-84 chromophore had only a moderately destabilizing effect on the heterohexamer (αβ)3. It was concluded that the intact chromophore structure is an important factor determining the quaternary structure of biliproteins. The tendency of heterohexamer destabilization is related to the situation in phycoerythrocyanin, where photoisomerization of the violobilin chromophore of the α subunit near the heterodimer—heterodimer contact region is also responsible for aggregate destabilization (Siebzehnrübl et al., Photochem. Photobiol., 46 (1989) 753)
Picosecond time-resolved energy transfer kinetics within C-phycocyanin and allophycocyanin aggregates
No full textFÖRSTER TRANSFER CALCULATIONS BASED ON CRYSTAL STRUCTURE DATA FROM Agmenellum quadruplicatum C-PHYCOCYANIN
No full textExcitation energy transfer in C-phycocyanin is modeled using the Forster inductive resonance mechanism. Detailed calculations are carried out using coordinates and orientations of the chromophores derived from X-ray crystallographic studies of C-phycocyanin from two different species (Schirmer et al, J. Mol. Biol. 184, 257–277 (1985) and ibid., 188, 651-677 (1986)). Spectral overlap integrals are estimated from absorption and fluorescence spectra of C-phycocyanin of Mastigocladus laminosus and its separated subunits. Calculations are carried out for the β-subunit, αβ-monomer, (αβ)3-trimer and (αβ)0-hexamer species with the following chromophore assignments: β155 = 's’(sensitizer), β84 =‘f (fluorescer) and α84 =‘m’(intermediate):]:. The calculations show that excitation transfer relaxation occurs to 3=98% within 200 ps in nearly every case; however, the rates increase as much as 10-fold for the higher aggregates. Comparison with experimental data on fluorescence decay and depolarization kinetics from the literature shows qualitative agreement with these calculations. We conclude that Forster transfer is sufficient to account for all of the observed fluorescence properties of C-phycocyanin in aggregation states up to the hexamer and in the absence of linker polypeptides
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