@article{AdelsbergerMeierKollBivigouKoumbaetal.2011,
  author    = {Adelsberger, Joseph and Meier-Koll, Andreas and Bivigou Koumba, Achille Mayelle and Busch, Peter and Holderer, Olaf and Hellweg, Thomas and Laschewsky, Andr{\´e} and M{\"u}ller-Buschbaum, Peter and Papadakis, Christine M.},
  title     = {The collapse transition and the segmental dynamics in concentrated micellar solutions of P(S-b-NIPAM) diblock copolymers},
  series = {Colloid and polymer science : official journal of the Kolloid-Gesellschaft},
  volume    = {289},
  journal   = {Colloid and polymer science : official journal of the Kolloid-Gesellschaft},
  number    = {5-6},
  publisher = {Springer},
  address   = {New York},
  issn      = {0303-402X},
  doi       = {10.1007/s00396-011-2382-3},
  pages     = {711 -- 720},
  year      = {2011},
  abstract  = {We investigate concentrated solutions of poly(styrene-b-N-isopropyl acrylamide) (P(S-b-NIPAM)) diblock copolymers in deuterated water (D2O). Both structural changes and the changes of the segmental dynamics occurring upon heating through the lower critical solution temperature (LCST) of PNIPAM are studied using small-angle neutron scattering and neutron spin-echo spectroscopy. The collapse of the micellar shell and the cluster formation of collapsed micelles at the LCST as well as an increase of the segmental diffusion coefficient after crossing the LCST are detected. Comparing to our recent results on a triblock copolymer P(S-b-NIPAM-b-S) [25], we observe that the collapse transition of P(S-b-NIPAM) is more complex and that the PNIPAM segmental dynamics are faster than in P(S-b-NIPAM-b-S).},
  language  = {en}
}
@article{WellertTierschKoetzetal.2011,
  author    = {Wellert, Stefan and Tiersch, Brigitte and Koetz, Joachim and Richardt, Andre and Lapp, Alain and Holderer, Olaf and Gaeb, Juergen and Blum, Marc-Michael and Schulreich, Christoph and Stehle, Ralf and Hellweg, Thomas},
  title     = {The DFPase from Loligo vulgaris in sugar surfactant-based bicontinuous microemulsions structure, dynamics, and enzyme activity},
  series = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  volume    = {40},
  journal   = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  number    = {6},
  publisher = {Springer},
  address   = {New York},
  issn      = {0175-7571},
  doi       = {10.1007/s00249-011-0689-0},
  pages     = {761 -- 774},
  year      = {2011},
  abstract  = {The enzyme diisopropyl fluorophosphatase (DFPase) from the squid Loligo vulgaris is of great interest because of its ability to catalyze the hydrolysis of highly toxic organophosphates. In this work, the enzyme structure in solution (native state) was studied by use of different scattering methods. The results are compared with those from hydrodynamic model calculations based on the DFPase crystal structure. Bicontinuous microemulsions made of sugar surfactants are discussed as host systems for the DFPase. The microemulsion remains stable in the presence of the enzyme, which is shown by means of scattering experiments. Moreover, activity assays reveal that the DFPase still has high activity in this complex reaction medium. To complement the scattering experiments cryo-SEM was also employed to study the microemulsion structure.},
  language  = {en}
}