@article{VelkUhligVikulinaetal.2016,
  author    = {Velk, Natalia and Uhlig, Katja and Vikulina, Anna and Duschl, Claus and Volodkin, Dmitry},
  title     = {Mobility of lysozyme in poly(L-lysine)/hyaluronic acid multilayer films},
  series = {Colloids and surfaces : an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin ; B, Biointerfaces},
  volume    = {147},
  journal   = {Colloids and surfaces : an international journal devoted to fundamental and applied research on colloid and interfacial phenomena in relation to systems of biological origin ; B, Biointerfaces},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0927-7765},
  doi       = {10.1016/j.colsurfb.2016.07.055},
  pages     = {343 -- 350},
  year      = {2016},
  abstract  = {The spatial and temporal control over presentation of protein-based biomolecules such as growth factors and hormones is crucial for in vitro applications to mimic the complex in vivo environment. We investigated the interaction of a model protein lysozyme (Lys) with poly(L-lysine)/hyaluronic acid (PLL/HA) multilayer films. We focused on Lys diffusion as well as adsorption and retention within the film as a function of the film deposition conditions and post-treatment. Additionally, an effect of Lys concentration on its mobility was probed. A combination of confocal fluorescence microscopy, fluorescence recovery after photobleaching, and microfluidics was employed for this investigation. Our main finding is that adsorption of PLL and HA after protein loading induces acceleration and reduction of Lys mobility, respectively. These results suggest that a charge balance in the film to a high extent governs the protein-film interaction. We believe that control over protein mobility is a key to reach the full potential of the PLL/HA films as reservoirs for biomolecules depending on the application demand. (C) 2016 The Authors. Published by Elsevier B.V.},
  language  = {en}
}
@article{TrautweinFredrikssonMoelleretal.2016,
  author    = {Trautwein, Matthias and Fredriksson, Kai and M{\"o}ller, Heiko Michael and Exner, Thomas E.},
  title     = {Automated assignment of NMR chemical shifts based on a known structure and 4D spectra},
  series = {Journal of biomolecular NMR},
  volume    = {65},
  journal   = {Journal of biomolecular NMR},
  publisher = {Springer},
  address   = {Dordrecht},
  issn      = {0925-2738},
  doi       = {10.1007/s10858-016-0050-0},
  pages     = {217 -- 236},
  year      = {2016},
  abstract  = {Apart from their central role during 3D structure determination of proteins the backbone chemical shift assignment is the basis for a number of applications, like chemical shift perturbation mapping and studies on the dynamics of proteins. This assignment is not a trivial task even if a 3D protein structure is known and needs almost as much effort as the assignment for structure prediction if performed manually. We present here a new algorithm based solely on 4D [H-1, N-15]-HSQC-NOESY-[H-1, N-15]-HSQC spectra which is able to assign a large percentage of chemical shifts (73-82 \%) unambiguously, demonstrated with proteins up to a size of 250 residues. For the remaining residues, a small number of possible assignments is filtered out. This is done by comparing distances in the 3D structure to restraints obtained from the peak volumes in the 4D spectrum. Using dead-end elimination, assignments are removed in which at least one of the restraints is violated. Including additional information from chemical shift predictions, a complete unambiguous assignment was obtained for Ubiquitin and 95 \% of the residues were correctly assigned in the 251 residue-long N-terminal domain of enzyme I. The program including source code is available at https://github.com/thomasexner/4Dassign.},
  language  = {en}
}