@article{KriegerowskiCescaOhrnbergeretal.2019,
  author    = {Kriegerowski, Marius and Cesca, Simone and Ohrnberger, Matthias and Dahm, Torsten and Kr{\"u}ger, Frank},
  title     = {Event couple spectral ratio Q method for earthquake clusters},
  series = {Solid Earth},
  journal   = {Solid Earth},
  number    = {10},
  publisher = {Copernicus Publications},
  address   = {G{\"o}ttingen},
  issn      = {1869-9529},
  doi       = {10.5194/se-10-317-2019},
  pages     = {317 -- 328},
  year      = {2019},
  abstract  = {We develop an amplitude spectral ratio method for event couples from clustered earthquakes to estimate seismic wave attenuation (Q-1) in the source volume. The method allows to study attenuation within the source region of earthquake swarms or aftershocks at depth, independent of wave path and attenuation between source region and surface station. We exploit the high-frequency slope of phase spectra using multitaper spectral estimates. The method is tested using simulated full wave-field seismograms affected by recorded noise and finite source rupture. The synthetic tests verify the approach and show that solutions are independent of focal mechanisms but also show that seismic noise may broaden the scatter of results. We apply the event couple spectral ratio method to northwest Bohemia, Czech Republic, a region characterized by the persistent occurrence of earthquake swarms in a confined source region at mid-crustal depth. Our method indicates a strong anomaly of high attenuation in the source region of the swarm with an averaged attenuation factor of Qp < 100. The application to S phases fails due to scattered P-phase energy interfering with S phases. The Qp anomaly supports the common hypothesis of highly fractured and fluid saturated rocks in the source region of the swarms in northwest Bohemia. However, high temperatures in a small volume around the swarms cannot be excluded to explain our observations.},
  language  = {en}
}
@article{BanerjeeLipowskySanter2020,
  author    = {Banerjee, Pallavi and Lipowsky, Reinhard and Santer, Mark},
  title     = {Coarse-grained molecular model for the Glycosylphosphatidylinositol anchor with and without protein},
  series = {Journal of Chemical Theory and Computation},
  volume    = {16},
  journal   = {Journal of Chemical Theory and Computation},
  number    = {6},
  publisher = {ACS Publications},
  address   = {Washington DC},
  issn      = {1549-9626},
  doi       = {10.1021/acs.jctc.0c00056},
  pages     = {15},
  year      = {2020},
  abstract  = {Glycosylphosphatidylinositol (GPI) anchors are a unique class of complex glycolipids that anchor a great variety of proteins to the extracellular leaflet of plasma membranes of eukaryotic cells. These anchors can exist either with or without an attached protein called GPI-anchored protein (GPI-AP) both in vitro and in vivo. Although GPIs are known to participate in a broad range of cellular functions, it is to a large extent unknown how these are related to GPI structure and composition. Their conformational flexibility and microheterogeneity make it difficult to study them experimentally. Simplified atomistic models are amenable to all-atom computer simulations in small lipid bilayer patches but not suitable for studying their partitioning and trafficking in complex and heterogeneous membranes. Here, we present a coarse-grained model of the GPI anchor constructed with a modified version of the MARTINI force field that is suited for modeling carbohydrates, proteins, and lipids in an aqueous environment using MARTINI's polarizable water. The nonbonded interactions for sugars were reparametrized by calculating their partitioning free energies between polar and apolar phases. In addition, sugar-sugar interactions were optimized by adjusting the second virial coefficients of osmotic pressures for solutions of glucose, sucrose, and trehalose to match with experimental data. With respect to the conformational dynamics of GPI-anchored green fluorescent protein, the accessible time scales are now at least an order of magnitude larger than for the all-atom system. This is particularly important for fine-tuning the mutual interactions of lipids, carbohydrates, and amino acids when comparing to experimental results. We discuss the prospective use of the coarse-grained GPI model for studying protein-sorting and trafficking in membrane models.},
  language  = {en}
}