54 results match your criteria: "Germany [2] Karlsruhe Institute for Technology KIT[Affiliation]"
Microsc Microanal
April 2014
2 Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232-0615, USA.
In this study, a combined tilt- and focal series is proposed as a new recording scheme for high-angle annular dark-field scanning transmission electron microscopy (STEM) tomography. Three-dimensional (3D) data were acquired by mechanically tilting the specimen, and recording a through-focal series at each tilt direction. The sample was a whole-mount macrophage cell with embedded gold nanoparticles.
View Article and Find Full Text PDFActa Crystallogr D Biol Crystallogr
January 2014
Department of Biochemistry, University of Oulu, Oulu, Finland.
P2 is a fatty acid-binding protein expressed in vertebrate peripheral nerve myelin, where it may function in bilayer stacking and lipid transport. P2 binds to phospholipid membranes through its positively charged surface and a hydrophobic tip, and accommodates fatty acids inside its barrel structure. The structure of human P2 refined at the ultrahigh resolution of 0.
View Article and Find Full Text PDFBiochim Biophys Acta
March 2014
Karlsruhe Institute for Technology (KIT), Institute for Biological Interfaces (IBG-2), POB 3640, 76021 Karlsruhe, Germany; KIT, Institute of Organic Chemistry and CFN, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany. Electronic address:
BP100 is a multifunctional membrane-active peptide of only 11 amino acids, with a high antimicrobial activity, an efficient cell-penetrating ability, and low hemolytic side-effects. It forms an amphiphilic α-helix, similar to other antimicrobial peptides like magainin. However, BP100 is very short and thus unlikely to form membrane-spanning pores as proposed for longer peptides as a mechanism of action.
View Article and Find Full Text PDFBeilstein J Nanotechnol
July 2013
National Institute for Materials Science (NIMS), 1-2-1 Sengen, Tsukuba-city Ibaraki 305-0047, Japan ; Physikalisches Institut, Karlsruhe Institute for Technology (KIT), 76131 Karlsruhe, Germany.
The growth mode of small Ni clusters evaporated in UHV on HOPG has been investigated by scanning tunnelling microscopy. The size, the size distribution, and the shape of the clusters have been evaluated for different evaporation conditions and annealing temperatures. The total coverage of the surface strongly depends on the evaporation rate and time, whereas the influence of these parameters is low on the cluster size.
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