Researcher Portfolio

 
   

Kappel, Christian

Central Scientific Facility Thin Film Laboratory, Max Planck Institute for Intelligent Systems, Max Planck Society, Dept. New Materials and Biosystems, Max Planck Institute for Intelligent Systems, Max Planck Society  

 

Researcher Profile

 
Position:
Position: Dept. New Materials and Biosystems, Max Planck Institute for Intelligent Systems, Max Planck Society
Position: Central Scientific Facility Thin Film Laboratory, Max Planck Institute for Intelligent Systems, Max Planck Society
Researcher ID: https://pure.mpg.de/cone/persons/resource/persons15299

External references

 
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Publications

 
 
 : Guasch, J., Conings, B., Neubauer, S., Rechenmacher, F., Ende, K., Rolli, C. G., Kappel, C., Schaufler, V., Micoulet, A., Kessler, H., Boyen, H.-G., Cavalcanti-Adam, E. A., & Spatz, J. P. (2015). Segregation Versus Colocalization: Orthogonally Functionalized Binary Micropatterned Substrates Regulate the Molecular Distribution in Focal Adhesions. Advanced Materials, 27, 3737-3747. doi:10.1002/adma.201500900. [PubMan] : Doelker, N., Blanchet, C. E., Voss, B., Haselbach, D., Kappel, C., Monecke, T., Svergun, D. I., Stark, H., Ficner, R., Zachariae, U., Grubmüller, H., & Dickmanns, A. (2013). Structural determinants and mechanism of mammalian CRM1 allostery. Structure, 21(8), 1350-1360. doi:10.1016/j.str.2013.05.015. [PubMan] : Herrmann, A., Sieben, C., Kappel, C., Zhu, R., Ranki, C., Wozniak, A., Hinterdorfer, P., & Grubmüller, H. (2013). Influenza virus binds its host cell using multiple dynamic interactions revealed by single virus force spectroscopy and force probe molecular dynamics. Biophysical Journal, 104(Suppl. 1), 415A-415A. [PubMan] : Sieben, C., Kappel, C., Zhu, R., Wozniak, A., Rankl, C., Hinterdorfer, P., Grubmüller, H., & Herrmann, A. (2012). Influenza virus binds its host cell using multiple dynamic interactions. Proceedings of the National Academy of Sciences of the United States of America, 106(34), 13626-13631. doi:10.1073/pnas.1120265109. [PubMan] : Kappel, C., Doelker, N., Kumar, R., & Grubmüller, H. (2012). Universal relaxation governs the nonequilibrium elasticity of biomolecules. Physical Review Letters, 109(11): 118304. doi:10.1103/PhysRevLett.109.118304. [PubMan] : Kappel, C. (2011). Structure and dynamics of proteins under force. PhD Thesis, Georg-August-Universität Göttingen, Göttingen. [PubMan] : Kappel, C., & Grubmüller, H. (2011). Velocity-dependent mechanical unfolding of bacteriorhodopsin is governed by a dynamic interaction network. Biophysical Journal, 100(4), 1109-1119. [PubMan] : Kappel, C., Zachariae, U., Dölker, N., & Grubmüller, H. (2010). An unusual hydrophobic core confers extreme flexibility to HEAT repeat proteins. Biophysical Journal, 99(5), 1596-1603. doi:10.1016/j.bpj.2010.06.032. [PubMan] : Bockmann, R., Kappel, C., & Grubmueller, H. (2007). Molecular dynamics simulation of lipids and lipid embossed proteins. Chemistry and Physics of Lipids, 149(Suppl. S), S4-S4. [PubMan] : Kappel, C. (2007). Enforced unfolding of bacteriorhodopsin via force probe molecular dynamics. Diploma Thesis, Universität Göttingen, Göttingen. [PubMan] : Kappel, C., & Grubmueller, H. (2007). Mechanical unfolding of bacteriorhodopsin via force probe molecular dynamics. Biophysical Journal, (Suppl. S), 555A-555A. [PubMan]