Publications of T Arnold

Michalik, M.; Orwick-Rydmark, M.; Habeck, M.; Alva, V.; Arnold, T.; Linke, D.: An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins. PLoS One 12 (8), e0182016 (2017)

Paulmann, M.; Arnold, T.; Linke, D.; Özdirekcan, S.; Kopp, A.; Gutsmann, T.; Kalbacher, H.; Wanke, I.; Schuenemann, V.; Habeck, M. et al.; Bürck, L.; Ulrich, A.; Schittek, B.: Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. Journal of Biological Chemistry 287 (11), pp. 8434 - 8443 (2012)

Gessmann, D.; Mager, F.; Naveed, H.; Arnold, T.; Weirich, S.; Linke, D.; Liang, J.; Nussberger, S.: Improving the resistance of a eukaryotic β-barrel protein to thermal and chemical perturbations. Journal of Molecular Biology 413 (1), pp. 150 - 161 (2011)

Arnold, T.; Zeth, K.; Linke, D.: Omp85 from the thermophilic cyanobacterium Thermosynechococcus elongatus differs from proteobacterial Omp85 in structure and domain composition. The Journal of Biological Chemistry 285 (23), pp. 18003 - 18015 (2010)

Arnold, T.; Zeth, K.; Linke, D.: Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain. The Journal of Biological Chemistry 284 (10), pp. 6403 - 6413 (2009)

Arnold, T.; Linke, D.: The use of detergents to purify membrane proteins. Current Protocols in Protein Science 53, pp. 4.8.1 - 4.8.30 (2008)

Arnold, T.; Linke, D.: Phase separation in the isolation and purification of membrane proteins. Biotechniques 43 (4), pp. 427 - 430 (2007)

Arnold, T.; Poynor, M.; Nussberger, S.; Lupas, A.; Linke, D.: Gene duplication of the eight-stranded beta-barrel OmpX produces a functional pore: a scenario for the evolution of transmembrane beta-barrels. Journal of Molecular Biology 366 (4), pp. 1174 - 1184 (2007)

Paulmann, M.; Zeth, K.; Arnold, T.; Senyürek, I.; Schünemann, V.; Kalbacher, H.; Linke, D.; Schittek, B.: The Dermcidin-derived antimicrobial peptide DCD-1L forms oligomeric structures and kills bacteria by interaction with the bacterial membrane. 37th Annual Meeting of the Arbeitsgemeinschaft Dermatologische Forschung (ADF), Lübeck, Germany (2010)