Schuetz, P., Wuttke, R., Schuler, B., & Caflisch, A. (2010). Free energy surfaces from single-distance information. The Journal of Physical Chemistry B, 114(46), 15227-15235. https://doi.org/10.1021/jp1053698 (Original work published)
Vitalis, A., & Caflisch, A. (2010). Micelle-like architecture of the monomer ensemble of Alzheimer’s amyloid-β peptide in aqueous solution and its implications for Aβ aggregation. Journal of Molecular Biology, 403(1), 148-165. https://doi.org/10.1016/j.jmb.2010.08.003 (Original work published)
Qi, B., Muff, S., Caflisch, A., & Dinner, A. R. (2010). Extracting physically intuitive reaction coordinates from transition networks of a beta-sheet miniprotein. The Journal of Physical Chemistry B, 114(20), 6979-6989. https://doi.org/10.1021/jp101476g (Original work published)
Guarnera, E., Pellarin, R., & Caflisch, A. (2009). How does a simplified-sequence protein fold? Biophys J, 97(6), 1737-1746. https://doi.org/10.1016/j.bpj.2009.06.047 (Original work published)
Krivov, S. V., Muff, S., Caflisch, A., & Karplus, M. (2008). One-dimensional barrier-preserving free-energy projections of a beta-sheet miniprotein: New insights into the folding process. The Journal of Physical Chemistry B, 112(29), 8701-8714. https://doi.org/10.1021/jp711864r (Original work published)
Muff, S., & Caflisch, A. (2008). Kinetic analysis of molecular dynamics simulations reveals changes in the denatured state and switch of folding pathways upon single-point mutation of a beta-sheet miniprotein. Proteins: Structure, Function, and Bioinformatics, 70(4), 1185-1195. https://doi.org/10.1002/prot.21565 (Original work published 2008)
Interlandi, G., Wetzel, S. K., Settanni, G., Plückthun, A., & Caflisch, A. (2008). Characterization and further stabilization of designed ankyrin repeat proteins by combining molecular dynamics simulations and experiments. Journal of Molecular Biology, 375(3), 837-854. https://doi.org/10.1016/j.jmb.2007.09.042 (Original work published)
Seeber, M., Fanelli, F., Paci, E., & Caflisch, A. (2006). Sequential unfolding of individual helices of bacterioopsin observed in molecular dynamics simulations of extraction from the purple membrane. Biophysical Journal, 91(9), 3276-3284. https://doi.org/10.1529/biophysj.106.088591 (Original work published)
Interlandi, G., Settanni, G., & Caflisch, A. (2006). Unfolding transition state and intermediates of the tumor suppressor p16INK4a investigated by molecular dynamics simulations. Proteins: Structure, Function, and Bioinformatics, 64(1), 178-192. https://doi.org/10.1002/prot.20953 (Original work published)
Tartaglia, G. G., Pellarin, R., Cavalli, A., & Caflisch, A. (2005). Organism complexity anti-correlates with proteomic beta-aggregation propensity. Protein Science, 14(10), 2735-2740. https://doi.org/10.1110/ps.051473805 (Original work published 2005)