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Department of Biochemistry

Calendar of Events

Publications of the Schuler Group (in alphabetical order)

König, I., Soranno, A., Nettels, D. & Schuler, B. Impact of In-Cell and In-Vitro Crowding on the Conformations and Dynamics of an Intrinsically Disordered Protein. Angew Chem Int Ed Engl 60, 10724-10729 (2021). PMID: 33587794.

Lerner, E., Barth, A., Hendrix, J., Ambrose, B., Birkedal, V., Blanchard, SC., Börner, R., Sung Chung, H., Cordes, T., Craggs, TD., Deniz, AA., Diao, J., Fei, J., Gonzalez, RL., Gopich, IV., Ha, T., Hanke, CA., Haran, G., Hatzakis, NS., Hohng, S., Hong, SC., Hugel, T., Ingargiola, A., Joo, C., Kapanidis, AN., Kim, HD., Laurence, T., Lee, NK., Lee, TH., Lemke, EA., Margeat, E., Michaelis, J., Michalet, X., Myong, S., Nettels, D., Peulen, TO., Ploetz, E., Razvag, Y., Robb, NC., Schuler, B., Soleimaninejad, H., Tang, C., Vafabakhsh, R., Lamb, DC., Seidel, CA. & Weiss, S. FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices. Elife 10, (2021). PMID: 33779550.

Ernst, P., Zosel, F., Reichen, C., Nettels, D., Schuler, B. & Plückthun, A. Structure-Guided Design of a Peptide Lock for Modular Peptide Binders. ACS Chem. Biol. 15, 457-468 (2020). PMID: 31985201.

Gosavi, S. & Schuler, B. Editorial overview: Molecular interactions that drive folding and binding: new challenges and opportunities. Curr. Opin. Struct. Biol. 60, iii-iv (2020). PMID: 32228883.

Schuler, B., Borgia, A., Borgia, MB., Heidarsson, PO., Holmstrom, ED., Nettels, D. & Sottini, A. Binding without folding - the biomolecular function of disordered polyelectrolyte complexes. Curr. Opin. Struct. Biol. 60, 66-76 (2020). PMID: 31874413.

Sottini, A., Borgia, A., Borgia, MB., Bugge, K., Nettels, D., Chowdhury, A., Heidarsson, PO., Zosel, F., Best, RB., Kragelund, BB. & Schuler, B. Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes. Nat Commun 11, 5736 (2020). PMID: 33184256.

Zijlstra, N., Nettels, D., Satija, R., Makarov, DE. & Schuler, B. Transition Path Dynamics of a Dielectric Particle in a Bistable Optical Trap. Phys Rev Lett 125, 146001 (2020). PMID: 33064519.

Zosel, F., Soranno, A., Buholzer, KJ., Nettels, D. & Schuler, B. Depletion interactions modulate the binding between disordered proteins in crowded environments. Proc. Natl. Acad. Sci. U.S.A. 117, 13480-13489 (2020). PMID: 32487732.

Assenza, S., Sassi, AS., Kellner, R., Schuler, B., De Los Rios, P. & Barducci, A. Efficient conversion of chemical energy into mechanical work by Hsp70 chaperones. Elife 8, e4891 (2019). PMID: 31845888.

Davey, NE., Babu, MM., Blackledge, M., Bridge, A., Capella-Gutierrez, S., Dosztanyi, Z., Drysdale, R., Edwards, RJ., Elofsson, A., Felli, IC., Gibson, TJ., Gutmanas, A., Hancock, JM., Harrow, J., Higgins, D., Jeffries, CM., Le Mercier, P., Mészáros, B., Necci, M., Notredame, C., Orchard, S., Ouzounis, CA., Pancsa, R., Papaleo, E., Pierattelli, R., Piovesan, D., Promponas, VJ., Ruch, P., Rustici, G., Romero, P., Sarntivijai, S., Saunders, G., Schuler, B., Sharan, M., Shields, DC., Sussman, JL., Tedds, JA., Tompa, P., Turewicz, M., Vondrasek, J., Vranken, WF., Wallace, BA., Wichapong, K. & Tosatto, SCE. An intrinsically disordered proteins community for ELIXIR. F1000Res 8, (2019). PMID: 31824649.

Holmstrom, ED., Liu, Z., Nettels, D., Best, RB. & Schuler, B. Disordered RNA chaperones can enhance nucleic acid folding via local charge screening. Nat Commun 10, 2453 (2019). PMID: 31165735.

Schuler, B., Borgia, A., Borgia, MB., Heidarsson, PO., Holmstrom, ED., Nettels, D. & Sottini, A. Binding without folding - the biomolecular function of disordered polyelectrolyte complexes. Curr. Opin. Struct. Biol. 60, 66-76 (2019). PMID: 31874413.

Best RB, Zheng W, Borgia A, Buholzer K, Borgia MB, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A & Schuler B. Comment on "innovative scattering analysis shows that hydophobic disordered proteins are expanded in water". Science 361, (2018). PMID: 30166459.

Borgia, A., Borgia, MB., Bugge, K., Kissling, VM., Heidarsson, PO., Fernandes, CB., Sottini, A., Soranno, A., Buholzer, KJ., Nettels, D., Kragelund, BB., Best, RB. &  Schuler, B.Extreme disorder in an ultrahigh-affinity protein complex. Nature 555, 61-66 (2018). PMID: 29466338.

Dingfelder F, Benke S, Nettels D & Schuler B. Mapping an equilibrium folding intermediate of the cytolytic pore toxin ClyA with single-molecule FRET. J Phys Chem B. 122, 11251-11261 (2018). PMID: 30156409.

Grotz, K., Nüesch, M., Holmstrom, E., Heinz, M., Stelzl, LS., Schuler, B. & Hummer, G. Dispersion correction alleviates dye stacking of single-stranded DNA and RNA in simulations of single-molecule fluorescence experiments. J Phys. Chem B. Oct 122, 11626-11639 (2018). PMID: 30285443.

Hansen, S., Ernst, P., König, SLB., Reichen, C., Ewald, C., Nettels, D., Mittl, PRE., Schuler, B. & Plückthun, A. Curvature of deignes armadillo repeat proteins allows modular peptide binding. J Struct Biol. 201 108-117 (2018). PMID: 28864298.

Hellenkamp, B., Schmid, S., Doroshenko, O., Opanasyuk, O., Kühnemuth, R., Adariani, SR., Ambrose, B., Aznauryan, M., Barth, A., Birkedal, V., Bowen, ME., Chen, H., Cordes, T., Eilert, T., Fijen, C., Gebhardt, C., Götz, M., Gouridis, G., Gratton, E., Ha, T., Hao, P., Hanke, CA., Hartmann, A., Hendrix, J., Hildebrandt, LL., Hirschfeld, V., Hohlbein, J., Hua, B., Hübner, CG., Kallis, E., Kapanidis, AN., Kim, JY., Krainer, G., Lamb, DC., Lee, NK., Lemke, EA., Levesque, B., Levitus, M., McCann, JJ., Naredi-Rainer, N., Nettels, D., Ngo, T., Qiu, R., Robb, NC., Röcker, C., Sanabria, H., Schlierf, M., Schröder, T., Schuler, B., Seidel, H., Streit, L., Thurn, J., Tinnefeld, P., Tyagi, S., Vandenberk, N., Vera, AM., Weninger, KR., Wünsch, B., Yanez-Orozco, IS., Michaelis, J., Seidel, CAM., Craggs, TD. & Hugel, T. Publisher Correction: Precision and accuracy of single-molecule FRET measurements-a multi-laboratory benchmark study. Nat. Methods 15, 984 (2018). PMID: 30327572.

Hellenkamp B, Schmid S, Doroshenko O, Opanasyuk O, Kühnemuth R, Rezaei Adariani S, Ambrose B, Aznauryan M, Barth A, Birkedal V, Bowen ME, Chen H, Cordes T, Eilert T, Fijen C, Gebhardt C, Götz M, Gouridis G, Gratton E, Ha T, Hao P, Hanke CA, Hartmann A, Hendrix J, Hildebrandt LL, Hirschfeld V, Hohlbein J, Hua B, Hübner CG, Kallis E, Kapanidis AN, Kim JY, Krainer G, Lamb DC, Lee NK, Lemke EA, Levesque B, Levitus M, McCann JJ, Naredi-Rainer N, Nettels D, Ngo T, Qiu R, Robb NC, Röcker C, Sanabria H, Schlierf M, Schröder T, Schuler B, Seidel H, Streit L, Thurn J, Tinnefeld P, Tyagi S, Vandenberk N, Vera AM, Weninger KR, Wünsch B, Yanez-Orozco IS, Michaelis J, Seidel CAM, Craggs TD & Hugel T. Precision and accuracy of single-molecule FRET measurements - a multi-laboratory benchmark study. Nat Methods. 15, 669-676 (2018). PMID: 30171252.

Holmstrom, ED., Nettels, D. & Schuler, B. Conformational plasticity of hepatitis C virus core protein enables RNA-induced formation of nucleocapsid-like particles. J Mol Biol. 430, 2453-2467 (2018). PMID: 29045818.

Holmstrom, ED., Holla, A., Zheng, W., Nettels, D., Best, RB. & Schuler, B. Accurate Transfer Efficiencies, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRET. Meth. Enzymol. 611, 287-325 (2018). PMID: 30471690.

Makarov, DE. & Schuler, B. Preface: Special Topic on single-molecule biophysics. J Chem Phys. 148, 123001 (2018). PMID: 29604869.

Marino, J., Buholzer, KJ., Zosel, F., Nettels, D. & Schuler, B. Charge interactions can dominate coupled folding and binding on the ribosome. Biophys. J. 115, 996-1006 (2018). PMID: 30173887.

Masliah, G., Maris, C., König, SL., Yulikov, M., Aeschimann, F., Malinowska, AL., Mabille, J., Weiler, J., Holla, A., Hunziker, J., Meisner-Kober, N., Schuler, B., Jeschke, G. & Allain, FH. Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains. EMBO J. 37(6), e97089 (2018). PMID: 29449323

Morger, D., Zosel, F., Bühlmann, M., Züger, S., Mittelviefhaus, M., Schuler, B., Luban, J. &  Grütter, MG.The three-fold axis of the HIV-1 capsid lattice is the species-specific binding interface for TRIM5  alpha. J. Virol. 92(5), e01541-17 (2018).  PMID: 29237846.

Reinartz, I., Sinner, C., Nettels, D., Stucki-Buchli, B., Stockmar, F., Panek, PT., Jacob, CR., Nienhaus, GU., Schuler, B. & Schug, A. Simulation of FRET dyes allows quantitative comparison against experimental data. J Chem Phys 148, 123321 (2018). PMID: 29604831.

Rezaei-Ghaleh N, Parigi G, Soranno A, Holla A, Becker S, Schuler B, Luchinat C & Zweckstetter M. Local and global dynamics in intrinsically disordered synuclein. Angew Chem Int Ed Engl. 57, 15262-15266 (2018). PMID: 30184304.

Schuler, B. Perspective: cahin dynamics of unfolded and intrinsically disordered proteins from nansecond fluorescence correlation spectroscopy combined with single-molecule FRET. J Chem Phys. 149:010901 (2018). PMID: 29981536.

Schuler, B., Szabo, A. & Wolynes, PG. Tribute to William A. Eaton. J Phys Chem B 122, 10971-10973 (2018). PMID: 30986080.

Sturzenegger, F., Zosel, F., Holmstrom, ED., Buholzer, KJ., Makarov, DE., Nettels, D. & Schuler, B. Transition path times of coupled folding and binding reveal the formation of an encounter complex. Nat Commun 9, 4708 (2018). PMID: 30413694.

Zheng, W., Zerze, GH., Borgia, A., Mittal, J., Schuler, B. & Best, RB. Inferring properties of disordered chains from FRET transfer efficiencies. J Chem Phys. 148, 123329 (2018). PMID: 29604882.

Zosel, F., Mercadante, D., Nettels, D. & Schuler, B. A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction. Nat Commun. 9,  3332 (2018). PMID: 30127362.

Benke, S., Nettels, D., Hofmann, H. & Schuler, B. Quantifying kinetics from time series of single-molecule Förster resonance energy transfer efficiency histograms. Nanotechnology 28, 114002 (2017). PMID: 28103588.

Dingfelder, F., Wunderlich, B., Benke, S., Zosel, F., Zijlstra, N., Nettels, D. & Schuler, B. Rapid Microfluidic Double-Jump Mixing Device for Single-Molecule Spectroscopy. J. Am. Chem. Soc. 139, 6062-6065 (2017). PMID: 28394601.

Hansen, S., Ernst, P., König, SLB., Reichen, C., Ewald, C., Nettels, D., Mittl, PRE., Schuler, B. & Plückthun, A. Curvature of deignes armadillo repeat proteins allows modular peptide binding. J Struct Biol. [Epub ahead of print] (2017). PMID: 28864298.
Marino, J., Holzhüter, K., Kuhn, B. & Geertsma, ER. Efficient Screening and Optimization of Membrane Protein Production in Escherichia coli. Meth. Enzymol. 594, 139-164 (2017). PMID: 28779839.

Plitzko, JM., Schuler, B. & Selenko, P. Structural Biology outside the box-inside the cell. Curr. Opin. Struct. Biol. 46, 110-121 (2017). PMID: 28735108. 

Ruggeri, F., Zosel, F., Mutter, N., Różycka, M., Wojtas, M., Ożyhar, A., Schuler, B. & Krishnan, M. Single-molecule electrometry. Nat Nanotechnol 12, 488-495 (2017). PMID: 28288117.

Soranno, A., Holla, A., Dingfelder, F., Nettels, D., Makarov, DE. & Schuler, B. Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations. Proc. Natl. Acad. Sci. U.S.A. 114, E1833-E1839 (2017). PMID: 28223518.

Zheng, W., Hofmann, H., Schuler, B. & Best, RB. Origin of internal friction in disordered proteins depends on solvent quality. J Phys. Chem B. Oct 122, 11478-11487 (2018). PMID: 30277791.

Zijlstra, N., Dingfelder, F., Wunderlich, B., Zosel, F., Benke, S., Nettels, D. & Schuler, B. Rapid Microfluidic Dilution for Single-Molecule Spectroscopy of Low-Affinity Biomolecular Complexes. Angew. Chem. Int. Ed. Engl. 56, 7126-7129 (2017). PMID: 28510311.

Zosel, F., Haenni, D., Soranno, A., Nettels, D. & Schuler, B. Combining short- and long-range fluorescence reporters with simulations to explore the intramolecular dynamics of an intrinsically disordered protein. J Chem Phys 147, 152708 (2017). PMID: 29055320.

Aznauryan, M., Delgado, L., Soranno, A., Nettels, D., Huang, JR., Labhardt, AM., Grzesiek, S. & Schuler, B. Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR and SAXS. Proc Natl Acad Sci U S A 113, E5389-98 (20169. PMID: 2756640.

Benke, S., Roderer, D., Wunderlich, B., Nettels, D., Glockshuber, R. & Schuler, B. Erratum: The assembly dynamics of the cytolytic pore toxin ClyA. Nat Commun 7, 10650 (2016). PMID: 26830972.

Borgia, A., Zheng, W., Buholzer, K., Borgia, MB., Schüler, A., Hofmann, H., Soranno, A., Nettels, D., Gast, K., Grishaev, A., Best, RB. & Schuler, B. Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods. J. Am. Chem. Soc. 138, 11714-26 (2016). PMID: 27583570.

Roderer, D., Benke, S., Schuler, B. & Glockshuber, R. Soluble oligomers of the pore-forming toxin Cytolysin A from Escherichia coli are off-pathway products of pore assembly. J. Biol. Chem. 291, 5652-63 (2016). PMID: 26757820.

Schuler, B., Soranno, A., Hofmann, H. & Nettels, D. Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins. Annu Rev Biophys [Epub ahead of print] (2016). PMID: 27145874.

Zheng, W., Borgia, A., Buholzer, K., Grishaev, A., Schuler, B. & Best, RB. Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment. J. Am. Chem. Soc. 138, 11702-13 (2016. PMID: 27583687.

Benke, S., Roderer, D., Wunderlich, B., Nettels, D., Glockshuber, R. & Schuler, B. The assembly dynamics of the cytolytic pore toxin ClyA. Nat Commun 6, 6198 (2015). PMID: 25652783.

Best, RB., Hofmann, H., Nettels, D. & Schuler, B. Quantitative interpretation of FRET experiments via molecular simulation: force field and validation. Biophys. J. 108, 2721-31 (2015). PMID: 26039173.

Borgia, A., Kemplen, KR., Borgia, MB., Soranno, A., Shammas, S., Wunderlich, B., Nettels, D., Best, RB., Clarke, J. & Schuler, B. Transient misfolding dominates multidomain protein folding. Nat Commun 6, 8861 (2015). PMID: 26572969.

Czar, MF., Zosel, F., König, I., Nettels, D., Wunderlich, B., Schuler, B., Zarrine-Afsar, A. & Jockusch, RA. Gas-Phase FRET Efficiency Measurements To Probe the Conformation of Mass-Selected Proteins. Anal. Chem. 87, 7559-65 (2015). PMID: 26110465.

König, I., Zarrine-Afsar, A., Aznauryan, M., Soranno, A., Wunderlich, B., Dingfelder, F., Stüber, JC., Plückthun, A., Nettels, D. & Schuler, B. Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells. Nat. Methods 12, 773-9 (2015). PMID: 26147918.

Nettels, D., Haenni, D., Maillot, S., Gueye, M., Barth, A., Hirschfeld, V., Hübner, CG., Léonard, J. & Schuler, B. Excited-state annihilation reduces power dependence of single-molecule FRET experiments. Phys Chem Chem Phys 17, 32304-15 (2015). PMID: 26584062.

Schuler, BD. & Smith, JL. Editorial overview: Biophysical and molecular biological methods: Structure, dynamics, and single molecules. Curr. Opin. Struct. Biol. 34, iv-vi (2015). PMID: 26547527.

Yuan, H., Gaiduk, A., Siekierzycka, JR., Fujiyoshi, S., Matsushita, M., Nettels, D., Schuler, B., Seidel, CA. & Orrit, M. Temperature-cycle microscopy reveals single-molecule conformational heterogeneity. Phys Chem Chem Phys 17, 6532-44 (2015). PMID: 25659944.

Zheng, W., Borgia, A., Borgia, MB., Schuler, B. & Best, RB. Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations. J Chem Theory Comput 11, 5543-53 (2015). PMID: 26574341.

Brucale, M., Schuler, B. & Samorì, B. Single-Molecule Studies of Intrinsically Disordered Proteins. Chem. Rev. Chem. Rev. 114, 3281-317 (2014). PMID: 24432838.

Hofmann, H., Hillger, F., Delley, C., Hoffmann, A., Pfeil, SH., Nettels, D., Lipman, EA. & Schuler, B. Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy. Biophys. J. 107, 2882-93 (2014). PMID: 25517154.

Kellner, R., Hofmann, H., Barducci, A., Wunderlich, B., Nettels, D. & Schuler, B. Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein. Proc. Natl. Acad. Sci. U.S.A. 111, 13355-60 (2014). PMID: 25165400.

Pochorovski, I., Knehans, T., Nettels, D., Müller, AM., Schweizer, WB., Caflisch, A., Schuler, B. & Diederich, F. Experimental and Computational Study of BODIPY Dye-Labeled Cavitand Dynamics. J. Am. Chem. Soc. 136, 2441-9 (2014). PMID: 24490940.

Roderer, D., Benke, S., Müller, M., Fäh-Rechsteiner, H., Ban, N., Schuler, B. & Glockshuber, R. Characterization of Variants of the Pore-Forming Toxin ClyA from Escherichia coli Controlled by a Redox Switch. Biochemistry 53, 6357-69 (2014). PMID: 25222267.

Soranno, A., Koenig, I., Borgia, MB., Hofmann, H., Zosel, F., Nettels, D. & Schuler, B. Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments. Proc. Natl. Acad. Sci. U.S.A. 111, 4874-9 (2014). PMID: 24639500.

Weisenburger, S., Jing, B., Hänni, D., Reymond, L., Schuler, B., Renn, A. & Sandoghdar, V. Cryogenic Colocalization Microscopy for Nanometer-Distance Measurements. Chemphyschem [Epub ahead of print] (2014). PMID: 24677759.

Wunderlich, B., Nettels, D. & Schuler, B. Taylor dispersion and the position-to-time conversion in microfluidic mixing devices. Lab Chip 14, 219-28 (2014). PMID: 24195996.

Wuttke, R., Hofmann, H., Nettels, D., Borgia, MB., Mittal, J., Best, RB. & Schuler, B. Temperature-dependent solvation modulates the dimensions of disordered proteins. Proc. Natl. Acad. Sci. U.S.A. 111, 5213-8 (2014). PMID: 24706910.

Aznauryan, M., Nettels, D., Holla, A., Hofmann, H. & Schuler, B. Single-molecule spectroscopy of cold denaturation and the temperature-induced collapse of unfolded proteins. J. Am. Chem. Soc. 135, 14040-3 (2013).

Haenni, D.,Zosel, F., Reymond, L., Nettels, D. & Schuler, B. Intramolecular distances and dynamics from the combined photon statistics of single-molecule FRET and photoinduced electron transfer. J Phys Che B. 117, 13015-23028 (2013).

Hofmann, H., Nettels, D. & Schuler, B. Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH. J Chem Phys 139, 121930 (2013).

Schuler, B. Single-molecule FRET of protein structure and dynamics - a primer. J Nanobiotechnology 11 Suppl 1, S2 (2013).

Schuler, B. & Hofmann, H. Single-molecule spectroscopy of protein folding dynamics-expanding scope and timescales. Curr Opin Struct Biol. 23, 36-47 (2013).

Schuler, B. & Clarke, J. Biophysics: rough passage across a barrier. Nature 502, 632-633 (2013).

Wunderlich, B., Nettels, D., Benke, S., Clark, J., Weidner, S., Hofmann, H., Pfeil, SH. & Schuler, B. Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes. Nat Protocols 8, 1459-1474 (2013).

Borgia, A., Wensley, BG., Soranno, A., Nettels, D., Borgia, MB., Hoffmann, A., Pfeil, SH., Lipamn, EA., Clarke, J. & Schuler, B. Localizing internal friction along the reaction corrdinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy. Nat Commun. 3, 1195 (2012).

Hofmann, H., Soranno, A., Borgia, A., Gast, K., Nettels, D. & Schuler, B. Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy. PNAS USA 109, 16155-16160 (2012).

Nettels, D., Hoffmann, A. & Schuler, B. Corrections to "Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds. J Phys Chem B. 112, 6137-6146 (2012).

Schuler, B., Müller-Späth, S., Soranno, A. & Nettels, D. Application of confocal single-molecule FRET to intrinsically disordered proteins. Methods Mol Biol 896, 21-45 (2012).

Soranno, A., Buchli, B., Nettels, D., Cheng, RR., Müller-Späth, S., Pfeil, SH., Hoffmann, A., Lipman, EA., Makarov, DE. & Schuler, B. Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy. PNAS 109,17800-17806 (2012).

Borgia, MB., Borgia, A., Best, RB., Steward, A., Nettels, D., Wunderlich, B., Schuler, B. & Clarke, J. Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins. Nature 474, 662-665 (2011).

Hoefling, M., Lima, N., Haenni, D., Seidel, CA., Schuler, B. & Grubmüller, H. Structural heterogeneity and quantitative FRET efficiency distributions of polyprolines through a hybrid atomistic simulation and Monte Carlo approach. "PloS one"6(5):e 19791 (2011).

Hoffmann, A., Nettels, D., Clark, J., Borgia, A., Radford, SE., Clarke, J. & Schuler, B. Quantifying heterogeneity and conformational dynamics from single molecule FRET of diffusing molecules: recurrence analysis of single particles. Phys Chem Chem Phys. 13, 1857-1871 (2011).

Yuan, H., Xia, T., Schuler, B. & Orrit, M. Temperature-cycle single-molecule FRET microscopy on polyprolines. Phys Chem Chem Phys. 13, 1762-1769 (2011).

Hofmann H, Hillger F, Pfeil SH, Hoffmann A, Streich D, Haenni D, Nettels D, Lipman EA & Schuler B. Single-molecule spectroscopy of protein folding in a chaperonin cage. Proc Natl Acad Sci U S A. 107, 11793-11798 (2010).

Müller-Späth, S., Soranno, A., Hirschfeld, V., Hofmann, H., Rüegger, S., Reymond, L., Nettels, D. & Schuler, B. Charge interactions can dominate the dimensions of intrinsically disordered proteins. Proc Natl Acad Sci U S A. 107, 14609-14614 (2010).

Schütz, P.,Wuttke, R., Schuler, B. & Caflisch, A. Free energy surfaces from single-distance information. J. Phys. Chem. B. 114, 15227-15235 (2010).  

Gopich, IV., Nettels, D., Schuler, B. & Szabo, A. Protein dynamics from single-molecule fluorescence intensity correlation functions. J Chem Phys. 131, 095102 (2009).

Nettels, D., Müller-Späth, S., Küster, F., Hofmann, H., Haenni, D., Rüegger, S., Reymond, L., Hoffmann, A., Kubelka, J., Heinz, B., Gast, K., Best, RB. & Schuler, B. Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins. Proc Natl Acad Sci U S A. 106, 20740-20745 (2009). 

Hillger, F., Hänni, D., Nettels, D., Geister, S., Grandin, M., Textor, M. & Schuler, B. Probing Protein-Chaperone Interactions with Single-Molecule Fluorescence Spectroscopy. Angew Chem Int Ed Engl47, 6184-6188 (2008).

Kane, AS., Hoffmann, A., Baumgärtel, P., Seckler, R., Reichardt, G., Horsley, DA., Schuler, B. & Bakajin, O. Microfluid mixers for the investigation of rapid protein folding kinetics using synchrotron radiation circular dichroism spectroscopy. Anal. Chem. 80, 9534-9541 (2008). 

Nettels, D., Hoffmann, A. & Schuler, B. Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds. J Phys Chem B. 112, 6137-6146 (2008).

Schuler, B. Single molecule spectroscopy in protein folding: from ensembles to single molecules. In: Protein Folding, Misfolding and Aggregation (ed. Munoz, V.) Cambridge, UK, p. 139-160 (2008).

Schuler, B. & Eaton, WA. Protein folding studied by single-molecule FRET. Curr. Opin. Struct. Biol. 18, 16-26 (2008).

Wahl, M., Rahn, HJ., Röhlicke, T., Kell, G., Nettels, D., Hillger, F., Schuler, B. & Erdmann, R. Scalable time-correlated photon counting system with multiple independent input channels. Rev. Sci. Instrum. 79, 123113-1 - 123113-8 (2008).

Best, RB., Merchant, KA., Gopich, IV., Schuler, B., Bax, A. & Eaton, WA. Effect of flexibility and cis residues in single-molecule FRET studies of polyproline. PNAS U.S.A. 104, 18964-18969 (2007). 

Hillger, F., Nettels, D., Dorsch, S. & Schuler B. Detection and Analysis of Protein Aggregation with Confocal Single Molecule Fluorescence Spectroscopy. J. Fluoresc. 17, 759-765 (2007).

Hoffmann, A., Kane, A.,Nettels, D., Hertzog, D., Baumgärtel, P., Lengefeld, J., Reichardt, G., Horsley, D.A., Seckler, R., Bakajin, O & Schuler, B. Mapping protein collapse with single molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy. Proc. Natl. Acad. Sci. USA 104, 105-110 (2007).

Nettels, D., Gopich, I. V., Hoffmann, A. & Schuler, B. Ultrafast dynamics of protein collapse from single molecule photon statistics. Proc. Natl. Acad. Sci. USA 104, 2655-2660 (2007).

Nettels, D. & Schuler, B. Subpopulation-resolved photon statistics of single-molecule energy transfer dynamics. IEEE J. Sel. Top. Quant. Electron. 13, 990-995 (2007). 

Schuler, B., Application of Single Molecule Förster Resonance Energy Transfer to Protein Folding. in: Protein Folding Protocols (Humana Press; Bai, Nussinov, Eds.), Methods Mol. Biol. 350, 115-138 (2007). 

Schuler, B. & Haran, G. Protein folding and dynamics from optical single molecule spectroscopy. In: Single Molecules and Nanotechnolgy (eds. Rigler, R. & Vogel, H.) (in press).

Camenisch, U., Dip, R., Schumacher, S. B., Schuler, B. & Naegeli, H. Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair. Nature Struct. & Mol. Biol. 13, 278-284 (2006).

Schuler, B. Single-molecule fluorescence spectroscopy of protein folding. Chem.Phys.Chem. 6, 1206-1220 (2005).

Schuler, B., Lipman, E. A., Steinbach, P. J., Kumke, M. & Eaton, W. A. Polyproline and the "spectroscopic ruler" revisited with single molecule fluorescence. Proc. Natl. Acad. Sci. USA 102, 2754-2759 (2005).

Rhoades, E., Cohen, M., Schuler, B. & Haran, G. Two-state folding observed in individual protein molecules. J. Am. Chem. Soc. 126, 14686-14687 (2004).

Buscaglia, M., Schuler, B., Lapidus, L. J., Eaton, W. A. & Hofrichter, J. Kinetics of intramolecular contact formation in a denatured protein. J. Mol. Biol. 332, 9-12 (2003).

Kremer, W., Arnold, M. R., Brunner, E., Schuler, B., Jaenicke, R. & Kalbitzer, H. R. in Advances in High Pressure Bioscience and Biotechnology II (ed. Winter, R.) 101-112 (Springer Verlag, Berlin Heidelberg New York, 2003).

Lipman, E. A., Schuler, B., Bakajin, O. & Eaton, W. A. Single-molecule measurement of protein folding kinetics. Science 301, 1233-1235 (2003).

Tolan, D. R., Schuler, B., Beernink, P. T. & Jaenicke, R. Thermodynamic analysis of the dissociation of the aldolase tetramer substituted at one or both of the subunit interfaces. Biol. Chem. 384, 1463-1471 (2003).

Schuler, B., Kremer, W., Kalbitzer, H. R. & Jaenicke, R. Role of entropy in protein thermostability: Folding kinetics of a hyperthermophilic cold shock protein at high temperatures using F-19 NMR. Biochemistry 41, 11670-11680 (2002).

Schuler, B., Lipman, E. A. & Eaton, W. A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature 419, 743-747 (2002).

Schuler, B. & Pannell, L. K. Specific labeling of polypeptides at amino-terminal cysteine residues using Cy5-benzyl thioester. Bioconjug. Chem. 13, 1039-43 (2002).

Kremer, W., Schuler, B., Harrieder, S., Geyer, M., Gronwald, W., Welker, C., Jaenicke, R. & Kalbitzer, H. R. Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima. Eur. J. Biochem. 268, 2527-39. (2001).

Schuler, B., Furst, F., Osterroth, F., Steinbacher, S., Huber, R. & Seckler, R. Plasticity and steric strain in a parallel beta-helix: rational mutations in the P22 tailspike protein. Proteins 39, 89-101. (2000).

Schuler, B., Rachel, R. & Seckler, R. Formation of fibrous aggregates from a non-native intermediate: the isolated P22 tailspike beta-helix domain. J. Biol. Chem. 274, 18589-96. (1999).

Miller, S., Schuler, B. & Seckler, R. A reversibly unfolding fragment of P22 tailspike protein with native structure: the isolated beta-helix domain. Biochemistry 37, 9160-8 (1998).

Miller, S., Schuler, B. & Seckler, R. Phage P22 tailspike protein: removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability. Protein Sci. 7, 2223-32. (1998).

Schuler, B. & Seckler, R. P22 tailspike folding mutants revisited: effects on the thermodynamic stability of the isolated beta-helix domain. J. Mol. Biol. 281, 227-34. (1998).