Ben Schuler Research Group

PEOPLE

PROJECTS

PAPERS

University of Zurich

Selected recent publications

 

Borgia, A., Borgia, M., Bugge, K., Kissling, V.M., Heidarsson, P.O., Fernandes, C.B., Sottini, A., Soranno, A., Buholzer, K., Nettels, D., Kragelund, B.B., Best, R.B., & Schuler, B. (2018)

Extreme disorder in an ultra-high-affinity protein complex.

Nature, 555, 61-66. [PDF]

See News & Views by Berlow & Wright: "Tight complexes from disordered proteins" Nature 555, 37-38. [PDF]

 

 

 

 

Soranno, A., Holla, A., Dingfelder, F., Nettels, D., Makarov, D.E. & Schuler, B. (2017)

Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations.

Proc. Natl. Acad. Sci. USA 114, E1833-E1839. [PDF]

 

 

 

 

Borgia, A., Zheng W., Buholzer, K., Borgia, M., Schüler A., Hofmann, H., Soranno, A., Nettels, D., Gast, K., Grishaev, A., Best, R.B. & Schuler B. (2016)

Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.

J. Am. Chem. Soc. 138, 11714−11726. [PDF]

See JACS Spotlight "Settling a Folding Debate Once and For All", J. Am. Chem. Soc. 2016, 138, 13083−13084. [PDF]

 

 

 

 

Aznauryan, M., Delgado, L., Soranno, A., Nettels, D., Huang, J., Labhardt, A.M., Grzesiek, S. & Schuler, B. (2016)

Comprehensive, structural and dynamical view of an unfolded protein from the combination of single-molecule FRET,  NMR and SAXS.

Proc. Natl. Acad. Sci. USA 113, E5389–E5398. [PDF]

 

 

 

 

Borgia, A., Kemplen, K.R., Borgia, M.B., Soranno, A., Shammas, S., Wunderlich, B., Nettels, D., Best, R.B., Clarke, J. & Schuler, B. (2015)

Transient misfolding dominates multidomain protein folding.

Nat. Comm. 6, 8861. [PDF]

 

 

 

 

König, I., Zarrine-Afsar, A., Aznauryan, M., Soranno, A., Wunderlich, B., Dingfelder, F., Stüber, J.C., Plückthun, A., Nettels, D. & Schuler, B. (2015)

Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells.

Nat. Methods 12, 773-779. [PDF]

 

 

 

 

Benke, S., Roderer, D., Wunderlich, B., Nettels, D., Glockshuber, R. & Schuler, B. (2015)

The assembly dynamics of the cytolytic pore toxin ClyA.

Nat. Comm. 6, 6198. [PDF]

 

 

 

 

Soranno, A., Koenig, I., Borgia, M.B., Hofmann, H., Zosel, F., Nettels, D. & Schuler, B. (2014)

Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments.

Proc. Natl. Acad. Sci. USA 111, 4874-4879. [PDF]

 

 

 

 

Wunderlich, B., Nettels, D., Benke, S., Clark, J., Weidner, S., Hofmann, H., Pfeil, S.H. & Schuler, B. (2014)

Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes.

Nat. Protocols 8, 1459-1474. [PDF]

 

 

 

 

Soranno, A., Buchli, B., Nettels, D., Cheng, R. R., Müller-Späth, S., Pfeil, S. H., Hoffmann, A., Lipman, E. A., Makarov, D. E. & Schuler, B. (2012)

Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

Proc. Natl. Acad. Sci. USA 109, 17800–17806. [PDF]

 

 

 

 

Hofmann, H., Soranno, A., Borgia, A., Gast, K., Nettels, D. & Schuler, B. (2012)

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single molecule spectroscopy.

Proc. Natl. Acad. Sci. USA 109, 16155–16160. [PDF]

 

 

 

 

Borgia, M., Borgia, A., Best, R. B., Steward, A., Nettels, D., Wunderlich, B., Schuler, B. & Clarke, J. (2011)

Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins.

Nature 474, 662-665. [PDF]

Recent reviews

Plitzko, J.M., Schuler, B. & Selenko, Ph. (2017)

Structural Biology outside the box - inside the cell.

Struct. Biology 46, 110–121. [PDF]

 

 

Schuler, B., Hofmann, H., Nettels, D. & Soranno, A. (2016)

Single-molecule FRET spectroscopy and the polymer physics of unfolded and intrinsically disordered proteins.

Annu. Rev. Biophys. 45, 207-231. [PDF]

 

 

Brucale, M., Schuler, B. & Samori, B. (2014)

Single-Molecule Studies of Intrinsically Disordered Proteins.

Chem. Rev. 114, 3281-3317. [PDF]

 

 

Schuler, B. (2013)

Single-molecule FRET of protein structureand dynamics - a primer.

J. Nanobiotechnol. 11 (S1), S2. [PDF]

 

 

Schuler, B. & Hofmann, H. (2013)

Single-molecule spectroscopy of protein folding dynamics - expanding scope and timescales.

Curr. Opin. Struct. Biol. 23, 36-47. [PDF]

 

 

 

Complete list of publications

2018

 

Borgia, A., Borgia, M., Bugge, K., Kissling, V.M., Heidarsson, P.O., Fernandes, C.B., Sottini, A., Soranno, A., Buholzer, K., Nettels, D., Kragelund, B.B., Best, R.B., & Schuler, B. (2018)

Extreme disorder in an ultra-high-affinity protein complex.

Nature, 555, 61-66. [PDF]

See News & Views by Berlow & Wright: "Tight complexes from disordered proteins" Nature 555, 37-38. [PDF]

 

 

Holmstrom, E., Nettels, D. & Schuler, B. (2018)

Conformational Plasticity of Hepatitis C Virus Core Protein Enables RNA-Induced Formation of Nucleocapsid-like Particles.

J. Mol. Biol., in press. (Special Issue on Intrinsically Disordered Proteins) [PDF]

 

 

Makarov, D. E. & Schuler, B. (2018)

Preface: Special Topic on Single-Molecule Biophysics.

J. Chem. Phys. 148, 123001. [PDF]

See https://aip.scitation.org/toc/jcp/148/12 for the complete Special Topic.

 

 

Zheng, W., Zerze, G.H., Borgia, A., Mittal, J., Schuler, B. & Best, R.B. (2018)

Inferring properties of disordered chains from FRET transfer efficiencies.

J. Chem. Phys. 148, 123329. (Special Issue on Single-Molecule Biophysics) [PDF]

 

 

Reinartz, I., Sinner, C., Nettels, D., Stucki-Buchli, B., Stockmar, F., Panek, P.T., Jacob, C.R., Nienhaus, G.U., Schuler, B. & Schug, A. (2018)

Simulation of FRET Dyes Allows Quantitative Comparison against Experimental Data.

J. Chem. Phys. 148, 123321. (Special Issue on Single-Molecule Biophysics) [PDF]

 

 

Masliah, G., Maris, C., König, S.L.B., Yulikov, M., Aeschimann, F., Mabille, J., Weiler, J., Holla, A., Hunziker, J., Meisner-Kober, N., Schuler, B., Jeschke, G., Allain, F.H.-T. (2018)

Structural basis of siRNA recognition by TRBP double-stranded RNA binding domains.

EMBO J. e97089. [PDF]

 

 

Hansen, S., Ernst, P., König, S.L.B., Reichen, C., Ewald, C., Nettels, D., Mittl, P.R.E., Schuler, B. & Plückthun, A. (2018)

Curvature of designed armadillo repeat proteins allows modular peptide binding.

J. Struct. Biol. 201, 108-117. (Special Issue on Proteins with Tandem Repeats) [PDF]

 

 

Morger, D., Zosel, F., Bühlmann, M., Züger, S., Mittelviefhaus, M., Schuler, B., Luban, J. & Grütter, M.G. (2018)

The three-fold axis of the HIV-1 capsid lattice is the species-specific binding interface for TRIM5α.

J. Virol. 92, e01541-17. [PDF]

 

 

2017

 

Plitzko, J.M., Schuler, B. & Selenko, Ph. (2017)

Structural Biology outside the box — inside the cell.

Curr. Opin. Struct. Biol. 46, 110–121. [PDF]

 

 

Soranno, A., Holla, A., Dingfelder, F., Nettels, D., Makarov, D.E. & Schuler, B. (2017)

Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations.

Proc. Natl. Acad. Sci. USA 114, E1833-E1839. [PDF]

 

 

Zosel, F., Haenni, D., Soranno, A., Nettels, D. & Schuler, B. (2017)

Combining short- and long-range fluorescence reporters with simulations to explore the intramolecular dynamics of an intrinsically disordered protein.

J. Chem. Phys. (Special Topic Issue: Reaction Pathways) 147, 152708-1-13. [PDF]

 

 

Zijlstra, N., Dingfelder, F., Wunderlich, B., Zosel, F., Benke, St., Nettels, D., & Schuler, B. (2017)

Rapid Microfluidic Dilution for Single-Molecule Spectroscopy of Low-Affinity Biomolecular Complexes.

Angew. Chem. Int. Ed. 56, 7126–7129, DOI: 10.1002/anie.201702439. [PDF]

 

 

Dingfelder, F., Wunderlich, B., Benke, St., Zosel, F., Zijlstra, N., Nettels, D. & Schuler, B. (2017)

Rapid Microfluidic Double-Jump Mixing Device for Single-Molecule Spectroscopy.

J. Am. Chem. Soc., DOI: 10.1021. [PDF]

 

 

Benke, St., Nettels, D., Hofmann, H. & Schuler, B. (2017)

Quantifying kinetics from time series of single-molecule Förster resonance energy transfer efficiency histograms.

Nanotechnology (Focus Collection on Protein Folding) 28, 114002. [PDF]

 

 

Ruggeri, F., Zosel, F., Mutter, N., Różycka, M., Wojtas, M., Ożyhar, A., Schuler, B. & Krishnan, M. (2017)

Single-molecule electrometry.

Nat. Nanotechnol., DOI: 10.1038/NNANO.2017.26, 488-495. [PDF]

 

 

2016

 

Borgia, A., Zheng W., Buholzer, K., Borgia, M., Schüler A., Hofmann, H., Soranno, A., Nettels, D., Gast, K., Grishaev, A., Best, R.B. & Schuler, B. (2016)

Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.

J. Am. Chem. Soc. 138, 11714−11726. [PDF]

See JACS Spotlight "Settling a Folding Debate Once and For All", J. Am. Chem. Soc. 2016, 138, 13083−13084. [PDF]

 

 

Zheng, W., Borgia, A., Buholzer, K., Grishaev, A., Schuler, B. & Best., R.B. (2016)

Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.

J. Am. Chem. Soc. 138, 11702−11713. [PDF]

 

 

Aznauryan, M., Delgado, L., Soranno, A., Nettels, D., Huang, J., Labhardt, A.M., Grzesiek, St. & Schuler, B. (2016)

Comprehensive, structural and dynamical view of an unfolded protein from the combination of single-molecule FRET,  NMR and SAXS.

Proc. Natl. Acad. Sci. USA 113, E5389–E5398. [PDF]

 

 

Roderer, D., Benke, St., Schuler, B. & Glockshuber, R. (2016)

Soluble Oligomers of the Pore-forming Toxin Cytolysin A from Escherichia coli Are Off-pathway Products of Pore Assembly.

J. Biol. Chem. 291, 5652–5663. [PDF]

 

 

2015

 

König, I., Zarrine-Afsar, A., Aznauryan, M., Soranno, A., Wunderlich, B., Dingfelder, F., Stüber, J.C., Plückthun, A., Nettels, D. & Schuler, B. (2015)

Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells.

Nat. Methods 12, 773-779. [PDF]

See News & Views by Plochowietz & Kapanidis. [PDF]

 

Borgia, A., Kemplen, K.R., Borgia, M.B., Soranno, A., Shammas, S., Wunderlich, B., Nettels, D., Best, R.B., Clarke, J. & Schuler, B. (2015)

Transient misfolding dominates multidomain protein folding.

Nat. Comm. Doi: 10.1038/ncomms9861. [PDF]

 

 

Nettels, D., Haenni, D., Maillot, S., Gueye, M., Barth, A., Hirschfeld, V., Hübner, C.G., Léonard, J. & Schuler, B. (2015)

Excited-state annihilation reduces power dependence of single-molecule FRET experiments.

Phys. Chem. Chem. Phys. 17, 32304-32315. [PDF]

 

 

Schuler, B. & Smith, J.L. (2015)

Editorial overview: Biophysical and molecular biological methods: Structure, dynamics, and single molecules.

Curr. Opin. Struct. Biol. 34, iv-vi. [PDF]

 

 

Zheng, W., Borgia, A., Borgia, M., Schuler, B. & Best, R.B. (2015)

Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations.

J. Chem. Theory Comput. 11, 5543-5553. [PDF]

 

 

Benke, S., Roderer, D., Wunderlich, B., Nettels, D., Glockshuber, R. & Schuler, B. (2015)

The assembly dynamics of the cytolytic pore toxin ClyA.

Nat. Comm. 6, 6198. [PDF]

 

 

Best, R.B., Hofmann, H., Nettels, D. & Schuler, B. (2015)

Quantitative Interpretation of FRET Experiments via Molecular Simulation: Force Field and Validation.

Biophys. J. 108, 2721-2731. [PDF]

 

 

Yuan, H., Gaiduk, A., Siekierzycka, J.R., Fujiyoshi, S., Matsushita, M., Nettels, D., Schuler, B., Seidel, C.A. & Orrit, M. (2015)

Temperature-cycle microscopy reveals single-molecule conformational heterogeneity.

Phys. Chem. Chem. Phys. 17, 6532-6544. [PDF]

 

 

Czar, M.F., Zosel, F., König, I., Nettels, D., Wunderlich, B., Schuler, B., Zarrine-Afsar, A. & Jockusch, RA. (2015)

Gas-Phase FRET Efficiency Measurements To Probe the Conformation of Mass-Selected Proteins.

Anal. Chem. 87, 7559-7565. [PDF]

 

 

2014

 

Soranno, A., Koenig, I., Borgia, M.B., Hofmann, H., Zosel, F., Nettels, D. & Schuler, B. (2014)

Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments.

Proc. Natl. Acad. Sci. USA 111, 4874-4879. [PDF]

 

 

Wunderlich, B., Nettels, D. & Schuler, B. (2014)

Taylor dispersion and the position-to-time conversion in microfluidic mixing devices.

Lab Chip 14, 219-228. [PDF]

 

 

Kellner, R., Hofmann, H., Barducci, A., Wunderlich, B., Nettels, D. & Schuler, B. (2014)

Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein.

Proc. Natl. Acad. Sci. USA 111, 13355-13360. [PDF]

 

 

Wuttke, R., Hofmann, H., Nettels, D., Borgia, M.B., Mittal, J., Best, R.B. & Schuler, B. (2014)

Temperature-dependent solvation modulates the dimensions of disordered proteins.

Proc. Natl. Acad. Sci. USA 111, 5213–5218. [PDF]

 

 

Hofmann, H., Hillger, F., Delley, C., Hoffmann, A., Pfeil, SH., Nettels, D., Lipman, EA. & Schuler, B. (2014)

Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy.

Biophys. J. 107, 2891-2902. [PDF]

 

 

Brucale, M., Schuler, B. & Samori, B. (2014)

Single-Molecule Studies of Intrinsically Disordered Proteins.

Chem. Rev. 114, 3281-3317. [PDF]

 

 

Weisenburger, S., Jing, B., Hänni, D., Reymond, L., Schuler, B., Renn, A. & Sandoghdar, V. (2014)

Cryogenic Colocalization Microscopy for Nanometer-Distance Measurements.

ChemPhysChem 15, 763-770. [PDF]

 

 

Pochorovski, I., Knehans, T., Nettels, D., Müller, A.M., Schweizer, W.B., Caflisch, A., Schuler, B. & Diederich, F. (2014)

Experimental and Computational Study of BODIPY Dye-Labeled Cavitand Dynamics.

J. Am. Chem. Soc. 136, 2441-2449. [PDF]

 

 

Roderer, D., Benke, S., Müller, M., Fäh-Rechsteiner, H., Ban, N., Schuler, B. & Glockshuber, R (2014)

Characterization of Variants of the Pore-Forming Toxin ClyA from Escherichia coli Controlled by a Redox Switch.

Biochemistry  53, 6357-6369. [PDF]

 

 

2013

 

Wunderlich, B., Nettels, D., Benke, S., Clark, J., Weidner, S., Hofmann, H., Pfeil, S.H. & Schuler, B. (2013)

Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes.

Nat. Protocols 8, 1459-1474. [PDF]

 

 

Schuler, B. (2013)

Single-molecule FRET of protein structure and dynamics - a primer.

J. Nanobiotechnol. 11 (S1), S2. [PDF]

 

 

Aznauryan, M., Nettels, D., Holla, A., Hofmann, H. & Schuler, B. (2013)

Single-molecule spectroscopy of cold denaturation and the temperature-induced collapse of unfolded proteins.

J. Am. Chem. Soc. 135, 14040-14043. [PDF]

 

 

Hofmann, H., Nettels, D. & Schuler, B. (2013)

Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH.

J. Chem. Phys. (Special Issue: Chemical Physics of Biological Systems) 139, 121930. [PDF]

 

 

Schuler, B. & Clarke, J. (2013)

Rough passage across a barrier.

Nature 502, 632-633. [PDF]

 

 

Haenni, D., Zosel, F., Reymond, L., Nettels, D. & Schuler, B. (2013)

Intramolecular distances and dynamics from the combined photon statistics of single-molecule FRET and photoinduced electron transfer.

J. Phys. Chem. B (Festschrift on the occasion of the 60th birthday of Peter W. Wolynes) 42, 13015-28. [PDF]

 

 

Schuler, B. & Hofmann, H. (2013)

Single-molecule spectroscopy of protein folding dynamics-expanding scope and timescales.

Curr. Opin. Struct. Biol. 23, 36-47. [PDF]

 

 

2012

 

Borgia, A., Wensley, B.G., Soranno, A., Nettels, D., Borgia, M.B., Hoffmann, A., Pfeil, S.H., Lipman, E.A., Clarke, J. & Schuler, B. (2012)

Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy.

Nat. Comm. 3, 1195. [PDF]

 

 

Hofmann, H., Soranno, A., Borgia, A., Gast, K., Nettels, D. & Schuler, B. (2012)

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single molecule spectroscopy.

Proc. Natl. Acad. Sci. USA 109, 16155–16160. [PDF]

 

 

Soranno, A., Buchli, B., Nettels, D., Cheng, R. R., Müller-Späth, S., Pfeil, S. H., Hoffmann, A., Lipman, E. A., Makarov, D. E. & Schuler, B. (2012)

Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

Proc. Natl. Acad. Sci. USA 109, 17800–17806. [PDF]

 

 

2011

 

Borgia, M., Borgia, A., Best, R. B., Steward, A., Nettels, D., Wunderlich, B., Schuler, B. & Clarke, J. (2011)

Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins.

Nature 474, 662-665. [PDF]

 

 

Hoffmann, A., Nettels, D., Clark, J., Borgia, A., Radford, S.E., Clarke, J. & Schuler, B. (2011)

Quantifying heterogeneity and conformational dynamics from single molecule FRET of diffusing molecules: Recurrence analysis of single particles (RASP).

PhysChemChemPhys (Special issue on Single-Molecule Optical Studies of Soft and Complex Matter) 13, 1857-1871. [PDF]

 

 

Hoefling, M., Lima, N., Haenni, D., Seidel, CA., Schuler, B. & Grubmüller, H. (2011)

Structural heterogeneity and quantitative FRET efficiency distributions of polyprolines through a hybrid atomistic simulation and Monte Carlo approach.

PLOS ONE 6(5):e 19791. [PDF]

 

 

Yuan, H., Xia, T., Schuler, B. & Orrit, M. (2011)

Temperature-cycle single-molecule FRET microscopy on polyprolines.

PhysChemChemPhys (Special issue on Single-Molecule Optical Studies of Soft and Complex Matter) 13, 1762-1769. [PDF]

 

 

2010

 

Müller-Späth, S., Soranno, A., Hirschfeld, V., Hofmann, H., Rüegger, S., Reymond, L., Nettels, D. & Schuler, B. (2010)

Charge interactions can dominate the dimensions of intrinsically disordered proteins.

Proc. Natl. Acad. Sci. USA 107, 14609-14614. [PDF]

See Commentary by England & Haran. [PDF]

 

 

Hofmann, H., Hillger, F., Pfeil, S. H., Hoffmann, A., Streich, D., Haenni, D., Nettels, D., Lipman, E. A. & Schuler, B. (2010)

Single-molecule spectroscopy of protein folding in a chaperonin cage.

Proc. Natl. Acad. Sci. USA 107, 11793-11798. [PDF]

 

 

Schuetz, P., Wuttke, R., Schuler, B. & Caflisch, A. (2010)

Free Energy Surfaces from Single-Distance Information.

J. Phys. Chem. B 114, 15227–15235. [PDF]

 

 

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, R.B. & Schuler, B. (2009)

Single molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

Proc. Natl. Acad. Sci. USA 106, 20740-20745. [PDF]

 

 

Gopich, I.V., Nettels, D., Schuler, B. & Szabo, A. (2009)

Protein dynamics from single-molecule intensity correlation functions.

J. Chem. Phys. 131, 095102. [PDF]

 

 

2008

 

Hillger, F., Hänni, D., Nettels, D., Geister, S., Grandin, M., Textor, M. & Schuler, B. (2008)

Probing protein-chaperone interactions with single molecule fluorescence spectroscopy.

Angew. Chem. Int. Ed. 47, 6184-6188 (Angew. Chem. 120, 6183-6194). [PDF]

 

 

Wahl, M, Rahn, H.-J., Röhlicke, T., Kell, G., Nettels, D., Hillger, F., Schuler, B. & Erdmann, R. (2008)

Scalable time-correlated photon counting system with multiple independent input channels.

Rev. Sci. Instrum. 79, 123113. [PDF]

 

 

Nettels, D., Hoffmann, A. & Schuler, B. (2008)

Unfolded protein and peptide dynamics investigated with single molecule FRET and correlation spectroscopy from picoseconds to seconds.

J. Phys. Chem. B (Festschrift on the occasion of the 60th birthday of Attila Szabo) B 112, 6137-6146. [PDF]

 

 

Schuler, B. & Eaton, W. A. (2008)

Protein folding studied by single molecule FRET.

Curr. Opin. Struct. Biol. 18, 16-26. [PDF]

 

 

Kane, A. S., Hoffmann, A., Baumgärtel, P., Seckler, R., Reichardt, G., Horsley, D. A., Schuler, B. & Bakajin, O. (2008)

Microfluidic Mixers for the Investigation of Rapid Protein Folding Kinetics Using Synchrotron Radiation Circular Dichroism Spectroscopy.

Anal. Chem. 80, 9534-9541. [PDF]

 

 

 

2007

 

Nettels, D., Gopich, V.I., Hoffmann, A. & Schuler, B. (2007)

Ultrarapid dynamics of protein collapse from single molecule photon statistics.

Proc. Natl. Acad. Sci. USA 104, 2655-2660. [PDF]

See Highlight in Science 315, 1194, “Editors’ choice”. [PDF]

 

 

Hoffmann, A., Kane, A., Nettels, D., Hertzog, D., Baumgärtel, P., Lengefeld, J., Reichardt, G., Horsley, D.A., Seckler, R., Bakajin, O. & Schuler, B. (2007)

Mapping protein collapse with single molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy.

Proc. Natl. Acad. Sci. USA 104, 105-110. [PDF]

 

 

Nettels, D. & Schuler, B. (2007)

Subpopulation-resolved photon statistics of single-molecule energy transfer dynamics.

IEEE J. Sel. Top. Quant. 313, 990-995. [PDF]

 

 

Hillger, F., Nettels, D., Dorsch, S. & Schuler, B. (2007)

Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy.

J. Fluoresc. (Special Issue: Single Molecule Spectroscopy) 17, 759-765. [PDF]

 

 

Schuler, B. (2007)

Application of Single Molecule Förster Resonance Energy Transfer to Protein Folding.

Protein Folding Protocols (Humana Press; Bai, Nussinov, Eds.), 115–138. [PDF]

 

 

Best, R.B., Merchant, K.A., Gopich, I.V., Schuler, B., Bax, A. & Eaton, W.A. (2007)

Effect of flexibility and cis residues in single-molecule FRET studies of polyproline.

Proc. Natl. Acad. Sci. USA 104, 18964–18969. [PDF]

 

 

2006

 

Camenisch, U., Dip, R., Briand Schumacher, S., Schuler, B. & Naegeli, H. (2006)

Recognition of helical kinks by xeroderma pigmentosum group A protein triggers DNA excision repair.

Nature Struct. Mol. Biol. 13, 278–284. [PDF]

 

 

2005

 

Schuler, B., Lipman, E. A., Steinbach, P. J., Kumke, M. & Eaton, W. A. (2005)

Polyproline and the “spectroscopic ruler” revisited with single molecule fluorescence.

Proc. Natl. Acad. Sci. USA 102, 2754-2759. [PDF]

See Highlight in Science 307, 1016, “Editors’ choice”. [PDF]

 

 

Schuler, B. (2005)

Single molecule spectroscopy of protein folding.

ChemPhysChem 6, 1206-1220. [PDF]

 

 

2004

 

Rhoades, E., Cohen, M., Schuler, B. & Haran, G. (2004)

Two-state folding observed in individual protein molecules.

J. Am. Chem. Soc. 126, 14686-14687. [PDF]

 

 

2003 and earlier

 

Lipman, E. A.*, Schuler, B.*, Bakajin, O. & Eaton, W. A. (2003)

Single molecule measurement of protein folding kinetics.

Science 301, 1233-1235. [PDF] [supplement]

 

 

Buscaglia, M., Schuler, B., Lapidus, L. J., Eaton, W. A. & Hofrichter, J. (2003)

Kinetics of Intramolecular Contact Formation in a Denatured Protein.

J. Mol. Biol. 332, 9-12. [PDF]

 

 

Schuler, B.*, Lipman, E. A.* & Eaton, W. A. (2002)

Probing the free energy surface for protein folding with single molecule fluorescence spectroscopy.

Nature 419, 743-747. [PDF] [supplement]

 

 

Schuler, B., Kremer, W., Kalbitzer, H. R. & Jaenicke, R. (2002)

Role of entropy in protein thermostability: Folding kinetics of a hyperthermophilic cold shock protein at high temperature using 19F-NMR.

Biochemistry 41, 11670-11680. [PDF]

 

 

Schuler, B. & Pannell, L. K. (2002)

Specific labeling of polypeptides at amino-terminal cysteine residues using Cy5-benzyl thioester.

Bioconjugate Chem. 13, 1039-1043. [PDF]

 

 

Kremer, W., Schuler, B., Harrieder, S., Geyer, M., Gronwald, W., Welker, C., Jaenicke, R. & Kalbitzer, H. R. (2001)

Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima.

Eur. J. Biochem. 268, 2527-2539. [PDF]

 

 

Schuler, B., Fürst, F., Osterroth, F., Steinbacher, S., Huber, R. & Seckler, R. (2000)

Plasticity and steric strain in a parallel ß-helix: Directed mutagenesis of the P22 tailspike protein.

Proteins 39, 89-101. [PDF]

 

 

Schuler, B. & Seckler, R. (1999)

The isolated P22 tailspike ß-helix domain: Formation of fibrous aggregates from a nonnative intermediate.

J. Biol. Chem. 274, 18589-18596. [PDF]

 

 

Schuler, B. & Seckler, R. (1998)

P22 tailspike folding mutants revisited: Effects on the thermodynamic stability of the isolated ß-helix domain.

J. Mol. Biol. 281, 227-234. [PDF]

 

 

Miller, S.*, Schuler, B.* & Seckler, R. (1998)

A reversibly unfolding fragment of P22 tailspike protein with native structure: The isolated ß-helix domain.

Biochemistry 37, 9160-9168. [PDF]

 

 

Miller, S., Schuler, B. & Seckler, R. (1998)

Phage P22 tailspike protein: Removal of head-binding domain unmasks effects of folding mutations on native-state thermal stability.

Protein Sci. 7, 2223-2232. [PDF]

 

 

 

 

 

 

 

 

University of Zurich