Laser spectroscopy of single molecules
Microfluidics for single-molecule dynamics
Kinetics of protein conformational changes
Single-molecule spectroscopy in live cells
Rapid microfluidic mixing
Spectrum of disorder in protein complexes
Laser spectroscopy of single molecules
Structure of the pore-forming toxin Cytolysin A
Microfluidics for single-molecule dynamics
Kinetics of protein conformational changes
Single-molecule spectroscopy in live cells
Rapid microfluidic mixing
Spectrum of disorder in protein complexes
previous arrow
next arrow
 

Selected publications

Heidarsson, P.O., Mercadante, D., Sottini, A., Nettels, D., Borgia, M.B., Borgia, A., Kilic, S., Fierz, B, Best, R.B. & Schuler, B. (2022)
Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein.
Nat. Chem. 14, 224-231. [PDF]

Nüesch, M.F., Ivanovic, M.T., Claude, J.-B., Nettels, D., Best, R.B., Wenger, J. & Schuler, B. (2022)
Single-molecule detection of ultrafast biomolecular dynamics with nanophotonics.
J. Am. Chem. Soc. 144, 52–56. [PDF] ACS Editors’ Choice
See JACS Spotlights “Now You See Me─Refining Detection Methods For Ultra-Fast Proteins” J. Am. Chem. Soc. 144, 1067–1068. [PDF]

Sottini, A., Borgia, A., Borgia, M.B., Bugge, K., Nettels, D., Chowdhury, A., Heidarsson, P.O., Zosel, F., Best, R.B., Kragelund, B.B., & Schuler, B. (2020)
Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes.
Nat. Commun. 11, 5736. [PDF]

Zosel, F., Soranno, A., Buholzer, K.J., Nettels & Schuler, B. (2020)
Depletion interactions modulate the binding between disordered proteins in crowded environments.
Proc. Natl. Acad. Sci. USA 117, 13480–13489. [PDF]

Holmstrom, E.D., Liu, Z., Nettels, D., Best, R.B. & Schuler, B. (2019)
Disordered RNA chaperones can enhance nucleic acid folding via local charge screening.
Nat. Commun. 10, 2453. [PDF]

Sturzenegger, F., Zosel, F., Holmstrom, E.D., Buholzer, K.J, Makarov, D.E., Nettels, D. & Schuler, B. (2018)
Transition path times of coupled folding and binding reveal the formation of an encounter complex.
Nat. Commun. 9, 4708. [PDF]

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 ultrahigh-affinity protein complex.
Nature 555, 61-66. [PDF]
See News & Views by Berlow & Wright (2018): “Tight complexes from disordered proteins” Nature 555, 37-38. [PDF]

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

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 (2015): “Single in the (Cell) City: a proteinfolding story” Nat. Methods 12, 715-716. [PDF]

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

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 (2010): “To fold or expand—a charged question” Proc. Natl. Acad. Sci. USA 107, 14519-14520. [PDF]

Recent reviews

Schuler, B., Borgia, A., Borgia, M.B., Heidarsson, P.O., Holmstrom, E.D., Nettels, D. & Sottini, A. (2020)
Binding without folding – the biomolecular function of disordered polyelectrolyte complexes.
Curr. Opin. Struct. Biol. 60, 66-76. [PDF]

Holmstrom, E.D., Holla, A., Wenwei, Z., Nettels, D., Best, R.B. & Schuler, B. (2018)
Accurate Transfer Efficiencies, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRET.
Methods Enzymol. 611, 287-325. [PDF]

Schuler, B. (2018)
Perspective: Chain dynamics of unfolded and intrinsically disordered proteins from nanosecond fluorescence correlation spectroscopy combined with single-molecule FRET.
J. Chem. Phys. 149, 010901. [PDF]

Plitzko, J.M., Schuler, B. & Selenko, P. (2017)
Structural Biology outside the box – inside the cell.
Curr. Opin. Struct. Biol. 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 structure and 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

2022

Heidarsson, P.O., Mercadante, D., Sottini, A., Nettels, D., Borgia, M.B., Borgia, A., Kilic, S., Fierz, B., Best, R.B. & Schuler, B. (2022)
Release of linker histone from the nucleosome driven by polyelectrolyte competition with a disordered protein.
Nat. Chem. 14, 224-231. [PDF]

Nüesch, M.F., Ivanovic, M.T., Claude, J.-B., Nettels, D., Best, R.B., Wenger, J. & Schuler, B. (2022)
Single-molecule detection of ultrafast biomolecular dynamics with nanophotonics.
J. Am. Chem. Soc. 144, 52–56. [PDF] ACS Editors’ Choice
See JACS Spotlights “Now You See Me─Refining Detection Methods For Ultra-Fast Proteins” J. Am. Chem. Soc. 144, 1067–1068. [PDF]

Zosel, F., Holla, A. & Schuler, B. (2022)
Labeling of Proteins for Single-Molecule Fluorescence Spectroscopy.
Protein Folding: Methods and Protocols, Methods Mol. Biol. 2376, 207-233. [PDF]

Stelzl, L.S, Pietrek, L.M., Holla, A., Oroz, J., Sikora, M., Köfinger, J., Schuler, B., Zweckstetter, M., Hummer, G. (2022)
Global Structure of the Intrinsically Disordered Protein Tau Emerges from Its Local Structure.
JACS Au online [PDF]

Martinsen, J.H., Saar, D., Fernandes, C.B., Schuler, B., Bugge, K., Kragelund, B.B. (2022)
Structure, dynamics, and stability of the globular domain of human linker histone H1.0 and the role of positive charges.
Protein Sci. 31, 918-932 [PDF]

2021

König, I., Soranno, A., Nettels, D. & Schuler, B. (2021)
Impact of in-cell and in-vitro crowding on the conformations and dynamics of an intrinsically disordered protein.
Angew. Chem. Int. Ed. 60, 10724-10729. [PDF]

Benke, S., Holla, A., Wunderlich, B., Soranno, A., Nettels, D. & Schuler, B. (2021)
Combining Rapid Microfluidic Mixing and Three-Color Single-Molecule FRET for Probing the Kinetics of Protein Conformational Changes.
J. Phys. Chem. B, 125, 6617-6628. [PDF]

Dingfelder, F., Macocco, I., Benke, Nettels, D., Faccioli, P. & Schuler, B. (2021)
Slow Escape from a Helical Misfolded State of the Pore-Forming Toxin Cytolysin A.
JACS Au 1, 1217–1230. [PDF]

Klose, D,, Holla, A., Gmeiner, C., Nettels, D., Ritsch, I., Bross, N., Yulikov, M., Allain, F.H.-T., Schuler, B., Jeschke, G. (2021)
Resolving distance variations by single-molecule FRET and EPR spectroscopy using rotamer libraries.
Biophys. J, 120, 4842–4858. [PDF]
See New and Notable by Mingu & Lemke (2021): “When two become one: Integrating FRET and EPR
into one structural model” Biophys. J. 120, 4637–4638. [PDF]

Lerner, E. et al. (2021)
FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices.
eLife 10, e60416. [PDF]

Stüber, C., Richter, C.P., Bellón, J.S., Schwill, M., König, I., Schuler, B., Piehler, J. & Plückthun, A. (2021)
Apoptosis-inducing anti-HER2 agents operate through oligomerization-induced receptor immobilization.
Commun. Biol. 4, 762. [PDF]

2020

Sottini, A., Borgia, A., Borgia, M.B., Bugge, K., Nettels, D., Chowdhury, A., Heidarsson, P.O., Zosel, F., Best, R.B., Kragelund, B.B. & Schuler, B. (2020)
Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes.
Nat. Commun. 11, 5736. [PDF]

Zijlstra, N., Nettels, D., Satija, R., Makarov, D.E. & Schuler, B. (2020)
Transition path dynamics of a dielectric particle in a bistable optical trap.
Phys. Rev. Lett. 125, 146001. [PDF]

Zosel, F., Soranno, A., Buholzer, K.J., Nettels, D. & Schuler, B. (2020)
Depletion interactions modulate the binding between disordered proteins in crowded environments.
Proc. Natl. Acad. Sci. USA 117, 13480–13489. [PDF]

Schuler, B., Borgia, A., Borgia, M.B., Heidarsson, P.O., Holmstrom, E.D., Nettels, D. & Sottini, A. (2020)
Binding without folding – the biomolecular function of disordered polyelectrolyte complexes.
Curr. Opin. Struct. Biol. 60, 66-76. [PDF]

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

Ernst, P., Zosel, F., Reichen, C., Nettels, D., Schuler, B. & Plückthun, A. (2020)
Structure-guided design of a peptide lock for modular peptide binders.
ACS Chem. Biol. 2020, 15, 457-468. [PDF]

2019

Holmstrom, E.D., Liu, Z., Nettels, D., Best, R.B. & Schuler, B. (2019)
Disordered RNA chaperones can enhance nucleic acid folding via local charge screening.
Nat. Commun. 10, 2453. [PDF]

Assenza, S., Sassi, A.S., Kellner, R., Schuler, B., De Los Rios, P. & Barducci, A. (2019)
Efficient conversion of chemical energy into mechanical work by Hsp70 chaperones.
eLife 8:e48491. [PDF]

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 ultrahigh-affinity protein complex.
Nature 555, 61-66. [PDF]
See News & Views by Berlow & Wright (2018): “Tight complexes from disordered proteins” Nature 555, 37-38. [PDF]

Sturzenegger, F., Zosel, F., Holmstrom, E.D., Buholzer, K.J, Makarov, D.E., Nettels, D. & Schuler, B. (2018)
Transition path times of coupled folding and binding reveal the formation of an encounter complex.
Nat. Commun. 9, 4708. [PDF]

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

Dingfelder, F., Benke, S., Nettels, D. & Schuler B. (2018)
Mapping an Equilibrium Folding Intermediate of the Cytolytic Pore Toxin ClyA with Single-Molecule FRET.
J. Phys. Chem. B 122, 11251-11261. (Festschrift on the occasion of the 80th birthday of William A. Eaton) [PDF]

Zheng, W., Hofmann, H., Schuler, B. & Best, R.B. (2018)
Origin of Internal Friction in Disordered Proteins Depends on Solvent Quality.
J. Phys. Chem. B 122, 11478-11487. [PDF]

Grotz, K.K., Nueesch, M.F., Holmstrom, E.D., Heinz, M., Stelzl, L.S., Schuler, B. & Hummer, G. (2018)
Dispersion Correction Alleviates Dye Stacking of Single-Stranded DNA and RNA in Simulations of Single-Molecule Fluorescence Experiments.
J. Phys. Chem. B 122, 11626-11639. [PDF]

Marino, J., Buholzer, K.J., Zosel, F., Nettels, D. & Schuler, B. (2018)
Charge Interactions Can Dominate Coupled Folding and Binding on the Ribosome.
Biophys J. 115, 996-1006. [PDF]

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]

Holmstrom, E.D., Holla, A., Wenwei, Z., Nettels, D., Best, R.B. & Schuler, B. (2018)
Accurate Transfer Efficiencies, Distance Distributions, and Ensembles of Unfolded and Intrinsically Disordered Proteins From Single-Molecule FRET.
Methods Enzymol. 611, 287-325. [PDF]

Best, R.B., Zheng, W., Borgia, A., Buholzer, K., Borgia, M.B., Hofmann, H., Soranno, A., Nettels. D., Gast, K., Grishaev, A. & Schuler, B. (2018)
Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”.
Science 361, eaar7101. [PDF]

Hellenkamp, B., Schmid, S., Doroshenko, O., Opanasyuk, O., Kühnemuth, R., Adariani, S.R., Ambrose, B., Aznauryan, M., Barth, A., Birkedal, V., Bowen, M.E., Chen, H., Cordes, T., Eilert, T., Fijen, C., Gebhardt, Ch., Götz, M., Gouridis, G., Gratton, E., Ha, T., Hao, P., Hanke, Ch.A., Hartmann, A., Hendrix, J., Hildebrandt, L.L., Hirschfeld, V., Hohlbein, J., Hua, B., Hübner, Ch.G, Kallis, E., Kapanidis, A.N., Kim, J.Y., Krainer, G., Lamb, D.C., Lee, N.K., Lemke, E.A., Levesque, B., Levitus, M., McCann, J.J, Naredi-Rainer, N., Nettels, D., Ngo, T., Qiu, R., Robb, N.C., Röcker, C., Sanabria, H., Schlierf, M., Schröder, T., Schuler, B., Seidel, H., Streit, L., Thurn, J., Tinnefeld, Ph., Tyagi, S., Vandenberk, N., Vera, A.M., Weninger, K.R., Wünsch, B., Yanez-Orozco, I.S., Michaelis, J., Seidel, C.A.M., Craggs, T.D., & Hugel, T. (2018)
Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study.
Nat. Methods 15, 669-676. [PDF]

Schuler, B. (2018)
Perspective: Chain dynamics of unfolded and intrinsically disordered proteins from nanosecond fluorescence correlation spectroscopy combined with single-molecule FRET.
J. Chem. Phys. 149, 010901. [PDF]

Nasrollah, R.-G., Parigi, G., Soranno, A., Holla, A., Becker, S., Schuler, B., Luchinat, C. & Zweckstetter, M. (2018)
Local and Global Dynamics in Intrinsically Disordered Synuclein.
Angew. Chem. Int. Ed. 57, 15262 –15266 [PDF]
Angew. Chem. 130, 15482-15486 [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. 430, 2453-2467 (Special Issue on Intrinsically Disordered Proteins) [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]

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.

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. 37, 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

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]

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

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

Plitzko, J.M., Schuler, B. & Selenko, P. (2017)
Structural Biology outside the box — inside the cell.
Curr. Opin. Struct. Biol. 46, 110–121. [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. 147, 152708. (Special Topic Issue: Reaction Pathways) [PDF]

Benke, S., Nettels, D., Hofmann, H. & Schuler, B. (2017)
Quantifying kinetics from time series of single-molecule Förster resonance energy transfer efficiency histograms.
Nanotechnology 28, 114002. (Focus Collection on Protein Folding) [PDF]

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

2016

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., 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]

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]

Roderer, D., Benke, S., 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 (2015): “Single in the (Cell) City: a protein-folding story” Nat. Methods 12, 715-716. [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. Commun. 6, 8861. [PDF]

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

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]

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]

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]

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]

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]

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]

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]

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]

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]

Hofmann, H., Hillger, F., Delley, C., Hoffmann, A., Pfeil, S.H., Nettels, D., Lipman, E.A. & Schuler, B. (2014)
Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy.
Biophys. J. 107, 2891-2902. [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]

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]

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]

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]

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 42, 13015-28. (Festschrift on the occasion of the 60th birthday of Peter W. Wolynes) [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. 139, 121930. (Special Issue: Chemical Physics of Biological Systems) [PDF]

Schuler, B. & Clarke, J. (2013)
Rough passage across a barrier.
Nature 502, 632-633. [PDF]

Schuler, B. (2013)
Single-molecule FRET of protein structure and 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]

2012

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]

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. Commun. 3, 1195. [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 13, 1857-1871. (Special issue on Single-Molecule Optical Studies of Soft and Complex Matter) [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, e19791. [PDF]

Yuan, H., Xia, T., Schuler, B. & Orrit, M. (2011)
Temperature-cycle single-molecule FRET microscopy on polyprolines.
PhysChemChemPhys 13, 1762-1769. (Special issue on Single-Molecule Optical Studies of Soft and Complex Matter) [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 (2010): “To fold or expand—a charged question” Proc. Natl. Acad. Sci. USA 107, 14519-14520. [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[PDF]
Angew. Chem. 120, 6183-6194. [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 112, 6137-6146. (Festschrift on the occasion of the 60th birthday of Attila Szabo) [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]

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)
Ultrafast 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”.

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”.

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]