Ben Schuler Research Group

University of Zurich

PEOPLE

PROJECTS

PAPERS

 

Selected recent publications

 

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.

PNAS, 114 no. 10 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]

 

 

 

 

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]

 

 

 

 

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]

 

 

 

 

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., 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]

 

 

 

 

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]

 

 

 

 

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]

 

 

 

 

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]

 

 

 

Recent reviews

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 Nanobiotechnology 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

2017

 

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

Single-molecule electrometry.

Nature Nanotechn., DOI: 10.1038/NNANO.2017.26  [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 28, Number 11, (14pp). [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.

PNAS, 114 no. 10 E1833-E1839. [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]

 

 

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]

 

 

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.

THE JOURNAL OF BIOLOGICAL CHEMISTRY, VOL. 291, NO. 11, 5652–5663. [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.

PNAS, 1607193313, E5389–E5398. [PDF]

 

 

2015

 

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.

ScienceDirect 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.

JCTC 11, 5543-5553. [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]

 

 

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.

Nature 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]

 

 

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]

 

 

2014

 

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]

 

 

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]

 

 

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]

 

 

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]

 

 

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]

 

 

2013

 

Schuler, B. (2013)

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

J. Nanobiotechnology 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. 139, 121930. [PDF]

 

 

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

Rough passage across a barrier.

Nature 502, 632-633. [PDF]

 

 

Wunderlich, B., Nettels, D. & Schuler, B. (2013)

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

Lab on a Chip 14, 219-228. [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. [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]

 

 

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]

 

 

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]

 

 

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]

 

 

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]

 

 

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

 

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

Free Energy Surfaces from Single-Distance Information.

J. Phys. Chem. B 114, 15227–15235. [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]

 

 

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]

 

 

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

 

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]

 

 

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 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]

 

 

2007

 

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]

 

 

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]

 

 

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]

 

 

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. (2005)

Single molecule spectroscopy of protein folding.

ChemPhysChem 6, 1206-1220. [PDF]

 

 

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]

 

 

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]

 

 

 

 

 

 

 

 

last modified March 24, 2017 / sb

University of Zurich