projects papers
ben schuler
 
     
 

 

selected recent publications
Wunderlich, B., Nettels, D., Benke, S., Clark, J., Weidner, S., Hofmann, H., Pfeil, SH. & 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]

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]


recent reviews
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
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 [Epub ahead of print] [PDF]

Wunderlich, B., Nettels, D. & Schuler, B. (2013)
Taylor dispersion and the position-to-time conversion in microfluidic mixing devices.
Lab on a Chip [Epub ahead of print] [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 [Epub ahead of print] [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, SH. & 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]

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, 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]

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]

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]

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., and 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]

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]

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]

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]

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]

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]

 

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Single Molecule Biophysics
Department of Biochemistry

 

 

 

 

 

 


 

 

last modified 28 Oct 2013, mm