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selected recent publications
Schuler, B. & Hofmann, H. (2013)
Single-molecule spectroscopy of protein folding dynamics - expanding scope and timescales.
Curr. Opin. Struct. Biol. in press
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]
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]
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]
complete list of publications
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 early edition [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]
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
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