A proline switch explains kinetic heterogeneity in a coupled folding and binding reaction

по Zosel, Franziska, Mercadante, Davide, Nettels, Daniel, Schuler, Benjamin
Опубликовано в: Nat Commun (2018)

Ultrafast dynamics of protein collapse from single-molecule photon statistics

по Nettels, Daniel, Gopich, Irina V., Hoffmann, Armin, Schuler, Benjamin
Опубликовано 2007

Protein dynamics from single-molecule fluorescence intensity correlation functions

по Gopich, Irina V., Nettels, Daniel, Schuler, Benjamin, Szabo, Attila
Опубликовано 2009

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

по Best, Robert B., Hofmann, Hagen, Nettels, Daniel, Schuler, Benjamin
Опубликовано в: Biophys J (2015)

Charge Interactions Can Dominate Coupled Folding and Binding on the Ribosome

по Marino, Jacopo, Buholzer, Karin J., Zosel, Franziska, Nettels, Daniel, Schuler, Benjamin
Опубликовано в: Biophys J (2018)

Depletion interactions modulate the binding between disordered proteins in crowded environments

по Zosel, Franziska, Soranno, Andrea, Buholzer, Karin J., Nettels, Daniel, Schuler, Benjamin
Опубликовано в: Proc Natl Acad Sci U S A (2020)

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

по Hofmann, Hagen, Soranno, Andrea, Borgia, Alessandro, Gast, Klaus, Nettels, Daniel, Schuler, Benjamin
Опубликовано 2012

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

по Kellner, Ruth, Hofmann, Hagen, Barducci, Alessandro, Wunderlich, Bengt, Nettels, Daniel, Schuler, Benjamin
Опубликовано 2014

The assembly dynamics of the cytolytic pore toxin ClyA

по Benke, Stephan, Roderer, Daniel, Wunderlich, Bengt, Nettels, Daniel, Glockshuber, Rudi, Schuler, Benjamin
Опубликовано в: Nat Commun (2015)

Erratum: The assembly dynamics of the cytolytic pore toxin ClyA

по Benke, Stephan, Roderer, Daniel, Wunderlich, Bengt, Nettels, Daniel, Glockshuber, Rudi, Schuler, Benjamin
Опубликовано в: Nat Commun (2016)

Disordered RNA chaperones can enhance nucleic acid folding via local charge screening

по Holmstrom, Erik D., Liu, Zhaowei, Nettels, Daniel, Best, Robert B., Schuler, Benjamin
Опубликовано в: Nat Commun (2019)

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

по Soranno, Andrea, Holla, Andrea, Dingfelder, Fabian, Nettels, Daniel, Makarov, Dmitrii E., Schuler, Benjamin
Опубликовано в: Proc Natl Acad Sci U S A (2017)

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

по Hoffmann, Armin, Nettels, Daniel, Clark, Jennifer, Borgia, Alessandro, Radford, Sheena E., Clarke, Jane, Schuler, Benjamin
Опубликовано 2011

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

по Soranno, Andrea, Koenig, Iwo, Borgia, Madeleine B., Hofmann, Hagen, Zosel, Franziska, Nettels, Daniel, Schuler, Benjamin
Опубликовано 2014

Temperature-dependent solvation modulates the dimensions of disordered proteins

по Wuttke, René, Hofmann, Hagen, Nettels, Daniel, Borgia, Madeleine B., Mittal, Jeetain, Best, Robert B., Schuler, Benjamin
Опубликовано 2014

Charge interactions can dominate the dimensions of intrinsically disordered proteins

по Müller-Späth, Sonja, Soranno, Andrea, Hirschfeld, Verena, Hofmann, Hagen, Rüegger, Stefan, Reymond, Luc, Nettels, Daniel, Schuler, Benjamin
Опубликовано 2010

Transition path times of coupled folding and binding reveal the formation of an encounter complex

по Sturzenegger, Flurin, Zosel, Franziska, Holmstrom, Erik D., Buholzer, Karin J., Makarov, Dmitrii E., Nettels, Daniel, Schuler, Benjamin
Опубликовано в: Nat Commun (2018)

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

по Borgia, Madeleine B., Borgia, Alessandro, Best, Robert B., Steward, Annette, Nettels, Daniel, Wunderlich, Bengt, Schuler, Benjamin, Clarke, Jane
Опубликовано 2011

Role of Denatured-State Properties in Chaperonin Action Probed by Single-Molecule Spectroscopy

по Hofmann, Hagen, Hillger, Frank, Delley, Cyrille, Hoffmann, Armin, Pfeil, Shawn H., Nettels, Daniel, Lipman, Everett A., Schuler, Benjamin
Опубликовано в: Biophys J (2014)

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

по Aznauryan, Mikayel, Delgado, Leonildo, Soranno, Andrea, Nettels, Daniel, Huang, Jie-rong, Labhardt, Alexander M., Grzesiek, Stephan, Schuler, Benjamin
Опубликовано в: Proc Natl Acad Sci U S A (2016)