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Chemistry

D-Index
64
Citations
16020
World Ranking
7983
National Ranking
167

Overview

Benjamin Schuler is affiliated with the University of Zurich in Switzerland. Their research primarily spans the fields of Biochemistry, Genetics and Molecular Biology, with a strong focus on Molecular Biology. Other subfields include Electrical and Electronic Engineering, Atomic and Molecular Physics and Optics, Biophysics, and Spectroscopy.

The main topics of their research work include:

  • Protein Structure and Dynamics
  • RNA Research and Splicing
  • Advanced Fluorescence Microscopy Techniques
  • Enzyme Structure and Function
  • Genomics and Chromatin Dynamics
  • RNA Interference and Gene Delivery
  • DNA and Nucleic Acid Chemistry

Benjamin Schuler has contributed to several recent scientific publications. Among these are:

  • "Extreme dynamics in a biomolecular condensate" (2023) published in Nature
  • "FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices" (2021) published in eLife
  • "Depletion interactions modulate the binding between disordered proteins in crowded environments" (2020) published in the Proceedings of the National Academy of Sciences
  • "Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes" (2020) published in Nature Communications
  • "Global Structure of the Intrinsically Disordered Protein Tau Emerges from Its Local Structure" (2022) published in JACS Au

The frequent co-authors collaborating with Benjamin Schuler include:

  • Daniel Nettels
  • Andrea Sottini
  • Aritra Chowdhury
  • Robert B. Best
  • Miloš T. Ivanović

Publication venues where Benjamin Schuler appears most often are:

  • Biophysical Journal
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Proceedings of the National Academy of Sciences
  • JACS Au

Best Publications

  • Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy

    Benjamin Schuler;Everett A. Lipman;William A. Eaton

  • Protein folding studied by single-molecule FRET.

    Benjamin Schuler;William A Eaton

  • Extreme disorder in an ultrahigh-affinity protein complex

    Alessandro Borgia;Madeleine B. Borgia;Katrine Østergaard Bugge;Vera M. Kissling

  • From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins

    Sonja Müller-Späth;Andrea Soranno;Verena Hirschfeld;Hagen Hofmann

  • Polyproline and the “spectroscopic ruler” revisited with single-molecule fluorescence

    Benjamin Schuler;Everett A. Lipman;Peter J. Steinbach;Michael Kumke

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

    Hagen Hofmann;Andrea Soranno;Alessandro Borgia;Klaus Gast

  • Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study

    Björn Hellenkamp;Björn Hellenkamp;Sonja Schmid;Sonja Schmid;Olga Doroshenko;Oleg Opanasyuk

  • Single-Molecule Measurement of Protein Folding Kinetics

    Everett A. Lipman;Benjamin Schuler;Olgica Bakajin;William A. Eaton

  • Charge interactions can dominate the dimensions of intrinsically disordered proteins

    Sonja Müller-Späth;Andrea Soranno;Verena Hirschfeld;Verena Hirschfeld;Hagen Hofmann

  • Ultrafast dynamics of protein collapse from single-molecule photon statistics

    Daniel Nettels;Irina V. Gopich;Armin Hoffmann;Benjamin Schuler

  • Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

    Andrea Soranno;Brigitte Buchli;Daniel Nettels;Ryan R. Cheng

  • Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins

    Benjamin Schuler;Andrea Soranno;Hagen Hofmann;Daniel Nettels

  • Single-molecule spectroscopy of protein folding dynamics--expanding scope and timescales.

    Benjamin Schuler;Hagen Hofmann

  • FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices

    Eitan Lerner;Anders Barth;Jelle Hendrix;Benjamin Ambrose

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

    Andrea Soranno;Iwo Koenig;Madeleine B. Borgia;Hagen Hofmann

  • Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells

    Iwo König;Arash Zarrine-Afsar;Mikayel Aznauryan;Andrea Soranno

  • Mapping protein collapse with single-molecule fluorescence and kinetic synchrotron radiation circular dichroism spectroscopy

    Armin S. Hoffmann;Avinash S. Kane;Daniel Nettels;David E. Hertzog

  • Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.

    Daniel Nettels;Sonja Müller-Späth;Frank Küster;Hagen Hofmann

  • Effect of flexibility and cis residues in single-molecule FRET studies of polyproline

    Robert B. Best;Kusai A. Merchant;Irina V. Gopich;Benjamin Schuler

  • Temperature-dependent solvation modulates the dimensions of disordered proteins

    René Wuttke;Hagen Hofmann;Daniel Nettels;Madeleine B. Borgia

  • Two-state folding observed in individual protein molecules.

    Elizabeth Rhoades;Mati Cohen;Benjamin Schuler;Gilad Haran

  • Unfolded protein and peptide dynamics investigated with single-molecule FRET and correlation spectroscopy from picoseconds to seconds.

    Daniel Nettels;and Armin Hoffmann;Benjamin Schuler

Frequent Co-Authors

Robert B. Best
Robert B. Best National Institutes of Health
Robert Seckler
Robert Seckler University of Potsdam
Claus A.M. Seidel
Claus A.M. Seidel Heinrich Heine University Düsseldorf
Edward A. Lemke
Edward A. Lemke Johannes Gutenberg University of Mainz
Philip Tinnefeld
Philip Tinnefeld Ludwig-Maximilians-Universität München
Jane Clarke
Jane Clarke University of Cambridge
Birthe B. Kragelund
Birthe B. Kragelund University of Copenhagen
Taekjip Ha
Taekjip Ha Johns Hopkins University
Don C. Lamb
Don C. Lamb Ludwig-Maximilians-Universität München
Andreas Plückthun
Andreas Plückthun University of Zurich

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