Advanced search

Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–13 of 13 results
Advanced filters: Author: Thorsten Hugel Clear advanced filters

  • Ribosomal translation is coupled to cotranslational protein folding, process assisted by dedicated chaperones. Here, authors present structures of the ribosome-bound yeast Hsp70 chaperone Ssb, identifying its ribosomal binding site and revealing its interactions with a model nascent chain.

    • Ying Zhang
    • Lorenz Grundmann
    • Sabine Rospert
    ResearchOpen Access
    Nature Communications
    Volume: 17, P: 1-15

  • The Hsp90 chaperone is responsible for the stabilization of a large variety of regulatory proteins. Single-molecule FRET was used to examine the conformational dynamics of Hsp90 in its different nucleotide-bound states. The findings suggest that, in the absence of substrate and cochaperone proteins, Hsp90's conformational changes are not strongly coupled to ATP hydrolysis.

    • Moritz Mickler
    • Martin Hessling
    • Thorsten Hugel
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 281-286

  • Crystals are often covered by a thin liquid layer of their own melt which can be related to phenomena of surface premelting, secondary nucleation and melting point depression. Here the authors show that semi cylindrical filaments of polyethylene contain a crystalline core bounded by molten regions and propose that these three phenomena are related and dominated by the intermolecular forces acting at crystal surfaces.

    • Da Huang
    • Thorsten Hugel
    • Günter Reiter
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-9

  • The Seventh International Conference on the Hsp90 Chaperone Machine took place in October 2014, in Seeon, Germany. The program highlighted recent findings in a variety of areas, including structures of heat-shock protein 90 (Hsp90)–client protein complexes, coordination of Hsp90 with cochaperones, new cellular and physiological roles for Hsp90 and therapeutic targeting of the Hsp90 ensemble for the treatment of disease and prevention of infection.

    • Serena Schwenkert
    • Thorsten Hugel
    • Marc B Cox
    News & Views
    Nature Structural & Molecular Biology
    Volume: 21, P: 1017-1021

  • Combining single-molecule Förster resonance energy transfer (FRET) and fluorescence lifetime information inside an anti-Brownian electrokinetic (ABEL) trap makes it possible to distinguish dozens of biomolecules in a sample mixture. This method enables extensive barcoding of biomolecules with a minimal set of chemical components and opens up a path toward biomolecule quantification in complex mixtures.

    • Thorsten Hugel
    News & Views
    Nature Nanotechnology
    Volume: 19, P: 1081-1082

  • The precise role of cochaperones and ATP hydrolysis in driving Hsp90’s chaperone cycle is largely unclear. Here, the authors use single-molecule FRET to show that several cochaperones are necessary to establish directionality in Hsp90’s conformational cycle.

    • Leonie Vollmar
    • Julia Schimpf
    • Thorsten Hugel
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-11

  • The ability to infer quantitative kinetic information from single-molecule FRET (smFRET) data can be challenging. Here the authors perform a blind benchmark study assessing different analysis tools used to infer kinetic rate constants from smFRET trajectories, testing on simulated and experimental data.

    • Markus Götz
    • Anders Barth
    • Sonja Schmid
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-12