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 1–20 of 20 results
Advanced filters: Author: Justin L. P. Benesch Clear advanced filters

  • Spider silk formation involves tightly regulated protein assembly, influenced by pH and the presence of ions. Here, single-molecule mass photometry reveals that mini-spidroin interactions are influenced by millimolar concentrations of sodium and potassium, which may control the formation of spidroin clusters.

    • Hannah Osterholz
    • Shree Senthil Jeyalekshmy
    • Michael Landreh
    ResearchOpen Access
    Communications Materials
    P: 1-8

  • Filamin C is a key actin-binding protein involved in cardiomyopathies and musculoskeletal disorders. Here, Wang et al reveal that it interacts with the heat shock protein HSPB7 under biomechanical stress, forming a stable hetero-dimer which is regulated by phosphorylation.

    • Zihao Wang
    • Guodong Cao
    • Justin L. P. Benesch
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-16

  • The weakest interactions of protein complexes are thought to be lost when such assemblies are removed from their natural, watery environments. Not so, reveals a study in the vacuum chamber of a mass spectrometer.

    • Justin L. P. Benesch
    • Carol V. Robinson
    News & Views
    Nature
    Volume: 462, P: 576-577

  • The small heat-shock protein HSP27 occurs predominantly in oligomeric forms, which makes its structural characterisation challenging. Here the authors employ CPMG and high-pressure NMR with native mass spectrometry and biophysical assays to show that the active monomeric form of HSP27 is substantially disordered and highly chaperone-active.

    • T. Reid Alderson
    • Julien Roche
    • Andrew J. Baldwin
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-16

  • Molecular phylogenetics, ancestral sequence reconstruction and biophysical protein characterization are used to investigate the interaction between the orange carotenoid protein and its unrelated regulator, the fluorescence recovery protein (FRP). This interaction evolved when a precursor of FRP was horizontally acquired by cyanobacteria.

    • Niklas Steube
    • Marcus Moldenhauer
    • Georg K. A. Hochberg
    ResearchOpen Access
    Nature Ecology & Evolution
    Volume: 7, P: 756-767

  • Citrate synthase from the cyanobacterium Synechococcus elongatus is shown to self-assemble into Sierpiński triangles, a finding that opens up the possibility that other naturally occurring molecular-scale fractals exist.

    • Franziska L. Sendker
    • Yat Kei Lo
    • Georg K. A. Hochberg
    ResearchOpen Access
    Nature
    Volume: 628, P: 894-900

  • Amphipols, bicelles and nanodiscs are used to study intact membrane protein complexes by mass spectrometry, with better preservation of oligomeric complexes than traditional detergent micelles.

    • Jonathan T S Hopper
    • Yvonne Ting-Chun Yu
    • Carol V Robinson
    Research
    Nature Methods
    Volume: 10, P: 1206-1208

  • Experimental analysis of reconstructed ancestral globins reveals that haemoglobin’s complex tetrameric structure and oxygen-binding functions evolved by simple genetic and biophysical mechanisms.

    • Arvind S. Pillai
    • Shane A. Chandler
    • Joseph W. Thornton
    Research
    Nature
    Volume: 581, P: 480-485

  • Mass photometry is a label-free optical approach capable of detecting, imaging and accurately measuring the mass of single biomolecules in solution. Here, the authors demonstrate the potential of mass photometry for quantitatively characterizing sample heterogeneity of purified protein complexes with implications for structural studies specifically and in vitro studies more generally.

    • Adar Sonn-Segev
    • Katarina Belacic
    • Philipp Kukura
    ResearchOpen Access
    Nature Communications
    Volume: 11, P: 1-10

  • Capsid proteins (CPs) of various icosahedral and rod-shaped viruses exhibit structural diversity and tunability as well as application in smart hybrid nanoparticles, however, the potential of CPs of filamentous plant viruses remains underexplored. Here, the authors exploit the structure-based design of CP from potato virus Y to tune the shape, size, RNA encapsidation ability, symmetry, stability, and surface functionalization of nanoparticles.

    • Luka Kavčič
    • Andreja Kežar
    • Marjetka Podobnik
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-19