A

Probing Single Chaperone Substrates

Royal Society of Chemistry eBooks, pp. 278–318

Abstract

Regulating protein states is considered the core function of chaperones. However, despite their importance to all major cellular processes, the conformational changes that chaperones impart on polypeptide chains are difficult to study directly due to their heterogeneous, dynamic, and multi-step nature. Here, we review recent advances towards this aim using single-molecule manipulation methods, which are rapidly revealing new mechanisms of conformational control and helping to define a different perspective on the chaperone function.

Authors 10

  1. Institute for Atomic and Molecular Physics

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

    bLUMICKS BV, Amsterdam, The Netherlands

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands; bLUMICKS BV, Amsterdam, The Netherlands

  2. Institute of Science and Technology Austria · Institute for Atomic and Molecular Physics

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

    cInstitute of Science and Technology Austria, Am Campus 1, Klosterneuburg 3400, Austria

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands; cInstitute of Science and Technology Austria, Am Campus 1, Klosterneuburg 3400, Austria

  3. University of Cambridge · Institute for Atomic and Molecular Physics

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

    dDepartment of Pharmacology, University of Cambridge, CB2 1PD Cambridge, UK

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands; dDepartment of Pharmacology, University of Cambridge, CB2 1PD Cambridge, UK

  4. University of Nottingham · Institute for Atomic and Molecular Physics · University of Birmingham

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

    eCentre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, Midlands, UK

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands; eCentre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, Midlands, UK

  5. Institute for Atomic and Molecular Physics

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

  6. Institute for Atomic and Molecular Physics

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

  7. Institute for Atomic and Molecular Physics

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

  8. Leiden University

    Affiliation as printed

    fMedical Systems Biophysics and Bioengineering, Leiden Academic Centre for Drug Research, Faculty of Science, Leiden University, 2333CC, Leiden, The Netherlands

    gCentre for Interdisciplinary Genome Research, Faculty of Science, Leiden University, Einsteinweg 55, 2333CC Leiden, The Netherlands

  9. Leiden University

    Affiliation as printed

    fMedical Systems Biophysics and Bioengineering, Leiden Academic Centre for Drug Research, Faculty of Science, Leiden University, 2333CC, Leiden, The Netherlands

    gCentre for Interdisciplinary Genome Research, Faculty of Science, Leiden University, Einsteinweg 55, 2333CC Leiden, The Netherlands

  10. Institute for Atomic and Molecular Physics · Delft University of Technology

    Affiliation as printed

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands

    hBionanoscience Department of Delft University of Technology and Kavli Institute of Nanoscience Delft, 2629HZ Delft, The Netherlands

    aAMOLF, Science Park 104, 1098 XG Amsterdam, The Netherlands; hBionanoscience Department of Delft University of Technology and Kavli Institute of Nanoscience Delft, 2629HZ Delft, The Netherlands

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References 204