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Biochimica et biophysica acta, 2011-08, Vol.1814 (8), p.1021-1029
2011
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Autor(en) / Beteiligte
Titel
Protein folding at single-molecule resolution
Ist Teil von
  • Biochimica et biophysica acta, 2011-08, Vol.1814 (8), p.1021-1029
Ort / Verlag
Netherlands: Elsevier B.V
Erscheinungsjahr
2011
Quelle
MEDLINE
Beschreibungen/Notizen
  • The protein folding reaction carries great significance for cellular function and hence continues to be the research focus of a large interdisciplinary protein science community. Single-molecule methods are providing new and powerful tools for dissecting the mechanisms of this complex process by virtue of their ability to provide views of protein structure and dynamics without associated ensemble averaging. This review briefly introduces common FRET and force methods, and then explores several areas of protein folding where single-molecule experiments have yielded insights. These include exciting new information about folding landscapes, dynamics, intermediates, unfolded ensembles, intrinsically disordered proteins, assisted folding and biomechanical unfolding. Emerging and future work is expected to include advances in single-molecule techniques aimed at such investigations, and increasing work on more complex systems from both the physics and biology standpoints, including folding and dynamics of systems of interacting proteins and of proteins in cells and organisms. This article is part of a Special Issue entitled: Protein Dynamics: Experimental and Computational Approaches. ► Powerful single-molecule tools dissect complex protein folding mechanisms. ► They provide views of intricate protein structural distributions and dynamics. ► This review briefly introduces common FRET and force methods. ► Folding landscapes, IDPs, assisted folding and biomechanical unfolding. ► Future work is expected on more complex systems in cells and organisms.
Sprache
Englisch
Identifikatoren
ISSN: 1570-9639, 0006-3002
eISSN: 1878-1454
DOI: 10.1016/j.bbapap.2011.01.011
Titel-ID: cdi_proquest_miscellaneous_1823946682

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