Single protein misfolding events captured by atomic force microscopy

Andres Oberhauser, Piotr E. Marszalek, Mariano Carrion-Vazquez, Julio M. Fernandez

Research output: Contribution to journalArticle

158 Citations (Scopus)

Abstract

Using single protein atomic force microscopy (AFM) techniques we demonstrate that after repeated mechanical extension/relaxation cycles, tandem modular proteins can misfold into a structure formed by two neighboring modules. The misfolding is fully reversible and alters the mechanical topology of the modules while it is about as stable as the original fold. Our results show that modular proteins can assume a novel misfolded state and demonstrate that AFM is able to capture, in real time, rare misfolding events at the level of a single protein.

Original languageEnglish (US)
Pages (from-to)1025-1028
Number of pages4
JournalNature Structural Biology
Volume6
Issue number11
DOIs
StatePublished - 1999
Externally publishedYes

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Atomic Force Microscopy
Atomic force microscopy
Proteins
Topology

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Single protein misfolding events captured by atomic force microscopy. / Oberhauser, Andres; Marszalek, Piotr E.; Carrion-Vazquez, Mariano; Fernandez, Julio M.

In: Nature Structural Biology, Vol. 6, No. 11, 1999, p. 1025-1028.

Research output: Contribution to journalArticle

Oberhauser, A, Marszalek, PE, Carrion-Vazquez, M & Fernandez, JM 1999, 'Single protein misfolding events captured by atomic force microscopy', Nature Structural Biology, vol. 6, no. 11, pp. 1025-1028. https://doi.org/10.1038/14907
Oberhauser, Andres ; Marszalek, Piotr E. ; Carrion-Vazquez, Mariano ; Fernandez, Julio M. / Single protein misfolding events captured by atomic force microscopy. In: Nature Structural Biology. 1999 ; Vol. 6, No. 11. pp. 1025-1028.
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