The study of protein mechanics with the atomic force microscope

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

Research output: Contribution to journalArticle

265 Citations (Scopus)

Abstract

The unfolding and folding of single protein molecules can be studied with an atomic force microscope (AFM). Many proteins with mechanical functions contain multiple, individually folded domains with similar structures. Protein engineering techniques have enabled the construction and expression of recombinant proteins that contain multiple copies of identical domains. Thus, the AFM in combination with protein engineering has enabled the kinetic analysis of the force-induced unfolding and refolding of individual domains as well as the study of the determinants of mechanical stability. Copyright (C) 1999 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)379-384
Number of pages6
JournalTrends in Biochemical Sciences
Volume24
Issue number10
DOIs
StatePublished - Oct 1 1999
Externally publishedYes

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Protein Engineering
Mechanics
Microscopes
Protein Folding
Recombinant Proteins
Proteins
Mechanical stability
Molecules
Kinetics

ASJC Scopus subject areas

  • Biochemistry

Cite this

The study of protein mechanics with the atomic force microscope. / Fisher, Thomas E.; Oberhauser, Andres; Carrion-Vazquez, Mariano; Marszalek, Piotr E.; Fernandez, Julio M.

In: Trends in Biochemical Sciences, Vol. 24, No. 10, 01.10.1999, p. 379-384.

Research output: Contribution to journalArticle

Fisher, TE, Oberhauser, A, Carrion-Vazquez, M, Marszalek, PE & Fernandez, JM 1999, 'The study of protein mechanics with the atomic force microscope', Trends in Biochemical Sciences, vol. 24, no. 10, pp. 379-384. https://doi.org/10.1016/S0968-0004(99)01453-X
Fisher, Thomas E. ; Oberhauser, Andres ; Carrion-Vazquez, Mariano ; Marszalek, Piotr E. ; Fernandez, Julio M. / The study of protein mechanics with the atomic force microscope. In: Trends in Biochemical Sciences. 1999 ; Vol. 24, No. 10. pp. 379-384.
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