The study of protein mechanics with the atomic force microscope

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

doi:10.1016/S0968-0004(99)01453-X

The study of protein mechanics with the atomic force microscope

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

Research output: Contribution to journal › Review article › peer-review

314 Scopus citations

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 language	English (US)
Pages (from-to)	379-384
Number of pages	6
Journal	Trends in biochemical sciences
Volume	24
Issue number	10
DOIs	https://doi.org/10.1016/S0968-0004(99)01453-X
State	Published - Oct 1 1999
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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title = "The study of protein mechanics with the atomic force microscope",

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.",

author = "Fisher, \{Thomas E.\} and Oberhauser, \{Andres F.\} and Mariano Carrion-Vazquez and Marszalek, \{Piotr E.\} and Fernandez, \{Julio M.\}",

note = "Funding Information: This work was funded by R01 grants from the National Institutes of Health to J. M. Fernandez.",

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T1 - The study of protein mechanics with the atomic force microscope

AU - Fisher, Thomas E.

AU - Oberhauser, Andres F.

AU - Carrion-Vazquez, Mariano

AU - Marszalek, Piotr E.

AU - Fernandez, Julio M.

N1 - Funding Information: This work was funded by R01 grants from the National Institutes of Health to J. M. Fernandez.

PY - 1999/10/1

Y1 - 1999/10/1

N2 - 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.

AB - 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.

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SP - 379

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JO - Trends in biochemical sciences

JF - Trends in biochemical sciences

IS - 10

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The study of protein mechanics with the atomic force microscope

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