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J. Biol. Chem., Vol. 283, Issue 11, 6617-6621, March 14, 2008

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 283/11/6617    most recent R700050200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Google Scholar Articles by Oberhauser, A. F. Articles by Carrión-Vázquez, M. PubMed PubMed Citation Articles by Oberhauser, A. F. Articles by Carrión-Vázquez, M. Social Bookmarking                      What's this?

Minireview

Mechanical Biochemistry of Proteins One Molecule at a Time^*

Andres F. Oberhauser¹ and Mariano Carrión-Vázquez²

From the Departments of Neuroscience and Cell Biology and of Biochemistry and Molecular Biology and the Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555 and the Instituto Cajal, Consejo Superior de Investigaciones Científicas, and the Centro de Investigación Biomédica en Red sobre Enfermedades Neurodegenerativas, E-28002 Madrid, Spain

The activity of proteins and their complexes often involves the conversion of chemical energy (stored or supplied) into mechanical work through conformational changes. Mechanical forces are also crucial for the regulation of the structure and function of cells and tissues. Thus, the shape of eukaryotic cells (and by extension, that of the multicellular organisms they form) is the result of cycles of mechanosensing, mechanotransduction, and mechanoresponse. Recently developed single-molecule atomic force microscopy techniques can be used to manipulate single molecules, both in real time and under physiological conditions, and are ideally suited to directly quantify the forces involved in both intra- and intermolecular protein interactions. In combination with molecular biology and computer simulations, these techniques have been applied to characterize the unfolding and refolding reactions in a variety of proteins. Single-molecule mechanical techniques are providing fundamental information on the structure and function of proteins and are becoming an indispensable tool to understand how these molecules fold and work.

^* This minireview will be reprinted in the 2008 Minireview Compendium, which will be available in January, 2009. This work was supported by Grant R01DK073394 from the National Institutes of Health, the John Sealy Memorial Endowment Fund for Biomedical Research, and Grant 116a2r from the Polycystic Kidney Foundation (to A. F. O.) and by Grant BIO200767116 from the Spanish Ministry of Science and Education, Grant S-0505/MAT/0283 from the Consejería de Educación of the Madrid Community, and Grant 200620F00 from the Spanish Research Council (to M. C.-V.).

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1 and an additional reference.

¹ To whom correspondence may be addressed: afoberha{at}utmb.edu. ² To whom correspondence may be addressed: mcarrion{at}cajal.csic.es.

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