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Determination of protein structural flexibility by microsecond force spectroscopy

Determination of protein structural flexibility by microsecond force spectroscopy Proteins are dynamic molecular machines having structural flexibility that allows conformational changes 1,2 . Current methods for the determination of protein flexibility rely mainly on the measurement of thermal fluctuations and disorder in protein conformations 3,4,5 and tend to be experimentally challenging. Moreover, they reflect atomic fluctuations on picosecond timescales, whereas the large conformational changes in proteins typically happen on micro- to millisecond timescales 6,7 . Here, we directly determine the flexibility of bacteriorhodopsin—a protein that uses the energy in light to move protons across cell membranes—at the microsecond timescale by monitoring force-induced deformations across the protein structure with a technique based on atomic force microscopy. In contrast to existing methods, the deformations we measure involve a collective response of protein residues and operate under physiologically relevant conditions with native proteins. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Nanotechnology Springer Journals

Determination of protein structural flexibility by microsecond force spectroscopy

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References (31)

Publisher
Springer Journals
Copyright
Copyright © 2009 by Nature Publishing Group
Subject
Materials Science; Materials Science, general; Nanotechnology; Nanotechnology and Microengineering
ISSN
1748-3387
eISSN
1748-3395
DOI
10.1038/nnano.2009.156
Publisher site
See Article on Publisher Site

Abstract

Proteins are dynamic molecular machines having structural flexibility that allows conformational changes 1,2 . Current methods for the determination of protein flexibility rely mainly on the measurement of thermal fluctuations and disorder in protein conformations 3,4,5 and tend to be experimentally challenging. Moreover, they reflect atomic fluctuations on picosecond timescales, whereas the large conformational changes in proteins typically happen on micro- to millisecond timescales 6,7 . Here, we directly determine the flexibility of bacteriorhodopsin—a protein that uses the energy in light to move protons across cell membranes—at the microsecond timescale by monitoring force-induced deformations across the protein structure with a technique based on atomic force microscopy. In contrast to existing methods, the deformations we measure involve a collective response of protein residues and operate under physiologically relevant conditions with native proteins.

Journal

Nature Nanotechnology – Springer Journals

Published: Jun 28, 2009

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