Letter abstract


Nature Nanotechnology 4, 514 - 517 (2009)
Published online: 28 June 2009 | doi:10.1038/nnano.2009.156

Subject Categories: Nanobiotechnology | Nanometrology and instrumentation

Determination of protein structural flexibility by microsecond force spectroscopy

Mingdong Dong1, Sudhir Husale1 & Ozgur Sahin1


Proteins are dynamic molecular machines having structural flexibility that allows conformational changes1, 2. Current methods for the determination of protein flexibility rely mainly on the measurement of thermal fluctuations and disorder in protein conformations3, 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 timescales6, 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.

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  1. Rowland Institute at Harvard, Harvard University, Cambridge, Massachusetts 02142 USA

Correspondence to: Ozgur Sahin1 e-mail: sahin@rowland.harvard.edu



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