Abstract
We use a high resolution atomic force microscopy technique to mechanically unzip and rezip single coiled-coil proteins. This allows us to read off the complete stability profile of the protein turn by turn. We investigated three coiled coils with different length as well as a point mutation and find force fluctuations between 9 and 15 pN that can be directly related to the amino-acid sequences. An equilibrium model previously applied to DNA fully describes the mechanical unzipping process including free-energy contributions of the individual turns and seed formation energy.
- Received 25 November 2005
DOI:https://doi.org/10.1103/PhysRevLett.96.118102
©2006 American Physical Society