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Three-dimensional bead position histograms reveal single-molecule nanomechanics.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Becker, Nils B. Altmann, Stephan M. Scholz, Tim Hoerber, J. K. Heinrich Stelzer, Ernst H. K. Rohrbach, Alexander |
| Copyright Year | 2005 |
| Abstract | We describe a method to investigate the structure and elasticity of macromolecules by a combination of single molecule experiments and kinematic modeling. With a photonic force microscope, we recorded spatial position histograms of a fluctuating microsphere tethered to full-length myosin-II. Assuming only that the molecule consists of concatenated rigid segments, a model derived from robot kinematics allows us to relate these histograms to the molecule's segment lengths and bending stiffnesses. Both our calculated position distributions and the experimental data show an asymmetry characteristic of a mixed entropic-enthalpic spring. Our model that fits best to experimental line profiles has two intramolecular hinges, one at the bound head domain, and another about 50 nm down the myosin tail, with a summed bending stiffness of about 3 k(B)T/rad. |
| Starting Page | 021907 |
| Ending Page | 021907 |
| Page Count | 1 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.imtek.de/data/lehrstuehle/bnp/pdf/publications/Becker2005_PRE/at_download/file |
| PubMed reference number | 15783352v1 |
| Volume Number | 71 |
| Issue Number | 2 |
| Part | 1 |
| Journal | Physical review. E, Statistical, nonlinear, and soft matter physics |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Bending - Changing basic body position Microscope Device Component Microspheres Muscle Rigidity Seizures macromolecule ribosome-associated ubiquitin-dependent protein catabolic process |
| Content Type | Text |
| Resource Type | Article |
