|
|
|
 Force Probe Molecular Dynamics |
|
|
|
|
Mechanical Properties of Alpha-Helices
|
|
Rainer Böckmann, Berthold Heymann and Helmut Grubmüller
|
| |
|
Unfolding and elastic properties of peptide secondary structure elements play an important role in many biological macromolecules. In the muscle protein myosin, e.g., an alpha-helix acts as a lever and induces the power stroke. Single molecule experiments allow to probe the underlying mechanisms by measuring elastic properties like the stretching force or the stiffness.
In order to get insight in the involved interactions at the atomic level we performed enforced unfolding molecular dynamics simulations of a cysteine3-lysine30-cysteine peptide which adopts an alpha-helical structure at high pH value [1]. Our computed elastic properties and unfolding forces agree with the corresponding experimental data [1].
Below you see a video of a 2.4 nanosecond (2.4*10-9 seconds) molecular dynamics unfolding simulation.
|
| |
|
|
| |
|
References
|
|
- M. A. Lantz, S. P. Jarvis, H. Tokumoto, T. Martynski, T. Kusumi, C. Nakamura and J. Miyake.
Stretching the α-helix: a direct measure of the hydrogen-bond energy of a single-peptide molecule.
Chem. Phys. Lett. 315 (1999) 61-68.
- R. Böckmann and H. Grubmüller, "Elastic properties of secondary structure elements: A molecular dynamics study", Europ. Biophys. J. 29 (2000), 381
[abstract]
|
| |
|
|
|
Top