1. Molecular dynamics (MD) simulations have their bases in theoretical models describing interactions between atoms through so-called force fields ( 66 – 68 ). In a typical MD simulation initial coordinates of the atoms in a macromolecule are obtained from crystallographic or NMR structures. The structure is then solvated in water and the motion of atoms in time is determined through integration of Newton's equations ( 68 ) assuming the mentioned force field. Current simulation packages such as NAMD ( 68 ) use standardized force fields and provide the source code of the simulation engine. The widespread use and availability of the software and force fields ensures constant verification and reproducibility of results.
2. SMD simulations apply in addition to indigenous forces external forces to biomolecules ( 17 ). There are two typical protocols for SMD simulations: constant force and constant velocity. In constant force SMD simulations a force is directly applied to one or more atoms and extension or displacement is monitored throughout dynamics. Customized time-dependent forces may be applied as well. In constant velocity SMD simulations a moving harmonic potential (spring) is used to induce motion along a reaction coordinate. The free end of the spring is moved at constant velocity while the protein atoms attached to the other end of the spring are subject to the steering force. The force applied is determined by the extension of the spring and can be monitored throughout the entire simulation.
3. Single-Molecule Biomechanics with Optical Methods
4. Single-Molecule Biology: What Is It and How Does It Work?
5. MECHANISM AND DYNAMICS OF CADHERIN ADHESION