Characteristic Motions in Proteins

Molecular dynamics is concerned with time dependent processes in molecular systems.

The following table surveys the different types of motions in a protein. These motions span almost 20 orders-of-magnitude in characteristic time (from picoseconds to hours).

Type of Motion Functionality Examples Time and Amplitude Scales
Local Motions:
  • Atomic fluctuation
  • Side chain motion


  • Ligand docking flexibility
  • Temporal diffusion pathways


fs - ps
(10-15 - 10-12 s)
less than 1 A
Medium Scale Motions:
  • Loop motion
  • Terminal-arm motion
  • Rigid-body motion (helices)


  • Active site conformation adaptation
  • Binding specificity


ns - micro s
(10-9 - 10-6 s)
1 - 5 A
Large Scale Motions:
  • Domain motion
  • Subunit motion


  • Hinge bending motion
  • Allosteric transitions


micro s - ms
(10-6 - 10-3 s)
5 - 10 A
Global Motions:
  • Helix-coil transition
  • Folding/unfolding
  • Subunit association


  • Hormone activation
  • Protein functionality


ms - h
(10-3 - 104 s)
more than 5 A

The equation that describes the temporal evolution of a physical system is called an equation of motion. There are several different equations of motion, which characterize the motion in different ways:

Equation of Motion Kind of System
Time-dependent Schroedinger Equation A quantum-mechanical system
Newton's Equations A classical-mechanical system
Langevin's Equation A stochastic system

Molecules are quantum-mechanical systems the motion of which should be described by the Schroedinger Equation. However, limits on computational power make the application of Schroedinger's Equation for large systems impractical. Hence, the motion of a molecule is usually approximated by the laws of classical mechanics and by Newton's equation of Motion.

Some important properties of Newton's equation of motion are:

These properties are used to test whether the numerical solution of the equation (i.e., the molecular dynamics simulation) is stable and reliable.


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