Dynamics of activated processes in globular proteins

  • McCammon J
  • Karplus M
  • 25


    Mendeley users who have this article in their library.
  • 72


    Citations of this article.


A procedure for the dynamical simulation of activated processes, such as ligand binding and enzymatic reactions, in a globular protein is outlined. Preliminary calculations of the transition state geometry and barrier crossing trajectories are presented for a model reaction, the rotation of an aromatic ring in the bovine pancreatic trypsin inhibitor. The results show that repulsive nonbonded interactions between the ring atoms and the atoms in the surrounding protein matrix determine the dynamical character of the reorientation process; the nonbonded interactions are the source of the rotational barrier and of the impulses that speed up or slow down the ring motion during the barrier crossings.

Author-supplied keywords

  • *Trypsin Inhibitors
  • Animals
  • Catalysis
  • Cattle
  • Enzyme Activation
  • Hydrogen
  • Motion
  • Pancreas/enzymology
  • Protein Conformation
  • Thermodynamics
  • Tyrosine

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • J A McCammon

  • M Karplus

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free