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. 1979 Aug;76(8):3585–3589. doi: 10.1073/pnas.76.8.3585

Dynamics of activated processes in globular proteins.

J A McCammon, M Karplus
PMCID: PMC383876  PMID: 291026

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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