Emerging computational approaches for the study of protein allostery

Arch Biochem Biophys. 2013 Oct 1;538(1):6-15. doi: 10.1016/j.abb.2013.07.025. Epub 2013 Aug 8.

Abstract

Allosteric regulation of protein function is key in controlling cellular processes so its underlying mechanisms are of primary concern to research in areas spanning protein engineering and drug design. However, due to the complex nature of allosteric mechanisms, a clear and predictive understanding of the relationship between protein structure and allosteric function remains elusive. Well established experimental approaches are available to offer a limited degree of characterization of mechanical properties within proteins, but the analytical capabilities of computational methods are evolving rapidly in their ability to accurately define the subtle and concerted structural dynamics that comprise allostery. This review includes a brief overview of allostery in proteins and an exploration of relevant experimental methods. An explanation of the transition from experimental toward computational methods for allostery is discussed, followed by a review of existing and emerging methods.

Keywords: Allostery; Conformational dynamics; Molecular dynamics; Simulation.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Allosteric Site*
  • Binding Sites
  • Computational Biology / methods*
  • Computer Simulation
  • Crystallography, X-Ray
  • Humans
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Microscopy, Fluorescence
  • Models, Molecular
  • Molecular Dynamics Simulation
  • Monte Carlo Method
  • Protein Structure, Secondary
  • Proteins / chemistry*

Substances

  • Proteins