Principal components of the protein dynamical transition

Phys Rev Lett. 2003 Nov 14;91(20):208106. doi: 10.1103/PhysRevLett.91.208106. Epub 2003 Nov 14.


Proteins exhibit a solvent-driven dynamical transition at 180-220 K, manifested by nonlinearity in the temperature dependence of the average mean-square displacement. Here, molecular dynamics simulations of hydrated myoglobin show that the onset of the transition at approximately 180 K is characterized by the appearance of a single double-well principal component mode involving a global motion of two groups of helices. As the temperature is raised a few more quasiharmonic and multiminimum components successively appear. The results indicate an underlying simplicity in the protein dynamical transition.

MeSH terms

  • Computer Simulation
  • Models, Chemical*
  • Models, Molecular
  • Myoglobin / chemistry*
  • Principal Component Analysis
  • Protein Conformation
  • Water / chemistry


  • Myoglobin
  • Water