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Phys Rev Lett. 2003 Nov 14;91(20):208106. Epub 2003 Nov 14.

Principal components of the protein dynamical transition.

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Computational Molecular Biophysics, Interdisciplinary Center for Scientific Computing (IWR), Im Neuenheimer Feld 368, Universit├Ąt Heidelberg, 69120 Heidelberg, Germany.


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.

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