Journal
PHYSICAL REVIEW LETTERS
Volume 91, Issue 20, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.91.208106
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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 similar to180 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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