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Vol. 93, Issue 1, 55-59, January 9, 1996

Biophysics
Hydrated myoglobin's anharmonic fluctuations are not primarily due to dihedral transitions

(protein dynamics / protein hydration / conformational substates / dynamical transition / molecular dynamics simulation)

Laboratory of Structural Biology, Division of Computer Research and Technology, National Institutes of Health, Bethesda, MD 20892

Communicated by Hans Frauenfelder, Los Alamos National Laboratory, Los Alamos, NM, September 25, 1995 (received for review April 5, 1995)

To characterize the functionally important anharmonic motions of proteins, simulations of carboxymyoglobin (MbCO) dynamics have been performed during which dihedral transitions were prohibited. Comparison of torsionally restrained and unrestrained protein dynamics simulated at three levels of hydration and at temperatures ranging from 100 to 400 K suggests that hydration "catalyzes" protein mobility by facilitating collective anharmonic motions that do not require dihedral transitions. When dihedral transitions were prohibited, dehydrated MbCO, to a good approximation, exhibited only harmonic fluctuations, whereas hydrated MbCO exhibited both harmonic and anharmonic motions. The fluctuation of helix centers of mass also remained highly anharmonic in the torsionally restrained hydrated system. Atomic mean-square fluctuation at 300 K was reduced upon prohibition of dihedral transitions by only 28% and 10% for MbCO hydrated by 350 and 3830 water molecules, respectively.

0027-8424/96/9355-5/0
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