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Biophys J, February 2001, p. 931-938, Vol. 80, No. 2
and
*INFM and Physics Department, University of Rome La Sapienza, 00185 Rome; and INFM and Department of Physical and
Astronomical Sciences, University of Palermo, 90123 Palermo, Italy
We report on a molecular dynamics (MD) simulation of
carboxy-myoglobin (MbCO) embedded in a water-trehalose system. The mean square fluctuations of protein atoms, calculated at different temperatures in the 100-300 K range, are compared with those from a
previous MD simulation on an H2O-solvated MbCO and with
experimental data from Mössbauer spectroscopy and incoherent
elastic neutron scattering on trehalose-coated MbCO. The results show
that, for almost all the atomic classes, the amplitude of the
nonharmonic motions stemming from the interconversion among the
protein's conformational substates is reduced with respect to the
H2O-solvated system, and their onset is shifted toward
higher temperature. Moreover, our simulation shows that, at 300 K, the
heme performs confined diffusive motions as a whole, leaving the
underlying harmonic vibrations unaltered.
Biophys J, February 2001, p. 931-938, Vol. 80, No. 2
© 2001 by the Biophysical Society 0006-3495/01/02/931/08 $2.00
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