Abstract:
: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.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Cottone G,Cordone L,Ciccotti Gdoi
10.1016/S0006-3495(01)76072-9subject
Has Abstractpub_date
2001-02-01 00:00:00pages
931-8issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(01)76072-9journal_volume
80pub_type
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