Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix.

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 J

journal_title

Biophysical journal

authors

Cottone G,Cordone L,Ciccotti G

doi

10.1016/S0006-3495(01)76072-9

subject

Has Abstract

pub_date

2001-02-01 00:00:00

pages

931-8

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(01)76072-9

journal_volume

80

pub_type

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