Journal
CHEMICAL PHYSICS
Volume 345, Issue 2-3, Pages 275-282Publisher
ELSEVIER
DOI: 10.1016/j.chemphys.2007.07.012
Keywords
protein dynamics; MbCO A substates; FTIR spectroscopy; elastic neutron scattering; molecular dynamics simulation; trehalose
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As it is well known, the thermal behaviour of the CO stretching band in MbCO reflects the interconversion among protein's taxonomic and lower tier substates. We compare here FTIR data on the thermal behaviour of the CO stretching band in MbCO embedded in non-liquid, water-trehalose matrixes, and neutron scattering data on dry and hydrated proteins and nucleic acids. The comparison, also in the light of simulative data, gives relevant information on the relationship between the mean square displacements of hydrogen atoms and the heme pocket thermal rearrangements in MbCO, as experienced by the bound CO, in the temperature region 100-200 K, and at higher temperature when large scale protein motions take place, following the so-called dynamic transition. The reported results point out how FTIR is a useful tool to study the protein internal dynamics, and complement information from neutron scattering measurements. (C) 2007 Elsevier B.V. All rights reserved.
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