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RESEARCH PRODUCT

Structure−Dynamics Coupling between Protein and External Matrix in Sucrose-Coated and in Trehalose-Coated MbCO:  An FTIR Study

Lorenzo CordoneSergio GiuffridaAnd Grazia Cottone

subject

disaccharides FTIR spectroscopy protein waterSucroseAnalytical chemistryTrehaloseSurfaces Coatings and FilmsCoupling (electronics)Matrix (chemical analysis)chemistry.chemical_compoundProtein environmentCrystallographychemistryMaterials ChemistryPhysical and Theoretical ChemistryFourier transform infrared spectroscopyHeme

description

We performed FTIR measurements on carboxy-myoglobin (MbCO) embedded in a sucrose−water matrix to study the degrees of freedom coupling between protein and external matrix in such a system. The work was undertaken on the light of recent results by Giuffrida et al. (J. Phys. Chem. B 2003, 107, 13211−13217), who evidenced, in trehalose-coated MbCO, a structured water−sugar environment of the protein, tightly coupled to the heme pocket structure. Such information was obtained through a suitable analysis of the temperature dependence of the CO stretching and of the water association bands in samples of different content of residual water. We applied here the same analysis to sucrose-coated MbCO. Comparison between the results obtained in the two saccharide systems points out the different free-energy landscape experienced by the protein and matrix atoms. This is put forward by the differences in heme pocket structure (shape of the CO stretching band) and in protein environment (shape of the water association b...

https://doi.org/10.1021/jp047894k