Dynamic properties of deoxy hemoglobin encapsulated in silica gels

Rausei, Magda; Cupane, Antonio
April 2000
AIP Conference Proceedings;2000, Vol. 513 Issue 1, p210
Academic Journal
We have encapsulated native human hemoglobin (Hb) in wet porous silica gels. Suitable treatment of the samples enables to obtain transparent gels in which the Hb molecule is still able to reversibly bind exogenous ligands; however, due to the constraints imposed by the vitreous silica matrix, the Hb tetramer is unable to perform the T-R quaternary transition. Using the gel encapsulation technique we have obtained deoxy Hb samples encapsulated in the “T” or “R” quaternary structure. The study of the temperature dependence of the Soret absorption band in the above samples enables to have informations on the local dynamic properties of the heme pocket and therefore to study the dynamics of the protein in a given ligation state but in different quaternary conformations. The results show that the “T” quaternary conformation is, from a dynamic point of view, intrinsically different from the “R” conformation and is characterized by increased anharmonic motions. © 2000 American Institute of Physics.


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