Please use this identifier to cite or link to this item: http://hdl.handle.net/2307/357
Title: Dielectric Relaxations in Confined Hydrated Myoglobin
Authors: Schiro, Giorgio
Cupane, Antonio
Vitrano, Eugenio
Bruni, Fabio
Keywords: NEUTRON-SCATTERING
PROTEIN DYNAMICS
LYSOZYME POWDERS
SILICA
HYDROGELS
WATER
SPECTROSCOPY
HEMOGLOBIN
SOLVENT
TRANSITION
ENCAPSULATION
Issue Date: Jul-2009
Publisher: American Chemical Society
Abstract: In this work we report the results of a broadband dielectricspectroscopy study on the dynamics of a globular protein, myoglobin, inconfined geometry, i.e. encapsulated in a porous silica matrix, at lowhydration levels, where about only one or two water layers surround theproteins. In order to highlight the specific effect of confinement inthe silica host, we compared this system with hydrated myoglobinpowders at the same hydration levels. The comparison between the datarelative to the two different systems indicates that geometricalconfinement within the silica matrix plays a crucial role inprotein-water dielectric relaxations, the effect of sol-gelencapsulation being essentially a suppression of cooperativerelaxations that involve the coherence/ cooperativity of solventmotions and solvent-coupled protein dynamics. We also provide directevidence that protein relaxations inside the gel depend on thehydration level and are "slaved" to the solvent beta-relaxation.
URI: http://hdl.handle.net/2307/357
ISSN: 1520-6106
DOI: 10.1021/jp901420r
Appears in Collections:A - Articolo su rivista
X_Dipartimento di Fisica 'Edoardo Amaldi'

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