We review recent studies on the role played by non-liquid, water-containing matrices on the dynamics and structure of embedded proteins. Two proteins were studied, in water–trehalose matrices: a water-soluble protein (carboxy derivative of horse heart myoglobin) and a membrane protein (reaction centre from Rhodobacter sphaeroides). Several experimental techniques were used: Mfssbauer spectroscopy, elastic neutron scattering, FTIR spectroscopy, CO recombination after flash photolysis in carboxy-myoglobin, kinetic optical absorption spectroscopy following pulsed and continuous photoexcitation in QB containing or QB deprived reaction centre from R. sphaeroides. Experimental results, together with the outcome of molecular dynamics simulations, concurred to give a picture of how water-containing matrices control the internal dynamics of the embedded proteins. This occurs, in particular, via the formation of hydrogen bond networks that anchor the protein surface to the surrounding matrix, whose stiffness increases by lowering the sample water content. In the conclusion section, we also briefly speculate on how the protein–matrix interactions observed in our samples may shed light on the protein–solvent coupling also in liquid aqueous solutions. D 2005 Elsevier B.V. All rights reserved. Keywords: Carboxy myoglobin; Trehalose; Water association band; CO stretching band; Flash photolysis; Reaction centre

Internal dynamics and protein–matrix coupling in trehalose-coated proteins / L., Cordone; G., Cottone; S., Giuffrida; G., Palazzo; G., Venturoli; Viappiani, Cristiano. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - 1749:(2005), pp. 252-281. [10.1016/j.bbapap.2005.03.004]

Internal dynamics and protein–matrix coupling in trehalose-coated proteins

VIAPPIANI, Cristiano
2005-01-01

Abstract

We review recent studies on the role played by non-liquid, water-containing matrices on the dynamics and structure of embedded proteins. Two proteins were studied, in water–trehalose matrices: a water-soluble protein (carboxy derivative of horse heart myoglobin) and a membrane protein (reaction centre from Rhodobacter sphaeroides). Several experimental techniques were used: Mfssbauer spectroscopy, elastic neutron scattering, FTIR spectroscopy, CO recombination after flash photolysis in carboxy-myoglobin, kinetic optical absorption spectroscopy following pulsed and continuous photoexcitation in QB containing or QB deprived reaction centre from R. sphaeroides. Experimental results, together with the outcome of molecular dynamics simulations, concurred to give a picture of how water-containing matrices control the internal dynamics of the embedded proteins. This occurs, in particular, via the formation of hydrogen bond networks that anchor the protein surface to the surrounding matrix, whose stiffness increases by lowering the sample water content. In the conclusion section, we also briefly speculate on how the protein–matrix interactions observed in our samples may shed light on the protein–solvent coupling also in liquid aqueous solutions. D 2005 Elsevier B.V. All rights reserved. Keywords: Carboxy myoglobin; Trehalose; Water association band; CO stretching band; Flash photolysis; Reaction centre
2005
Internal dynamics and protein–matrix coupling in trehalose-coated proteins / L., Cordone; G., Cottone; S., Giuffrida; G., Palazzo; G., Venturoli; Viappiani, Cristiano. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - 1749:(2005), pp. 252-281. [10.1016/j.bbapap.2005.03.004]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11381/1447271
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