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Title of Journal: Cell Biochem Biophys

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Abbravation: Cell Biochemistry and Biophysics

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Springer-Verlag

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DOI

10.1007/s11240-008-9398-5

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1559-0283

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Spectroscopic Determination of Lysozyme Conformati

Authors: Davide Barreca Giuseppina Laganà Silvana Ficarra Giuseppe Gattuso Salvatore Magazù Roberto La Torre Ester Tellone Ersilia Bellocco
Publish Date: 2012/11/27
Volume: 66, Issue: 2, Pages: 297-307
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Abstract

The bioprotective action of the disaccharide trehalose has been studied against the wellknown denaturating agent guanidine hydrochloride The results indicated a direct influence of trehalose on both enzymatic activity and conformational changes of lysozyme as shown by the decrease of the inactivation rate constant of about 148fold and the loss of αhelix structure of lysozyme In addition ESI–MS hydrogen–deuterium H/D exchange experiments allowed us to correlate the structural and dynamic features of the protein in the presence of the two additives highlighting as trehalose remarkably influenced this exchange by decreasing local protein environment changes and solvent accessibility to the amide peptide backbone as further evidenced by circular dichroism and 1H NMR measurements

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