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Volume 22 (2008), Issue 2-3, Pages 165-176

Hydration structure analysis of lysozyme amyloid fibrils by thermally stimulated depolarization currents (TSDC) technique

Maria Grazia Bridelli1,2 and Rosanna Capelletti1

1Dipartimento di Fisica and CNISM, University of Parma, Parma, Italy
2Department of Physics, University of Parma, Viale G.P, Usberti 7/A, Parco Area delle Scienze, 43100 Parma, Italy

Copyright © 2008 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Thermally stimulated depolarization currents technique has been employed to investigate the conformation of hen egg white lysozyme in native and amyloid form, in the state of powder at very low hydration level. The technique, able to detect the current generated by thermally activated reorientation of water dipoles previously oriented by an electric field, exploits H2O dipoles, belonging to the solvation shell, as a probe to gain information on the protein conformation.

Large differences are detected between the TSDC spectra related to the two different protein conformations, for what concerns the number and position of the main peaks, the native form displaying two peaks, at TM=175 K and at TM=297 K, and the amyloid one, only one at intermediate temperature (TM=235 K). The spectra have been compared with those monitored for poly-L-lysine (MW 80400), as received and prepared in different ways, i.e. α-helix, β-sheet, and coil conformation, respectively. The poly-L-lysine spectra show specific features that can be attributed to water texture around the secondary structure adopted by the macromolecule: the results stress how TSDC technique is a tool of great potential value in the conformational analysis of proteins.