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Thermodynamic Properties Underlying the α-Helix-to-β-Sheet Transition, Aggregation, and Amyloidogenesis of Polylysine as Probed by Calorimetry, Densimetry, and Ultrasound Velocimetry

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    Thermodynamic Properties Underlying the α-Helix-to-β-Sheet Transition, Aggregation, and Amyloidogenesis of Polylysine as Probed by Calorimetry, Densimetry, and Ultrasound Velocimetry
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    University of Dortmund, Department of Chemistry, Physical Chemistry I, Otto-Hahn-Strasse 6, D-44227 Dortmund, Germany
    TF Instruments, Im Neuenheimer Feld 515, D-69129 Heidelberg, Germany
    Institute for High Pressure Physics, Polish Academy of Sciences, Sokolowska 29/37, 01-142 Warsaw, Poland
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    The Journal of Physical Chemistry B

    Cite this: J. Phys. Chem. B 2005, 109, 41, 19043–19045
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    https://doi.org/10.1021/jp053283w
    Published September 27, 2005
    Copyright © 2005 American Chemical Society
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    Abstract

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    In this work, we performed a detailed thermodynamic study of an aggregation-prone polypeptide, polylysine, to gain a deeper insight into the scenario of physicochemical events during its unfolding, aggregation, and amyloidogenesis. The precise and simultaneous determination of the partial molar volume, the heat capacity, and the coefficients of thermal expansion, as well as adiabatic and isothermal compressibility of the protein upon unfolding and aggregation, yields a thermodynamic picture of the aggregation process highlighting the importance of volume fluctuations during unfolding and amyloidogenesis of proteins.

    Copyright © 2005 American Chemical Society

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     Corresponding author. E-mail:  [email protected].

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    The Journal of Physical Chemistry B

    Cite this: J. Phys. Chem. B 2005, 109, 41, 19043–19045
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jp053283w
    Published September 27, 2005
    Copyright © 2005 American Chemical Society
    Request reuse permissions

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