• DocumentCode
    2389808
  • Title

    Water and protein dynamics in protein - Water mixtures over wide ranges of composition

  • Author

    Kyritsis, A. ; Panagopoulou, A. ; Pissis, P. ; Serra, R. S i ; Ribelles, J. L Gómez ; Shinyashiki, N.

  • Author_Institution
    Dept. of Phys., Nat. Tech. Univ. of Athens, Athens, Greece
  • fYear
    2011
  • fDate
    28-31 Aug. 2011
  • Firstpage
    49
  • Lastpage
    50
  • Abstract
    In this paper, glass transition and water and protein dynamics were studied in water mixtures of two globular proteins, lysozyme and BSA, by DSC, DRS and TSDC measurements. DSC measurements were used for the study of crystallization and melting phenomena of absorbed water. The noncrystallized water has been determined to be about 0.20 and 0.24 for Lysozyme and BSA, respectively, independent on hw. Dielectric measurements reveal the α relaxation process associated with the glass transition of the hydrated proteins for both systems, in agreement with DSC results. For water fractions where no crystallization of water occurs during cooling our results shown a strong plasticization of Tg. Splitting of the the α relaxation process, observed for hw >; 0.20, is maybe due to microphase separation occurred on both hydrated proteins at that hydration levels.
  • Keywords
    biochemistry; crystallisation; differential scanning calorimetry; enzymes; glass transition; melting; molecular biophysics; phase separation; solvation; sorption; water; α relaxation process; BSA; DRS; DSC; H2O; TSDC; absorbed water; cooling; crystallization; dielectric measurement; glass transition; globular proteins; hydrated proteins; lysozyme; melting phenomena; microphase separation; noncrystallized water; plasticization; water mixtures; water-protein dynamics; Glass; Heating; Proteins;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Electrets (ISE), 2011 14th International Symposium on
  • Conference_Location
    Montpellier
  • ISSN
    2153-3253
  • Print_ISBN
    978-1-4577-1023-0
  • Type

    conf

  • DOI
    10.1109/ISE.2011.6084976
  • Filename
    6084976