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Specific heat upon aqueous unfolding of the protein interior: a theoretical approach

Author

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  • Bakk, Audun
  • Høye, Johan S.
  • Hansen, Alex

Abstract

We study theoretically the thermodynamics, over a broad temperature range (5–125°C), related to hydrated water upon protein unfolding. The hydration effect is modeled as interacting dipoles in an external field, mimicking the influence from the unfolded surfaces on the surrounding water compared to bulk water. The heat capacity change upon hydration is compared with experimental data from Privalov and Makhatadze on four different proteins: myoglobin, lysozyme, cytochrome c and ribonuclease. Despite the simplicity of the model, it yields good correspondence with experiments. With some interest we note that the effective coupling constants are the same for myoglobin, lysozyme, and cytochrome c, although they are slightly different for ribonuclease.

Suggested Citation

  • Bakk, Audun & Høye, Johan S. & Hansen, Alex, 2002. "Specific heat upon aqueous unfolding of the protein interior: a theoretical approach," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 304(3), pages 355-361.
    • Handle: RePEc:eee:phsmap:v:304:y:2002:i:3:p:355-361
    DOI: 10.1016/S0378-4371(01)00569-6
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    References listed on IDEAS

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    1. Hansen, Alex & Jensen, Mogens H & Sneppen, Kim & Zocchi, Giovanni, 1999. "A model for the thermodynamics of globular proteins," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 270(1), pages 278-287.
    2. Bakk, Audun & Hansen, Alex & Sneppen, Kim, 2001. "Protein model exhibiting three folding transitions," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 291(1), pages 60-70.
    3. Hansen, Alex & Jensen, Mogens H & Sneppen, Kim & Zocchi, Giovanni, 2000. "Proteins top–down: a statistical mechanics approach," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 288(1), pages 21-30.
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    Cited by:

    1. Bakk, Audun, 2002. "Heat capacities of solid state proteins: implications for protein stability in solution," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 313(3), pages 540-548.

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    2. Bakk, Audun & Hansen, Alex & Sneppen, Kim, 2001. "Protein model exhibiting three folding transitions," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 291(1), pages 60-70.

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