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Proteins top–down: a statistical mechanics approach

Author

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  • Hansen, Alex
  • Jensen, Mogens H
  • Sneppen, Kim
  • Zocchi, Giovanni

Abstract

Biopolymers have many fascinating properties coming from a competition between universal features, well known in the physics of synthetic polymers, and specific elements which are crucial for the biological function of these molecules. Proteins are an example of this richness: proteins are heteropolymers consisting of hydrophobic and hydrophilic segments, and carry charges of both signs along the backbone. Simple models of such heteropolymers have been studied in connection with the folding and evolution of proteins. However, these models can only give a limited understanding of real proteins, and elements specific to proteins must be included. Our approach to this problem has been to construct a model of the specific self-interactions of proteins by defining a unique folding pathway. This model reproduces the thermodynamic properties of proteins.

Suggested Citation

  • 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.
    • Handle: RePEc:eee:phsmap:v:288:y:2000:i:1:p:21-30
    DOI: 10.1016/S0378-4371(00)00412-X
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    Cited by:

    1. 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.

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