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Protein folding is one of the most mysterious problems of the modern science, since the early sixties. This web-page has the purpose to shed light on some aspects of the folding kinetics, methods often used in the investigation of folding, and the general aspects of in vitro and in vivo protein folding. Although the protein folding has a wide literature, nowadays experiments on RNA-folding has chance for great improvement as well (Thirumalai & Woodson, 1996). In this web-page you can read about the following topics:

  • Introduction
  • General considerations on protein structure and folding
  • The so-called Levinthal paradox
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  • Molecular forces, determining protein folding
  • Hydrophobic forces
  • van der Waals interactions
  • Hydrogen bonds
  • Electrostatic interactions
  • Covalent bonding
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  • Methods in investigating protein folding
  • Anfinsen's experiment on ribonuclease folding
  • Gel-electrophoresis (urea-gradient gel-electrophoresis)
  • NMR (amide proton exchange)
  • Circular Dichroism (CD)
  • Other methods
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  • Considerations on the kinetics of protein folding
  • Native and denatured conformations
  • Theories on folding
  • The hydrophobic collapse model
  • The nucleation theory
  • The viscosity-collision model
  • Energy landscape models
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  • Protein folding in vivo
  • Protein folding in vitro
  • Protein folding in vivo, the role of molecular chaperones (if you would like to read more on chaperones, you can can browse through this page)
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  • References
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    If you have any comments about this web-page, please contact Attila Rácz.