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Biophys J. 2008 Jul;95(2):503-9. doi: 10.1529/biophysj.107.121855. Epub 2008 May 9.

Toward resolution of ambiguity for the unfolded state.

Author information

  • Department of Chemical and Materials Engineering, University of Cincinnati, Cincinnati, Ohio, USA. beaucag@uc.edu

Abstract

The unfolded states in proteins and nucleic acids remain weakly understood despite their importance in folding processes; misfolding diseases (Parkinson's and Alzheimer's); natively unfolded proteins (as many as 30% of eukaryotic proteins, according to Fink); and the study of ribozymes. Research has been hindered by the inability to quantify the residual (native) structure present in an unfolded protein or nucleic acid. Here, a scaling model is proposed to quantify the molar degree of folding and the unfolded state. The model takes a global view of protein structure and can be applied to a number of analytic methods and to simulations. Three examples are given of application to small-angle scattering from pressure-induced unfolding of SNase, from acid-unfolded cytochrome c, and from folding of Azoarcus ribozyme. These examples quantitatively show three characteristic unfolded states for proteins, the statistical nature of a protein folding pathway, and the relationship between extent of folding and chain size during folding for charge-driven folding in RNA.

PMID:
18469075
[PubMed - indexed for MEDLINE]
PMCID:
PMC2440439
Free PMC Article

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