Polymeric Aspects of Protein Folding: a Brief Overview
Document Type
Article
Publication Date
2003
Keywords
Protein Folding, Equilibrium Structures, Polymer Globules, Pre-molten Globule, Squeezed Coils, Globular Proteins, Polymer Homologues
Digital Object Identifier (DOI)
http://dx.doi.org/10.2174/0929866033478988
Abstract
Regardless of the differences in primary amino acid sequences, protein molecules in a number of conformational states behave as polymer homologues, allowing speculations as to the volume interactions being a driving force in formation of equilibrium structures. For instance, both native and molten globules exhibit key features of polymer globules, where the fluctuations of the molecular density are expected to be much less than the molecular density itself. Protein molecules in the compact denatured (pre-molten globule) states possess properties of squeezed coils. In fact, even high concentrations of strong denaturants (e.g., urea and GdmCl) more likely constitute bad solvents for protein chains. Thus, globular proteins are probably never random coils without positional correlations and biological polypeptide chains represent the macromolecular coils below a critical point even under harsh denaturing conditions. Several implications of these findings to protein folding are discussed.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Protein & Peptide Letters, v. 10, issue 3, p. 239-245
Scholar Commons Citation
Tcherkasskaya, Olga and Uversky, Vladimir N., "Polymeric Aspects of Protein Folding: a Brief Overview" (2003). Molecular Medicine Faculty Publications. 709.
https://digitalcommons.usf.edu/mme_facpub/709
