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• W2317464557 startingPage "12059" @default.
• W2317464557 abstract "Similarities in global properties of homopolymers and unfolded proteins provide approaches to mechanistic description of protein folding. Here, hydrodynamic properties and relaxation rates of the unfolded state of carbonmonoxide-liganded cytochrome c (cyt-CO) have been measured using nuclear magnetic resonance and laser photolysis methods. Hydrodynamic radius of the unfolded chain gradually increases as the solvent turns increasingly better, consistent with theory. Curiously, however, the rate of intrachain contact formation also increases with an increasing denaturant concentration, which, by Szabo, Schulten, and Schulten theory for the rate of intramolecular contact formation in a Gaussian polymer, indicates growing intramolecular diffusion. It is argued that diminishing nonbonded atom interactions with increasing denaturant reduces internal friction and, thus, increases the rate of polypeptide relaxation. Qualitative scaling of the extent of unfolding with nonbonded repulsions allows for description of internal friction by a phenomenological model. The degree of nonbonded atom interactions largely determines the extent of internal friction." @default.
• W2317464557 created "2016-06-24" @default.
• W2317464557 creator A5041440429 @default.
• W2317464557 creator A5069186079 @default.
• W2317464557 creator A5078233653 @default.
• W2317464557 date "2013-09-30" @default.
• W2317464557 modified "2023-09-24" @default.
• W2317464557 title "Expansion and Internal Friction in Unfolded Protein Chain" @default.
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• W2317464557 doi "https://doi.org/10.1021/jp408718c" @default.
• W2317464557 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24044733" @default.
• W2317464557 hasPublicationYear "2013" @default.
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