Home > Publications database > Relevance of Internal Friction and Structural Constraints for the Dynamics of Denatured Bovine Serum Albumin |
Journal Article | FZJ-2018-03243 |
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2018
ACS
Washington, DC
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Please use a persistent id in citations: doi:10.1021/acs.jpclett.8b00825
Abstract: A general property of disordered proteins is their structural expansion that results in a high molecular flexibility. The structure and dynamics of bovine serum albumin (BSA) denatured by guanidinium hydrochloride (GndCl) were investigated using small-angle neutron scattering (SANS) and neutron spin–echo spectroscopy (NSE). SANS experiments demonstrated the relevance of intrachain interactions for structural expansion. Using NSE experiments, we observed a high internal flexibility of denatured BSA in addition to center-of-mass diffusion detected by dynamic light scattering. Internal motions measured by NSE were described using concepts based on polymer theory. The contribution of residue-solvent friction was accounted for using the Zimm model including internal friction (ZIF). Disulfide bonds forming loops of amino acids of the peptide backbone have a major impact on internal dynamics that can be interpreted with a reduced set of Zimm modes.
Keyword(s): Polymers, Soft Nano Particles and Proteins (1st) ; Soft Condensed Matter (2nd) ; Biology (2nd)
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