%0 Journal Article
%A Ameseder, Felix
%A Radulescu, Aurel
%A Holderer, Olaf
%A Falus, Peter
%A Richter, Dieter
%A Stadler, Andreas M.
%T Relevance of Internal Friction and Structural Constraints for the Dynamics of Denatured Bovine Serum Albumin
%J The journal of physical chemistry letters
%V 9
%N 10
%@ 1948-7185
%C Washington, DC
%I ACS
%M FZJ-2018-03243
%P 2469 - 2473
%D 2018
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:29688725
%U <Go to ISI:>//WOS:000432756600004
%R 10.1021/acs.jpclett.8b00825
%U https://juser.fz-juelich.de/record/847922