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| 001 | 847922 | ||
| 005 | 20210129233857.0 | ||
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| 100 | 1 | _ | |a Ameseder, Felix |0 P:(DE-Juel1)166208 |b 0 |u fzj |
| 245 | _ | _ | |a Relevance of Internal Friction and Structural Constraints for the Dynamics of Denatured Bovine Serum Albumin |
| 260 | _ | _ | |a Washington, DC |c 2018 |b ACS |
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| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Stadler, Andreas M. |0 P:(DE-Juel1)140278 |b 5 |e Corresponding author |
| 773 | _ | _ | |a 10.1021/acs.jpclett.8b00825 |g Vol. 9, no. 10, p. 2469 - 2473 |0 PERI:(DE-600)2522838-9 |n 10 |p 2469 - 2473 |t The @journal of physical chemistry letters |v 9 |y 2018 |x 1948-7185 |
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