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000847922 1001_ $$0P:(DE-Juel1)166208$$aAmeseder, Felix$$b0$$ufzj
000847922 245__ $$aRelevance of Internal Friction and Structural Constraints for the Dynamics of Denatured Bovine Serum Albumin
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000847922 520__ $$aA 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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000847922 65017 $$0V:(DE-MLZ)GC-1602-2016$$2V:(DE-HGF)$$aPolymers, Soft Nano Particles and  Proteins$$x0
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000847922 7001_ $$0P:(DE-Juel1)130905$$aRadulescu, Aurel$$b1$$ufzj
000847922 7001_ $$0P:(DE-Juel1)130718$$aHolderer, Olaf$$b2$$ufzj
000847922 7001_ $$0P:(DE-HGF)0$$aFalus, Peter$$b3
000847922 7001_ $$0P:(DE-Juel1)130917$$aRichter, Dieter$$b4$$ufzj
000847922 7001_ $$0P:(DE-Juel1)140278$$aStadler, Andreas M.$$b5$$eCorresponding author
000847922 773__ $$0PERI:(DE-600)2522838-9$$a10.1021/acs.jpclett.8b00825$$gVol. 9, no. 10, p. 2469 - 2473$$n10$$p2469 - 2473$$tThe @journal of physical chemistry letters$$v9$$x1948-7185$$y2018
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