TY  - JOUR
AU  - Ameseder, Felix
AU  - Radulescu, Aurel
AU  - Holderer, Olaf
AU  - Falus, Peter
AU  - Richter, Dieter
AU  - Stadler, Andreas M.
TI  - Relevance of Internal Friction and Structural Constraints for the Dynamics of Denatured Bovine Serum Albumin
JO  - The journal of physical chemistry letters
VL  - 9
IS  - 10
SN  - 1948-7185
CY  - Washington, DC
PB  - ACS
M1  - FZJ-2018-03243
SP  - 2469 - 2473
PY  - 2018
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:29688725
UR  - <Go to ISI:>//WOS:000432756600004
DO  - DOI:10.1021/acs.jpclett.8b00825
UR  - https://juser.fz-juelich.de/record/847922
ER  -