Localised contacts lead to nanosecond hinge motions in dimeric bovine serum albumin

Abstract

Domain motions in proteins are crucial for biological function.

Temperature and salt controlled tuning of protein clusters

“…Thus, we measured the salt series at j h = 0.18, 0.33, and 0.46. While a distribution of monomers and dimers of BSA in solution has been observed at low protein concentrations in the absence of salt, 34,35 at the high protein concentrations investigated here, the solutions free from trivalent salts agree with the picture of an effectively monomeric system, 36 corroborated by the onset of self-buffering.…”

“…3), illustrating growing clusters with rising temperature and salt concentration. solution has been observed at low protein concentrations in the absence of salt, 34,35 at the high protein concentrations investigated here, the salt-free solutions agree with the picture of an effectively monomeric system. [36][37][38] Previously, 32 cluster formation of BSA in D 2 O was observed upon approaching c* for YCl 3 at constant temperature (295 K), using incoherent QENS.…”

Reversible Dimerization of Human Serum Albumin

“…According to the distance between the two radicals in al-bumin molecules~2 nm we can propose the interaction of Domain I, precisely subdomains IA and IB, of two HSA molecules (Cys-34 is in subdomain IA). The close structure of the dimer was proposed and published for bovine serum albumin [30]. However, BSA has two cysteines at residues 34 and 513 that can form intermolecular disulfide bonds connecting two BSA monomers.…”

“…However, BSA has two cysteines at residues 34 and 513 that can form intermolecular disulfide bonds connecting two BSA monomers. For BSA structure cysteine at residue 513 could form a molecular hinge between the BSA monomers and stabilize the BSA dimer [30]. The disulfide bridge in the BSA dimer defines a rotational axis that is visible as well in the normal mode displacement patters.…”

Separation of the inelastic and elastic scattering in time-of-flight mode on the pinhole small-angle neutron scattering diffractometer KWS-2

“…Being interested in the effect of the inelastic scattering on the background, we focused only on measurements above the Q value of the correlation maximum. An interesting feature of the highly structured BSA (due to a high content of helices) is highlighted in the high-Q region: the shoulder at 0.15 Å À1 arising from the twofold structure of the BSA monomer (Ameseder et al, 2019). When only the elastic region of the TOF spectrum is considered for data analysis, after the correction for the solvent scattering is applied, a lower background level is obtained at high Q compared with the case where the whole spectrum is analysed [Fig.…”