Protein-protein interactions in dilute to concentrated solutions: α-chymotrypsinogen in acidic conditions.

ABSTRACT: Protein-protein interactions were investigated for α-chymotrypsinogen by static and dynamic light scattering (SLS and DLS, respectively), as well as small-angle neutron scattering (SANS), as a function of protein and salt concentration at acidic conditions. Net protein-protein interactions were probed via the Kirkwood-Buff integral G22 and the static structure factor S(q) from SLS and SANS data. G22 was obtained by regressing the Rayleigh ratio versus protein concentration with a local Taylor series approach, which does not require one to assume the underlying form or nature of intermolecular interactions. In addition, G22 and S(q) were further analyzed by traditional methods involving fits to effective interaction potentials. Although the fitted model parameters were not always physically

SUBMITTER: Blanco MA 

PROVIDER: S-EPMC4051245 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature