A mechanistic examination of salting out in protein-polymer membrane interactions.

ABSTRACT: Developing a mechanistic understanding of protein dynamics and conformational changes at polymer interfaces is critical for a range of processes including industrial protein separations. Salting out is one example of a procedure that is ubiquitous in protein separations yet is optimized empirically because there is no mechanistic description of the underlying interactions that would allow predictive modeling. Here, we investigate peak narrowing in a model transferrin-nylon system under salting out conditions using a combination of single-molecule tracking and ensemble separations. Distinct surface transport modes and protein conformational changes at the negatively charged nylon interface are quantified as a function of salt concentration. Single-molecule kinetics relate macroscale improve

SUBMITTER: Moringo NA 

PROVIDER: S-EPMC6859367 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature