Quantitative measurements of protein-surface interaction thermodynamics.

ABSTRACT: Whereas proteins generally remain stable upon interaction with biological surfaces, they frequently unfold on and adhere to artificial surfaces. Understanding the physicochemical origins of this discrepancy would facilitate development of protein-based sensors and other technologies that require surfaces that do not compromise protein structure and function. To date, however, only a small number of such artificial surfaces have been reported, and the physics of why these surfaces support functional biomolecules while others do not has not been established. Thus motivated, we have developed an electrochemical approach to determining the folding free energy of proteins site-specifically attached to chemically well-defined, macroscopic surfaces. Comparison with the folding free energies seen

SUBMITTER: Kurnik M 

PROVIDER: S-EPMC6099891 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature