Experimental Measurement of the Thermodynamics Underlying the Surface-Induced Structural Changes of Nucleic Acids and Proteins

Abstract

Proteins frequently unfold on and adhere to artificial surfaces, but rarely do so on biological surfaces such as cell membranes. While a number of man-made materials on which biomolecules generally retain their function have been reported, the physics of why they do so on these few materials and not on others are not fully understood.Thus motivated, our lab recently developed an approach to quantitatively measure the thermodynamics of interactions between nucleic acids and artificial surfaces. Moving beyond our initial DNA testbed, we have now adapted this technique to probe the folding thermodynamics of surface-attached proteins. Comparison to equivalent measurements in bulk solution allows us to resolve the surface interaction energetics. The goal is to design protein/surface pairs supporting fully reversible refolding, for use in research and biotechnology.