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Denaturing and refolding of protein molecules on surfaces

Keeping protein molecules in the active state on a solid surface is essential to protein microarrays and other protein‐based biosensors. Here, we show that the 2‐D chemical environment controls the refolding of the denatured green fluorescent proteins tethered to solid surfaces. Refolding occurs readily on the repulsive PEG functionalized surface but is inhibited on the attractive –NH2 functionalized surface. This result shows the critical importance of the 2‐D chemical environment in the maintenance and revival of protein activity on surfaces and opens the door to designing 2‐D molecular chaperones for protein folding.