Denaturing and refolding of protein molecules on surfaces |
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Authors: | Holtz Bryan Wang Yini Zhu Xiao-Yang Guo Athena |
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Institution: | MicroSurfaces, Minneapolis, MN 55455, USA. |
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Abstract: | 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--NH(2) 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. |
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Keywords: | Biochip Protein immobilization ProteoChip Surface modification |
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