Proteomics. 2007 Jun;7(11):1771-4.

Denaturing and refolding of protein molecules on surfaces.

Source

MicroSurfaces, Minneapolis, MN 55455, USA.

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.

PMID:: 17476712; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

Publication Types

Research Support, N.I.H., Extramural

MeSH Terms

Substances

Green Fluorescent Proteins

Grant Support

2R44RR017130/RR/NCRR NIH HHS/United States

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