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Denaturing and refolding of protein molecules on surfaces
Author(s) -
Holtz Bryan,
Wang Yini,
Zhu XiaoYang,
Guo Athena
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700053
Subject(s) - chemistry , molecule , protein folding , biophysics , folding (dsp implementation) , biosensor , protein microarray , fluorescence , surface modification , surface protein , chemical modification , nanotechnology , biochemistry , dna microarray , materials science , biology , organic chemistry , gene , gene expression , physics , quantum mechanics , virology , electrical engineering , engineering
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.