Abstract
We have developed a method based on self-assembly of thiols on Au substrates to immobilize membrane proteins at interfaces. Using water soluble nitrilotriacetic acid (NTA)-terminated oligo(ethylene glycol) thiols, a histidine-tagged G protein-coupled membrane receptor (GPCR) was captured in a defined orientation with little nonspecific binding.
Publication types
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Research Support, American Recovery and Reinvestment Act
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Research Support, N.I.H., Intramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Ethylene Glycol / chemistry
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Gold / chemistry
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Models, Molecular
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Molecular Structure
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Nitrilotriacetic Acid / chemistry
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Receptors, G-Protein-Coupled / chemistry*
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Solubility
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Sulfhydryl Compounds / chemistry
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Surface Properties
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Water / chemistry
Substances
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Receptors, G-Protein-Coupled
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Sulfhydryl Compounds
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Water
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Gold
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Ethylene Glycol
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Nitrilotriacetic Acid