title: A generalized strategy for immobilizing uniformly oriented membrane proteins at solid interfaces.
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.
authors: National Institute of Standards and Technology (NIST) Center for Neutron Research, Gaithersburg, MD 20899, USA. amit.vaish@nist.gov
authors: Amit
authors: A
authors: Vaish
authors: Vitalii
authors: V
authors: Silin
authors: Marlon L
authors: ML
authors: Walker
authors: Kristen L
authors: KL
authors: Steffens
authors: Susan
authors: S
authors: Krueger
authors: Alexei A
authors: AA
authors: Yeliseev
authors: Klaus
authors: K
authors: Gawrisch
authors: David J
authors: DJ
authors: Vanderah
mesh_terms: D019855:Ethylene Glycol / Q000737:chemistry; D006046:Gold / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D009571:Nitrilotriacetic Acid / Q000737:chemistry; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry*; D012995:Solubility; D013438:Sulfhydryl Compounds / Q000737:chemistry; D013499:Surface Properties; D014867:Water / Q000737:chemistry
chemical_list: D043562:Receptors, G-Protein-Coupled; D013438:Sulfhydryl Compounds; D014867:Water; D006046:Gold; D019855:Ethylene Glycol; D009571:Nitrilotriacetic Acid