The sample parameters are: 30 μLÁmin
À1 flow rate, 180 s contact time, and 120 s dissociation
time. The regeneration parameters are: 30 μLÁmin
À1
flow rate and 60 s contact time, wash in running
buffer.
Protocol adapted by Manuela Zoonens from Zoonens et al. (2014)
References
Ansar, S.M., Haputhanthri, R., Edmonds, B., Liu, D., Yu, L., Sygula, A., Zhang, D. (2011) Determination of the binding
affinity, packing, and conformation of thiolate and thione ligands on gold nanoparticles. J. Phys. Chem. C
115:653–660.
Arora, A., Abildgaard, F., Bushweller, J.H., Tamm, L.K. (2001) Structure of outer membrane protein A transmembrane
domain by NMR spectroscopy. Nat. Struct. Biol. 8:334–338.
Bailey, K., Bally, M., Leifert, W., Vörös, J., McMurchie, T. (2009) G protein-coupled receptor array technologies: Site
directed immobilisation of liposomes containing the H 1 -histamine or M 2 -muscarinic receptors. Proteomics
9:2052–2063.
Bain, C.D., Biebuyck, H.A., Whitesides, G.M. (1989a) Comparison of self-assembled monolayers on gold: Coadsorption
of thiols and disulfides. Langmuir 5:723–727.
Bain, C.D., Evall, J., Whitesides, G.M. (1989b) Formation of monolayers by the coadsorption of thiols on gold: Variation
in the head group, tail group, and solvent. J. Am. Chem. Soc. 111:7155–7164.
Bano, F., Fruk, L., Sanavio, B., Glettenberg, M., Casalis, L., Niemeyer, C.M., Scoles, G. (2009) Toward multiprotein
nanoarrays using nanografting and DNA-directed immobilization of proteins. Nano Lett. 9:2614–2618.
Basit, H., Sharma, S., Van der Heyden, A., Gondran, C., Breyton, C., Dumy, P., Winnik, F.M., Labbé, P. (2012)
Amphipol-mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein
pb5. Chem. Commun. 48:6037–6039.
Bellot, G., McClintock, M.A., Chou, J.J., Shih, W.M. (2013) DNA nanotubes for NMR structure determination of
membrane proteins. Nat. Protoc. 8:755–770.
Berry, E.A., Guergova-Kuras, M., Huang, L.-S., Crofts, A.R. (2000) Structure and function of cytochrome bc 1
complexes. Annu. Rev. Biochem. 69:1005–1075.
Beulen, M.W.J., Huisman, B.-H., van der Heijden, P.A., van Veggel, F.C.J.M., Simons, M.G., Biemond, E.M.E.F., de
Lange, P.J., Reinhoudt, D.N. (1996) Evidence for nondestructive adsorption of dialkyl sulfides on gold. Langmuir
12:6170–6172.
Bidan, G., Billon, M., Galasso, K., Livache, T., Mathis, C., Roget, A., Torres-Rodriguez, L.M., Vieil, E. (2000)
Electropolymerization as a versatile route for immobilizing biological species onto surfaces – Application to DNA
biochips. Appl. Biochem. Biotechnol. 89:183–193.
Bieri, C., Ernst, O.P., Heyse, S., Hofmann, K.P., Vogel, H. (1999) Micropatterned immobilization of a G protein-coupled
receptor and direct detection of G protein activation. Nat. Biotech. 17:1105–1108.
Binz, H.K., Stumpp, M.T., Forrer, P., Amstutz, P., Plückthun, A. (2003) Designing repeat proteins: well-expressed,
soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol.
332:489–503.
Blanchard, S.G., Quast, U., Reed, K., Lee, T., Schimerlik, M.I., Vandlen, R., Claudio, T., Strader, C.D., Moore, H.P.,
Raftery, M.A. (1979) Interaction of
125
I-α-bungarotoxin with acetylcholine receptor from Torpedo californica.
Biochemistry 18:1875–1883.
Block, H., Maertens, B., Spriestersbach, A., Brinker, N., Kubicek, J., Fabis, R., Labahn, J., Schäfer, F. (2009)
Immobilized-metal affinity chromatography (IMAC): a review. Methods Enzymol. 463:439–473.
Boersma, Y.L., Plückthun, A. (2011) DARPins and other repeat protein scaffolds: advances in engineering and
applications. Curr. Opin. Biotechnol. 22:849–857.
Catoire, L.J., Damian, M., Giusti, F., Martin, A., van Heijenoort, C., Popot, J.-L., Guittet, E., Banères, J.-L. (2010)
Structure of a GPCR ligand in its receptor-bound state: leukotriene B 4 adopts a highly constrained conformation when
associated to human BLT2. J. Am. Chem. Soc. 132:9049–9057.
Champeil, P., Menguy, T., Tribet, C., Popot, J.-L., le Maire, M. (2000) Interaction of amphipols with the sarcoplasmic
reticulum Ca
2+ -ATPase. J. Biol. Chem. 275:18623–18637.
Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K.L., Popot, J.-L.
(2009) The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.
Proc. Natl. Acad. Sci. USA 106:405–410.
Christman, K.L., Enriquez-Rios, V.D., Maynard, H.D. (2006a) Nanopatterning proteins and peptides. Soft Matter
2:928–939.
References
619
À1 flow rate, 180 s contact time, and 120 s dissociation
time. The regeneration parameters are: 30 μLÁmin
À1
flow rate and 60 s contact time, wash in running
buffer.
Protocol adapted by Manuela Zoonens from Zoonens et al. (2014)
References
Ansar, S.M., Haputhanthri, R., Edmonds, B., Liu, D., Yu, L., Sygula, A., Zhang, D. (2011) Determination of the binding
affinity, packing, and conformation of thiolate and thione ligands on gold nanoparticles. J. Phys. Chem. C
115:653–660.
Arora, A., Abildgaard, F., Bushweller, J.H., Tamm, L.K. (2001) Structure of outer membrane protein A transmembrane
domain by NMR spectroscopy. Nat. Struct. Biol. 8:334–338.
Bailey, K., Bally, M., Leifert, W., Vörös, J., McMurchie, T. (2009) G protein-coupled receptor array technologies: Site
directed immobilisation of liposomes containing the H 1 -histamine or M 2 -muscarinic receptors. Proteomics
9:2052–2063.
Bain, C.D., Biebuyck, H.A., Whitesides, G.M. (1989a) Comparison of self-assembled monolayers on gold: Coadsorption
of thiols and disulfides. Langmuir 5:723–727.
Bain, C.D., Evall, J., Whitesides, G.M. (1989b) Formation of monolayers by the coadsorption of thiols on gold: Variation
in the head group, tail group, and solvent. J. Am. Chem. Soc. 111:7155–7164.
Bano, F., Fruk, L., Sanavio, B., Glettenberg, M., Casalis, L., Niemeyer, C.M., Scoles, G. (2009) Toward multiprotein
nanoarrays using nanografting and DNA-directed immobilization of proteins. Nano Lett. 9:2614–2618.
Basit, H., Sharma, S., Van der Heyden, A., Gondran, C., Breyton, C., Dumy, P., Winnik, F.M., Labbé, P. (2012)
Amphipol-mediated surface immobilization of FhuA: a platform for label-free detection of the bacteriophage protein
pb5. Chem. Commun. 48:6037–6039.
Bellot, G., McClintock, M.A., Chou, J.J., Shih, W.M. (2013) DNA nanotubes for NMR structure determination of
membrane proteins. Nat. Protoc. 8:755–770.
Berry, E.A., Guergova-Kuras, M., Huang, L.-S., Crofts, A.R. (2000) Structure and function of cytochrome bc 1
complexes. Annu. Rev. Biochem. 69:1005–1075.
Beulen, M.W.J., Huisman, B.-H., van der Heijden, P.A., van Veggel, F.C.J.M., Simons, M.G., Biemond, E.M.E.F., de
Lange, P.J., Reinhoudt, D.N. (1996) Evidence for nondestructive adsorption of dialkyl sulfides on gold. Langmuir
12:6170–6172.
Bidan, G., Billon, M., Galasso, K., Livache, T., Mathis, C., Roget, A., Torres-Rodriguez, L.M., Vieil, E. (2000)
Electropolymerization as a versatile route for immobilizing biological species onto surfaces – Application to DNA
biochips. Appl. Biochem. Biotechnol. 89:183–193.
Bieri, C., Ernst, O.P., Heyse, S., Hofmann, K.P., Vogel, H. (1999) Micropatterned immobilization of a G protein-coupled
receptor and direct detection of G protein activation. Nat. Biotech. 17:1105–1108.
Binz, H.K., Stumpp, M.T., Forrer, P., Amstutz, P., Plückthun, A. (2003) Designing repeat proteins: well-expressed,
soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol.
332:489–503.
Blanchard, S.G., Quast, U., Reed, K., Lee, T., Schimerlik, M.I., Vandlen, R., Claudio, T., Strader, C.D., Moore, H.P.,
Raftery, M.A. (1979) Interaction of
125
I-α-bungarotoxin with acetylcholine receptor from Torpedo californica.
Biochemistry 18:1875–1883.
Block, H., Maertens, B., Spriestersbach, A., Brinker, N., Kubicek, J., Fabis, R., Labahn, J., Schäfer, F. (2009)
Immobilized-metal affinity chromatography (IMAC): a review. Methods Enzymol. 463:439–473.
Boersma, Y.L., Plückthun, A. (2011) DARPins and other repeat protein scaffolds: advances in engineering and
applications. Curr. Opin. Biotechnol. 22:849–857.
Catoire, L.J., Damian, M., Giusti, F., Martin, A., van Heijenoort, C., Popot, J.-L., Guittet, E., Banères, J.-L. (2010)
Structure of a GPCR ligand in its receptor-bound state: leukotriene B 4 adopts a highly constrained conformation when
associated to human BLT2. J. Am. Chem. Soc. 132:9049–9057.
Champeil, P., Menguy, T., Tribet, C., Popot, J.-L., le Maire, M. (2000) Interaction of amphipols with the sarcoplasmic
reticulum Ca
2+ -ATPase. J. Biol. Chem. 275:18623–18637.
Charvolin, D., Perez, J.-B., Rouvière, F., Giusti, F., Bazzacco, P., Abdine, A., Rappaport, F., Martinez, K.L., Popot, J.-L.
(2009) The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports.
Proc. Natl. Acad. Sci. USA 106:405–410.
Christman, K.L., Enriquez-Rios, V.D., Maynard, H.D. (2006a) Nanopatterning proteins and peptides. Soft Matter
2:928–939.
References
619