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Protein bioconjugate

Hering, V. R., Gibson, G., Schumacher, R. I., Faljoni-Alario, A. and Politi, M. J. (2007). Energy transfer between CdSe/ZnS core/shell quantum dots and fluorescent proteins. Bioconjug. Chem. 18, 1705-8. [Pg.525]

Gaertner, H.F., and Offord, R.E. (1996) Site-specific attachment of functionalized poly(ethylene glycol) to the amino terminus of proteins. Bioconjugate. Chem. 7, 38-44. [Pg.1064]

Medintz, I L., Konnert, J.H., Clapp, A.R., Stanish, I., Twigg, M.E., Mattoussi, H., Mauro, J.M., and Deschamps, J.R. (2004) A fluorescence resonance energy transfer-derived structure of a quantum dot-protein bioconjugate nanoassembly. Proc. Natl. Acad. Sci. USA 101(26), 9612-9617. [Pg.1093]

Miron, T., and Wilchek, M. (1993) A simplified method for the preparation of succinimidyl carbonate polyethylene glycol for coupling to proteins. Bioconjugate Ghent. 4, 568-569. [Pg.1095]

Singh, P. (1998) Terminal groups in starburst dendrimers Activation and reactions with proteins. Bioconjugate Chem. 9, 54-63. [Pg.1114]

Whetstone, P.A., Butlin, N.G., Corneillie, T.M., and Meares, C.F. (2003) Element-coded affinity tags for peptides and proteins. Bioconjugate Chem. 15, 3-6. [Pg.1127]

Medintz IL, Goldman ER, Lassman ME, Mauro JM (2003) A fluorescence resonance energy transfer sensor based on maltose binding protein. Bioconjug Chem 14 909-918... [Pg.187]

NANOSCALE SENSING ASSEMBLIES USING QUANTUM DOT-PROTEIN BIOCONJUGATES... [Pg.285]

Naval Research Laboratory 4555 Overlook Avenue SW Washington, DC, 20375 Chemistry Division/6112 Ph 202.404.3337 (Greg E. Collins) Greg.collins nrl.navy.mil Optical Sciences Division/5611 Ph 202.767.9473 (Hedi Mattoussi) hedimat ccs.nrl.navy, mil www.nrl.navy.mil Laboratory on a chip for explosive detection, quantum dot-protein bioconjugates, biosensors, UAV radar, and much more in basic research. [Pg.317]

Chapter 14, Nanoscale Sensing Assemblies Using Quantum Dot-Protein Bioconjugates, also describes a kind of sensor technology in that ultra-small size, but one using a very different approach. [Pg.390]

Finally, a model protein bioconjugate 52 was prepared with the reactive fluorophore 50 and bovine serum albumin (BSA). The conjugate was identified spectrophotometrically and its steady state fluorescence emission spectra... [Pg.135]

Cooke, S.P., R.B. Pedley, R. Boden, R.H. Begent, and K.A. Chester, In vivo tumor delivery of a recombinant single-chain Fvr.tumor necrosis factor a fusion protein. Bioconjug Chem, 2002.13(1) 7-15. [Pg.380]

Backer, M.V. Patel, V., Jehning, B and Backer, J. M. (2006) Self-assembled dock and lock system for linking payloads to targeting proteins. Bioconjugate Chem. 17, 912-919. [Pg.293]

Human-type protein analog consisting of natural amino acid Human-type protein analog containing nonnatural amino acid Bioconjugate of human-type protein and other protein Bioconjugate of human-type protein and organic linker... [Pg.101]

Johnson, C. P., Jensen, I. E., Prakasam, A., Vijayendran, R., Leckband, D., Vijayendran, R. a., Leckband, D. E. (2003). Engineered protein a for the orientational control of immobilized proteins. A quantitative assessment of heterogeneity for surface-immobilized proteins. Bioconjug. Chem. 14, 974—978. [Pg.154]

Schellenberger EA, Sosnovik D, Weissleder R, Josephson L. Magneto/optical annexin V, a multimodal protein. Bioconjug. Chem. 2004 15 1062-1067. [Pg.1096]

These considerations form the basis for the numerous techniques that are now available for the chemical modification of proteins. The sections that follow will examine these techniques and the reactive principles by which they function. A section describing reactions that display orthogonal reactivity to native protein functional groups has also been included because of the growing importance of these reactions as tools to label proteins in complex mixtures. Because it is not practical to summarize all protein bioconjugation methods here, this information instead is intended to serve as an introduction to the concepts that drive the development of these reactions. Several additional reviews and books on protein modification have been listed in the Further Reading section. [Pg.1609]

Ni, J., Singh, S., Wang, L. X. (2003). Synthesis of maleimide-activated carbohydrates as chemoselective tags for site-specific glycosylation of peptides and proteins. Bioconjug. Chem., 14, 232-238. [Pg.222]

Table 2.3 Applications of carbon nanotube-protein bioconjugates. Table 2.3 Applications of carbon nanotube-protein bioconjugates.
Table 2.6 Applications of carbon nanotube-nanoparticle-protein bioconjugates. Table 2.6 Applications of carbon nanotube-nanoparticle-protein bioconjugates.

See other pages where Protein bioconjugate is mentioned: [Pg.137]    [Pg.552]    [Pg.395]    [Pg.401]    [Pg.286]    [Pg.287]    [Pg.287]    [Pg.383]    [Pg.383]    [Pg.18]    [Pg.276]    [Pg.303]    [Pg.1608]    [Pg.1620]    [Pg.54]    [Pg.593]    [Pg.593]    [Pg.595]   
See also in sourсe #XX -- [ Pg.135 ]




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