Labelling of proteins

Moleeular biology eloning expression isotope labeling of protein target... 

G. Site-specific labeling of proteins with a rigid lanthanide-binding tag. ChemEioChem 2006, 7,1599-1504. 

In vitro labeling of proteins using isotope-coded affinity tags... 

With advances in multidimensional NMR technology and the development of methods for uniform labeling of proteins with 15N and 13C, direct NMR studies on unfolded states of full-length proteins, rather than protein fragments, became possible. These studies were aided by the advent of high-field NMR spectrometers, which provide the necessary dispersion and sensitivity. High sensitivity is a critical factor in the study of unfolded and partly folded proteins, since NMR experiments must often be performed at very low concentrations to prevent aggregation. 

Craig, D.B., Dovichi, NJ. (1998). Multiple labeling of proteins Anal. Chem. 70, 2493-2494. 

The strategy described has been demonstrated by the in vivo labeling of proteins in both bacterial and mammalian systems thereby making it potentially useful for future bioimaging and proteomics applications [163],... 

Chattopadhaya S, Srinivasan R, Yeo DSY et al (2009) Site-specific covalent labeling of proteins inside live cells using small molecule probes. Bioorg Med Chem 17 981-989... 

Soh, N. (2008). Selective chemical labeling of proteins with small fluorescent molecules based on metal-chelation methodology. Sensors 8, 1004-24. 

Hubbell, W.L., Gross, A., Langen, R., and Lietzow, M.A. 1998. Recent advances in site-directed spin labeling of proteins. Current Opinion in Structural Biology 8 649-656. 

Bolton, A.E., and Hunter, W.M. (1973) The labeling of proteins to high specific radioactivities by conjugation to a 1251-containing acylating agent. Biochem. J. 133, 529-539. 

Kurzchalia, T.V., Wiedmann, M., Breter, H., Zimmermann, W., Bauschke, E., and Rapoport, T.A. (1988) tRNA-mediated labeling of proteins with biotin. A nonradioactive method for the detection of cell-free translation products. Eur. J. Biochem. 172, 663-668. 

Rhodes, B.A. (1991) Direct labeling of proteins with 99mTc. Nucl. Med. Biol. 18, 667-676. 

Thevenin, B., Shahrokh, Z., Williard, R., Fujimoto, E., Ikemoto, N., and Shohet, S. (1991) A novel reagent for functionally-directed site-specific fluorescent labeling of proteins, Abstract. Biophys. J. 59, Tu-Pos 476, p. 358a. 

Varenne, A., Salmain, M., Brisson, C., and Jaouen, G. (1992) Transition metal carbonyl labeling of proteins. A novel approach to a solid-phase two-site immunoassay using Fourier transform infrared spectroscopy. Bioconjugate Chem. 3, 471-476. 

Jones DH, Cellitti SE, Hao X, Zhang Q, Jahnz M, Summerer D, Schultz PG, Uno T, Geierstanger BH (2010) Site-specific labeling of proteins with NMR-active unnatural amino acids. J Biomol NMR 46 89-100... 

Photoaffinity Labeling of Protein Targets in Additional Signaling Pathways... 

The selective modification of reactive side chains within proteins with compounds containing NMR-sensitive isotopes offers an alternative route to the labeling of proteins. The chemical modification of side chains with reagents labeled with NMR-sensitive isotopes may permit detailed structural and dynamic questions to be addressed, although perturbations of the system caused by the labeling may be of concern in cases where the chemical identity... 

L. Strekowski, M. Lipowska and G. Patonay, Substitution reactions of a nucleofugal group in heptamethine cyanine dyes. Synthesis of an isothiocyanato derivative for labeling of proteins with a near-infrared chromophore, J. Org. Chem. 57.4578-4580(1992). 

Gels are run for either analytical or preparative purposes. The intended use of the gel imposes restrictions on the amount of protein to be loaded and the means of detection. At one time it was popular to use radioactive labeling of proteins, with detection of proteins done by autoradiography. It is now more common to... 

Based on our current understanding of ribosomal protein synthesis, several strategies have been developed to incorporate amino acids other than the 20 standard proteinogenic amino acids into a peptide using the ribosomal machinery . This allows for the design of peptides with novel properties. On the one hand, such a system can be used to synthesize nonstandard peptides that are important pharmaceuticals. In nature, such peptides are produced by nonribosomal peptide synthetases, which operate in complex pathways. On the other hand, non-natural residues are a useful tool in biochemistry and biophysics to study proteins. For example, incorporation of non-natural residues by the ribosome allows for site-specific labeling of proteins with spin labels for electron paramagnetic resonance spectroscopy, with... 

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