Detection and characterization proteins

Functional array Purified proteins are arrayed on the surface and used to detect and characterize protein - protein, protein - DNA or protein - small molecule interactions... 

The new methods to detect and characterize variations in gene and protein expression across the human genome in individuals will become common... 

One of the most powerful spectroscopic techniques for the detection and characterization of persistent and transient phenoxyls is time-resolved resonance Raman (RR) spectroscopy. Vibrational frequencies and the relative intensities of the resonance-enhanced bands have proven to be sensitive markers for tyrosyl radicals in proteins. For example, Sanders-Loehr and co-workers (31) detected the tyrosyl radical in native ribonucleotide reductase from Escherichia coli by a resonance-enhanced Raman mode at 1498 cm 1 that they assigned to the Ula Wilson mode of the tyrosyl, which is predominantly the u(C=0) stretching mode. 

Nozue, M. et al.. Detection and characterization of a vacuolar protein (VP24) in anthocyanin-producing cells of sweet potato in suspension culture. Plant Cell Physiol, 36, 883, 1995. 

Proteomics and its possible applications for assessment of allergenicity of food products are described by Bannon et al. (2008), who draw attention to the fact that reproducibility of results obtained though proteomic techniques need to be improved by introducing more precise definitions of the parameters of technical determinations. Nonetheless, proteomics provides high-throughput methods for detection and characterization of proteins. 

Mass spectrometry allows the detection and characterization of mutations within proteins, whether they are natural or obtained through directed mutagenesis [97-100]. The approach generally involves three steps molecular mass determination of the intact protein to detect the mutation, PMF of an enzymatic digest to identify mutated peptides, and finally, MS/MS to determine or confirm the position and the nature of the amino acid that has mutated. 

Shimizu, A., Nakanishi, T., and Miyazaki, A. (2006) Detection and characterization of variant and modified structures of proteins in blood and tissues by mass spectrometry. 

Burlingame, A.L. University of California Berkeley Detection and characterization of protein and DNA adducts by mass spectrometry NIEHS... 

J. C. T. Eijkel, Potentiometric detection and characterization of adsorbed protein using stimulus-response measurement techniques, thesis. University of Twente. Enschede, The Netherlands, ISBN 90-9008615-3, 1995. 

UV photolysis of CpMn(CO)3 in toluene leads to loss of CO and formation of CpMn(CO)2( ] -toluene). Kinetic studies suggest that the binding energy of the toluene is ca. 60kJmor. The binding of H2 to CpMn(CO)2 has been studied in supercritical CO2 solvent. It has been proposed that pyrylium and pyridinium salts such as (35) can be used to label proteins and thereby aid in the detection and characterization of receptor sites. Cymantrene bound to lysine residues of bovine serum albumin (BSA) has been used as a redox label. Electrochemical reduction of the label established an impressive BSA detection limit of 2 x 10 M. 

Automated carboxy-terminal (C-terminal) protein sequence analysis enables the direct and unambiguous confirmation of the C-terminal sequence of native and expressed proteins, the detection and characterization of protein processing at the C-terminus, the identification of post-translational proteolytic cleavages, and partial sequence information on amino-terminally blocked protein samples. In order for C-terminal sequence analysis to be of immediate benefit, each of the 20 common amino acid residues must be detectable. Additionally, the scope of typically analyzable protein samples must span a usefully broad molecular weight range and degree of structural complexity. 

Some of the areas where interfacial protein layers dominate the boundary chemistry are reviewed, and we introduce some nondestructive armlytical methods which can be used simultaneously and/or sequentially to detect and characterize the microscopic amounts of matter at protein or other substrates which spontaneously acquire protein conditioning films. Examples include collagen and gelatin, synthetic polypeptides, nylons, and the biomedically important surfaces of vessel grafts, skin, tissue, and blood. The importance of prerequisite adsorbed films of proteins during thrombus formation, cell adhesion, use of intrauterine contraceptives, development of dental adhesives, and prevention of maritime fouling is discussed. Specifics of protein adsorption at solid/liquid and gas/liquid interfaces are compared. 

Another important development in the field of biopolymer analysis is the introduction of matrix-assisted laser desorption ionization (MALDl), which is a rather recent soft ionization technique that produces molecular ions of large organic molecules. In combination with time-of-flight (TOP) mass spectrometry, it was proposed as a valuable tool for the detection and characterization of biopolymers, such as proteins, peptides, and oligosaccharides, in many types of samples.The use of these recently developed techniques has not decreased the use of chromatography in determinations of biopolymers. Some efforts on the adaptation of the separation abilities of HPLC to the high potential of MALDl-TOF for the sensitive determination of additives in biocomposites are currently being carried out. 

Nagy SR, Sanborn JR, Hammock BD, Denison MS. 2002. Development of a green fluorescent protein based cell bioassay for the rapid and inexpensive detection and characterization of AhR agonists. Toxicol. Sci. 65 200-10... 

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