Protein labeling, schematic representation

FIGURE 5.6 Schematic representation of the immunosensor based on a Protein A-GEB biocomposite as a transducer, (a) Immobilization of RlgG on the surface via interaction with Protein A, (b) competitive immunoassay using anti-RIgG and biotinylated anti-RIgG, (c) enzyme labeling using HRP-streptavidin and (d) electrochemical enzyme activity determination. (Reprinted from [31] with permission from Elsevier.)... 

Figure 8.6 Schematic representation of a biomolecular-nanoparticle supramolecular assembly consisting of double-stranded DNA (ds-ODN) modified electrodes for the capture of p53 protein. Electrochemical signal generation and amplification occurred by subsequent labeling of the p53 tetramer with biotin (Biotin-Mi) and capture of streptavidin-modified Fc-capped AuNPs.26 (Reprinted with permission from J. Wang et al., Anal. Chem. 2008,80,769 -774. Copyright 2008 American Chemical Society.)...

Figure 13.7 Schematic representation of quantification using metabolic labeling of relative abundances of proteins from two cell populations.

Fig. 1. A schematic representation of the twin-site ELISA for fos and myc proteins. The signal from the alkaline phosphatase label is amplified via the AMPAK enzyme cycle to generate the red formazan dye.

Fig. 8.1. Two-dimensional schematic representation of the structure of the adenine nucleotide carrier. The line represents the amino acid chain of the protein and all numbers on or within the line represent the number of the amino acids in the linear sequence. The black dots are cysteine residues, about which there is significant sequence homology [186]. The helical regions are segments of hydrophobic amino acids thought to span the membrane [186]. The CAT arrow represents the site of photoaffinity labelling of an azido derivative of atractyloside [189]. The open circles are lysine residues which react with pyridoxal phosphate in intact mitochondria or submitochondrial particles [190,191].

Figure 8.3. Modular structure of two proteins involved in blood clotting. Schematic representation of the modular structure of human tissue plasminogen activator and coagulation factor XII. A module labeled C is shared by several proteins involved in blood clotting. FI and F2 are frequently repeated units that were first seen in fibronectin. E is a module resembling epidermal growth factor. A module known as a "kringle domain" is denoted K.

Fig. 13. Biofunctional QDs as fluorescent biological labels. (A) Size- and material-dependent emission spectra of different surfactant-coated semiconductor nanocrystals. The blue series represents CdSe nanocrystals with diameters of 2.1, 2.4, 3.1, 3.6, and 4.6nm (from right to left). The green series represents InP nanocrystals with diameters of 3.0, 3.5, and 4.6 nm. The red series represents InAs nanocrystals with diameters of 2.8,3.6,4.6, and 6.0 nm. (B) True-colour images of silica coated core (CdSe)-shell (ZnS or CdS) nanocrystals in aqueous buffer, illuminated with an ultraviolet lamp. (C) Schematic representation of a core (CdSe)-shell (ZnS)quantum dot that is covalently coupled to a protein by mercaptoacetic add. (D) TEM of QD-transferrin conjugates. Scale bar, 100 run. Adapted from Refe. 167 and 168. (See Color Plate 36.)...

Fig. 13. Schematic representation of direct labelling methods using (A) primary antibody coupled to gold or (B) Fab fragment coupled to gold and indirect labelling methods using (C) protein A-gold, (D) secondary antibody coupled to gold or (E) the streptavidin-biotin system, showing clearly the difference between resolution and sensitivity.

Figure 1 A schematic representation of a gene regulatory network involving modules of molecular classes (shown in boxes) the modules shown are the transcriptional units in the genome (G), primary transcripts (Ro), mature transcripts (R), primary proteins (Po), modified proteins (P), and metabolites (M). The labeled steps shown in black lines are transcription (x), RNA processing (p), translation (a), protein modification (p), metabolic pathways (ti), and genome replication (a). The feedback interactions shown in gray lines are discussed in the text. Filled circles represent either inhibition or activation.

Fig. 4. Hemoglobin. Schematic representation of the four subunits of deoxyhemoglobin. Helical regions are labeled A, B, C, etc., the same designation as in Fig. 3. For the true perspective of the tetramer, see Fig.6 below, and Figs.9 10 in proteins. DPG = 2,3-diphosphoglycerate.

FIGURE 1 Schematic representation of the labeling of a GTP-binding protein in a perme-abilized cell using [a- P]GTP. For further information refer to the text. 

It is essential to utilize C- or N-labeled proteins or peptides, instead of natural abundance, as samples to be used for solid-state NMR, in order to improve the sensitivity and/or selectivity of the amino acid residues under consideration. Such isotopically labeled bR samples needed for NMR studies are readily available from the large-scale culture of Halobacterium salinarum S-9 strain using synthetic media in which certain unlabeled amino acids are replaced with Relabeled amino acid species such as [3- RC]Ala or [l- RC]Val. This is shown in the circled or boxed residues, respectively, in the schematic representation of the primary sequence of bR, taking into account the secondary folding on the basis of X-ray diffraction, in Fig. 4. Undoubtedly, selective isotope labeling in this way, although not site-directed isotope labeling, could be most favorable in... 

Figure 29 Schematic representation of the QD-dye-labeled protein conjugate (DHLA dihydroUpoic acid, a water-soluble capping ligand MBP maltose binding protein Dye AlexaFluor 488 or Cy3) used to investigate the properties of QDs as acceptors in FRET processes. (Reproduced with permission from Ref. 64. 2005, American Chemical Society.)...

Schematic representations of methods for stable-isotope protein labeling for quantitative proteomics. 2003 Nature Publishing Group.

Fig. 23. Schematic representation the trapi g protein-labeled DNA in a get aj Chain in the trap, with field pulling down 6/ Chain in the course of crossing the potential barrier (thermal detrapping), with field pulling down c/ Chain detra qied dj same as a/ ej Chain in the course of detrapping activated by a reverse field-pulse (fidd pulling up) fj Chain detrai d by the reverse pulse...

---