ALS amino acid sequences

M Welschof, P Temess, F Kolbinger, et al. Amino acid sequence based PCR primers for amplification of rearranged human heavy and light chain immunoglobulin variable region genes. J Immunol Meth 179 203-214, 1995. 

MacLennan DH, Brandi CJ, Koreczak B, et al. Amino acid sequence of the Ca dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 1985 316 696-700. 

Michel, H., et al. The "heavy" subunit of the photosynthetic reaction center from Rhodopseudomonas viridis isolation of the gene, nucleotide and amino acid sequence. EMBO J. 4 1667-1672, 1985. 

Figure 17.2 An example of prediction of the conformations of three CDR regions of a monoclonal antibody (top row) compared with the unrefined x-ray structure (bottom row). LI and L2 are CDR regions of the light chain, and HI is from the heavy chain. The amino acid sequences of the loop regions were modeled by comparison with the sequences of loop regions selected from a database of known antibody structures. The three-dimensional structure of two of the loop regions, LI and L2, were in good agreement with the preliminary x-ray structure, whereas HI was not. However, during later refinement of the x-ray structure errors were found in the conformations of HI, and in the refined x-ray structure this loop was found to agree with the predicted conformations. In fact, all six loop conformations were correctly predicted in this case. (From C. Chothia et al.. Science 233 755-758, 1986.)...

Figure 17.16 Ribbon diagram representations of the structures of domain B1 from protein G (blue) and the dimer of Rop (red). The fold of B1 has been converted to an a-helical protein like Rop by changing 50% of its amino acids sequence. (Adapted from S. Dalai et al.,...

A cDNA encoding apoobelin was obtained from O. longissima and sequenced (Illarionov et al., 1995). The deduced amino acid sequence of the apoobelin consists of 195 amino acid residues, with a calculated molecular mass of about 22.2 kDa, closely matching the apoproteins of other Ca2+-sensitive photoproteins such as aequorin from the jellyfish Aequorea (Inouye et al., 1985 Prasher et al., 1985) and clytin from the jellyfish Phialidium gregarium (Inouye and Tsuji, 1993). To obtain recombinant apoobelin, the cDNA encoding apoobelin was expressed in E. coli (Illarionov et al., 2000). The recombinant apoobelin produced was purified and converted into obelin by incubation with coelenterazine in the presence of molecular oxygen and 2-mercaptoethanol or dithioerythritol, as in the case of aequorin. 

The cDNA encoding the luciferase of Renilla reniformis has been obtained and expressed in Escherichia coli (Lorenz et al., 1991). The cDNA contained an open reading frame encoding a 314-amino acid sequence. The recombinant Renilla luciferase obtained had a molecular weight of 34,000, and showed an emission maximum at 480 nm in the luminescence reaction of coelenterazine, in good agreement with the data of natural Renilla luciferase. 

Charbonneau, H., et al. (1985). Amino acid sequence of the calcium-dependent photoprotein aequorin. Biochemistry 24 6762-6771. 

Johnston, T. C., et al. (1990). The nucleotide sequence of the luxA and luxB genes of Xenorhabdus luminescence HM and a comparison of the amino acid sequences of luciferases from four species of bioluminescent bacteria. Biochem. Biophys. Res. Commun. 170 407- 115. 

Figure 1. An unrooted phylogenetic tree of the myosins based on the amino acid sequence comparison of their head domains demonstrating the division of the myosin superfamily into nine classes. The lengths of the branches are proportional to the percent of amino acid sequence divergence and a calibration bar for 5% sequence divergence is shovk n. The different classes of myosins have been numbered using Roman numerals in rough order of their discovery and hypothetical models of the different myosin structures are shown. Question marks indicate either hypothetical or unknown structural features, and only a fraction of the known myosins are shown. (Taken, in modified form, from Cheney et al., 1993).

There are 17 human type I IFN genes, all clustering on chromosome 9. They are intronless and encode secretory signal peptide sequences that are proteolytically cleaved prior to secretion from the cell. Type I IFNs are genetically and structurally closely related. They range in length from 161 to 208 amino acids and have apparent molecular weights of 15-24 kDa (Table 1) (Chen et al. 2004). The different subtypes of human IFN-a have approximately 50% amino acid sequence identity, whereas IFN-a shares approximately 22% amino acid identity with human IFN-p and 37% with human IFN-m (Chen et al. 2004). 

Coacervation occurs in tropoelastin solutions and is a precursor event in the assembly of elastin nanofibrils [42]. This phenomenon is thought to be mainly due to the interaction between hydro-phobic domains of tropoelastin. In scanning electron microscopy (SEM) picmres, nanofibril stmc-tures are visible in coacervate solutions of elastin-based peptides [37,43]. Indeed, Wright et al. [44] describe the self-association characteristics of multidomain proteins containing near-identical peptide repeat motifs. They suggest that this form of self-assembly occurs via specific intermolecular association, based on the repetition of identical or near-identical amino acid sequences. This specificity is consistent with the principle that ordered molecular assembhes are usually more stable than disordered ones, and with the idea that native-like interactions may be generally more favorable than nonnative ones in protein aggregates. 

Venom is secreted from the dorsal, pelvic and anal spines. A review of original papers indicates that many papers have failed to specify from which spine the venom was obtained. Therefore, some publications are meaningless scientifically. Not a single component of fish venoms has been characterized for the amino acid sequence yet. Even the molecular weight of fish toxins is not clear. Deakins and Saunders (25) concluded that the molecular weight of Scorpaena toxin was 150,000, while Schaeffer et al. (26) concluded that it had a molecular weight range of 50,000 to 800,000. 

Receptor subunits are numbered al, j61, etc. where there are more than one subunit of that type. Between different a subunits in any family there is around 60-70% amino-acid sequence homology whereas between a and subtypes, for example, there is normally around only 40% sequence homology. Mouse NMDA receptor subunits are denoted by the Greek letters and g while rat and human are indicated as shown. 

Recently, a new pectate lyase gene pelZ, was identified at the vicinity of the pelB-pelC cluster (Pissavin et al, submitted). ApelZ homologue was also foimd in Erwinia carotovora. PelZ defines a new family of endo-pectate lyase since its amino acid sequence displays only very low homology with that of other pectinases. 

The PE2 isoform has been purified and fully sequenced (Markovic and Joumval 1986). Using this sequence data Ray et al (1988) succeeded in isolating a clone fi om a tomato fruit cDNA library. The predicted amino acid sequence fi om this clone had high homology to the actual amino acid sequence determined for PE2 but was not identical. Subsequent screening of the tomato... 

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