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Diversity sequence

Amyloid fibrils form from a variety of native proteins with diverse sequences and folds. The classic method for the structural analysis of amyloid has been X-ray fiber diffraction amyloid fibrils exhibit a characteristic diffraction signature, called the cross-/) pattern. This cross-/ pattern suggested a repeating structure in which /1-sheets run parallel to the fiber axis with their constituent /1-strands perpendicular to that direction (Sunde and Blake, 1997). This diffraction signature pointed to an underlying common core molecular structure for the amyloid fibril that could accommodate diverse sequences and folds. A number of groups have proposed amyloid folds that are consistent with the experimental data and these can be linked to repeating /1-structured units. [Pg.115]

Lemmon, M.A., Ferguson, K.M. and Schlessinger, 1. PH Domains Diverse sequences with a common fold recruit signaling molecules to the cell surface (1996) Cell 85, 621-624... [Pg.322]

In addition to RNA-binding domains, the auxiliary domains are important components of the hnRNPs (Biamonti and Riva, 1994). Unlike RNA-binding domains, these domains are unstructured and have diverse sequences, making their classification difficult. The best characterized domain is the glycine-rich type found in hnRNPs Al and A2/B1. In hnRNP Al, the glycine-rich domain is localized near the C-terminus and is... [Pg.237]

The majority of conotoxin structures (115 of 125 structures in the PDB) have been determined by NMR spectroscopy as opposed to X-ray crystallography. They have significant structural diversity as a result of their diverse sequences and disulphide connectivities. Furthermore, conotoxins also have a large number of post-translational modifications, including the presence of hydroxyproline, y-carboxyglutamic acid and bromotryptophan residues, epimerisation, glycosyla-tion and amidation,144,145 that enhance their structural diversity. A recent analysis of NMR data for the unusual amino acids present in conotoxins3 provides a reference source for chemical shifts of post-translationally modified amino acids. [Pg.134]

Takagi, J., Kamata, T., Meredith, J., Puzon-McLaughlin, W., and Takada, Y. (1997). Changing ligand specificities of av/31 and av/33 integrins by swapping a short diverse sequence of the / subunit. /. Biol. Chem. 272, 19794—19800. [Pg.62]

Jensen, K. et al (2006) Identifying functionally important mutations from phenotypically diverse sequence data. Appl Environ. Microbiol, 72 (5), 3696- 3701. [Pg.782]

Fig. 8. Autoradiograms of a model library of structure R-Xj-S-Xj-M-TentaGel incubated with 7[ P] ATP either with (Panel A) or without (Panel B) the catalytic subunit of protein kinase A (PKA-C). Only the first four Edman cycles were performed for this experiment. Side-by-side spreads of the beads and exposure on a single film for 3 h at RT are shown. The sequences of labeled beads are indicated along with the percentage of the total radiolabel competed off by nonradioactive ATP. It is clear that considerable amounts of label can associate noncovalently with diverse sequences, so competition and quantitative methods are important to successful screening. The substrate motif for PKA-C is RRXS (13). represents a sequencing cycle with a proprietary unnatural amino acid. Fig. 8. Autoradiograms of a model library of structure R-Xj-S-Xj-M-TentaGel incubated with 7[ P] ATP either with (Panel A) or without (Panel B) the catalytic subunit of protein kinase A (PKA-C). Only the first four Edman cycles were performed for this experiment. Side-by-side spreads of the beads and exposure on a single film for 3 h at RT are shown. The sequences of labeled beads are indicated along with the percentage of the total radiolabel competed off by nonradioactive ATP. It is clear that considerable amounts of label can associate noncovalently with diverse sequences, so competition and quantitative methods are important to successful screening. The substrate motif for PKA-C is RRXS (13). represents a sequencing cycle with a proprietary unnatural amino acid.
Baerga-Ortiz, A., Hughes, C.A., Mandell, J.G. and Komives, E.A., Epitope mapping of a monoclonal antibody against hnman thrombin by R/D-exchange mass spectrometry reveals selection of a diverse sequence in a highly conserved protein. Protein Sci., 11, 1300-1308 (2002). [Pg.194]

Molecular features, substrate specificities, inhibitors, stoichiometry of the catalyzed reaction, spectroscopic features, prosthetic groups, and reaction mechanisms of plant CuAOs have been reviewed previously (Medda et al. 1995a). CuAOs are homodimers in which each subunit, consisting of approximately 6 0- 80 amino acids, contains a copper ion and a redox cofactor TPQ, generated by posttransla-tional autocatalytic modification from an active-site tyrosine residue (Mpller and McPherson 1998 Dawkes and Phillips 2001). CuAOs have rather diverse sequences, and only approximately 30 amino acid residues are fully conserved (Tipping and... [Pg.82]


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See also in sourсe #XX -- [ Pg.462 ]




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