989 resultados para CHLORO-SIDE-GROUP
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Current findings, news and announcements related to the history of Australian newspapers.
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Two experiments examined the effects of interpersonal and group-based similarity on perceived self-other differences in persuasibility (i.e. on third-person effects, Davison, 1983). Results of Experiment 1 (N=121), based on experimentally-created groups, indicated that third-person perceptions with respect to the impact of televised product ads were accentuated when the comparison was made with interpersonally different others. Contrary to predictions, third-person perceptions were not affected by group-based similarity (i.e. ingroup or outgroup other). Results of Experiment 2 (N = 102), based an an enduring social identity, indicated that both interpersonal and group-based similarity moderated perceptions of the impact on self and other of least-liked product ads. Overall, third-person effects were more pronounced with respect to interpersonally dissimilar others. However, when social identity was salient, information about interpersonal similarity of the target did not affect perceived self-other differences with respect to ingroup targets. Results also highlighted significant differences in third-person perceptions according to the perceiver's affective evaluation of the persuasive message. (C) 1998 John Wiley & Sons, Ltd.
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Structures of free, substrate-bound and product-bound forms of Escherichia coli xanthine-guanine phosphoribosyltransferase (XGPRT) have been determined by X-ray crystallography. These are compared with the previously determined structure of magnesium and sulphate-bound XPRT. The structure of free XGPRT at 2.25 Angstrom resolution confirms the flexibility of residues in and around a mobile loop identified in other PRTases and shows that the cis-peptide conformation of Arg37 at the active site is maintained in the absence of bound ligands. The structures of XGPRT complexed with the purine base substrates guanine or xanthine in combination with cPRib-PP, an analog of the second substrate PRib-PP, have been solved to 2.0 Angstrom resolution. In these two structures the disordered phosphate-binding loop of uncomplexed XGPRT becomes ordered through interactions with the 5'-phosphate group of cPRib-PP. The cyclopentane ring of cPRib-PP has the C3 exo pucker conformation, stabilised by the cPRib-PP-bound Mg2+. The purine base specificity of XGPRT appears to be due to water-mediated interactions between the 2-exocyclic groups of guanine or xanthine and side-chains of Glu136 and Asp140, as well as the main-chain oxygen atom of Ile135. Asp92, together with Lys115, could help stabilise the N7-protonated tautomer of the incoming base and could act as a general base to remove the proton from N7 .when the nucleotide product is formed. The 2.6 Angstrom resolution structure of XGPRT complexed with product GMP is similar to the substrate-bound complexes. However, the ribose ring of GMP is rotated by similar to 24 degrees compared with the equivalent ring in cPRib-PP. This rotation results in the loss of all interactions between the ribosyl group and the enzyme in the product complex. (C) 1998 Academic Press.