MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2014n-1 Edge strand engineering prevents native-like aggregation in Sulfolobus solfataricus acylphosphatase in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined stefano.ricagno@unimi.it 2014 imex curation de Rosa M., Bemporad F., Pellegrino S., Chiti F., Bolognesi M., Ricagno S. FEBS J. (1742-464X) Only protein-protein interactions acyp_sacs2 Acylphosphatase SSO0887 acyP Acylphosphate phosphohydrolase protein protein sulso Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEVEKVDYSFSEYKGEFEDFETY acyp-acyp 1539784 n/a Sso AcP 1539785 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a Sso AcP 1539785 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false f4 In order to verify whether the same model holds for the three B4 mutants here investigated, we monitored the aggregation time courses of the full length V84P, V84D and Y86E Sso AcP in the presence of increasing concentrations of the N11 peptide, ranging from 0 to a 20-fold molar excess, and using Thioflavin-T fluorescence as the aggregation probe (Figure 4). The results revealed that no significant differences in the aggregation behaviour of the three mutants could be observed as the amount of N11 was increased. While a 10-fold molar excess of N11 decreases the aggregation rate of wt Sso AcP by 80% (Figure 4B; reprinted from [33]), in the case of the three mutants the observed aggregation rates were within 10% of the value obtained in the absence of the peptide (Figure 4D, 4F, 4H). These results show that aggregation of the V84D, V84P and Y86E Sso AcP variants is nottriggered by the intermolecular interaction between the N-terminal segment and B4, as instead previously shown for wt Sso AcP.