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 Effect of pH on the catalytic function and zinc content of native and immobilized anthrax lethal factor. Effect of pH on the catalytic function and zinc content of native and immobilized anthrax lethal factor. FEBS Lett. (0014-5793) 2013 Montpellier LH., Siemann S. in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Montpellier LH., Siemann S. FEBS Lett. (0014-5793) 2013 lef_bacan Lethal factor Anthrax lethal toxin endopeptidase component lef pXO1-107 BXA0172 GBAA_pXO1_0172 protein protein bacan Bacillus anthracis MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS DIP protein P15917 original sequence version: 109 DIP protein P15917 original sequence version: 138 DIP protein P15917 original sequence version: 93 DIP protein P15917 original sequence version: 98 DIP protein P15917 original sequence version: 112 DIP protein P15917 original sequence version: 125 2076B4D7277317EE lef-lef 1 LF 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified LF 2 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2 mint As shown in Fig. 2 (inset), the max value of the emission spectra at 333 nm was found to remain constant from pH 4.0 to 7.0, indicating that the C-terminal domains of LF (which house the protein s five tryptophan residues [3]) remain folded upon acidification. However, the significant increase in fluorescence intensity at 300 nm between pH 4 and 5 is a clear reflection of increased scattering, and thus of protein aggregation