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Results 1 - 7 of 7
EC Number
x * 49800, His-tagged enzyme, sequence calculation, x * 62000, recombinant His-tagged enzyme, SDS-PAGE
x * 52400, His-tagged enzyme, sequence calculation, x * 53000, recombinant His-tagged enzyme, SDS-PAGE
1 * 50700, recombinant His-tagged Mak, SDS-PAGE
1 * 57000, SDS-PAGE
Pep2 forms a heterooctameric complex with trehalose synthase TreS, the complex formation markedly accelerates the maltokinase activity of Pep2
the N-terminal lobe can be divided into two subdomains: a cap N-terminal subdomain comprising the first 88 amino acid residues and an intermediate subdomain composed of an anti-parallel beta-sheet flanked by two helices. The C-terminal lobe is mostly alpha-helical. While the N-terminal cap subdomain and the C-terminal lobe are predominantly acidic, the intermediate subdomain is enriched in positively charged residues. The N-terminal cap subdomain is composed of three long antiparallel beta-strands forming a curved beta-sheet that encloses the N-terminal alpha-helix and a short two-stranded beta-sheet running perpendicular to the longest beta-sheet axis, on its concave surface. The intermediate subdomain (residues 89-200) contains a central seven-stranded beta-sheet flanked by two alpha-helical segments. A nine-residue linker (residues 201-209) containing a short beta-strand connects the intermediate subdomain and the C-terminal lobe. This last domain is composed of two central 4-helical bundles, a short beta-hairpin and a small two-stranded beta-sheet
trimer or tetramer
x * 52000, ultracentrifugation
Results 1 - 7 of 7