2008
DOI: 10.2478/s11535-008-0026-5
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Distinctive attributes for predicted secondary structures at terminal sequences of non-classically secreted proteins from proteobacteria

Abstract: C-and N-terminal sequences (64 amino acid residues each) of 89 non-classically secreted type I, type III and type IV proteins (SwissProt/TrEMBL) from proteobacteria were transformed into predicted secondary structures. Multivariate analysis of variance (MANOVA) confirmed the significance of location (C-or N-termini) and secretion type as essential factors in respect of quantitative representations of structured (a-helices, b-strands) and unstructured (coils) elements. The profiles of secondary structures were … Show more

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Cited by 3 publications
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“…Here, "T1SP" represents the type I secreted protein, and the remaining are named by analogy with it. A public independent dataset of 89 NCSPs was constructed by Kampenusa and Zikmanis [21], which contains 32 T1SPs, 41 T3SPs and 16 T4SPs. The detailed data processing has been described in our previous work [20], and all data sets used in this study are listed in Table 1.…”
Section: Data Setsmentioning
confidence: 99%
“…Here, "T1SP" represents the type I secreted protein, and the remaining are named by analogy with it. A public independent dataset of 89 NCSPs was constructed by Kampenusa and Zikmanis [21], which contains 32 T1SPs, 41 T3SPs and 16 T4SPs. The detailed data processing has been described in our previous work [20], and all data sets used in this study are listed in Table 1.…”
Section: Data Setsmentioning
confidence: 99%