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      The Quantitative Proteome of the Cement and Adhesive Gland of the Pedunculate Barnacle, Pollicipes pollicipes

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          Abstract

          Adhesive secretion has a fundamental role in barnacles’ survival, keeping them in an adequate position on the substrate under a variety of hydrologic regimes. It arouses special interest for industrial applications, such as antifouling strategies, underwater industrial and surgical glues, and dental composites. This study was focused on the goose barnacle Pollicipes pollicipes adhesion system, a species that lives in the Eastern Atlantic strongly exposed intertidal rocky shores and cliffs. The protein composition of P. pollicipes cement multicomplex and cement gland was quantitatively studied using a label-free LC-MS high-throughput proteomic analysis, searched against a custom transcriptome-derived database. Overall, 11,755 peptide sequences were identified in the gland while 2880 peptide sequences were detected in the cement, clustered in 1616 and 1568 protein groups, respectively. The gland proteome was dominated by proteins of the muscle, cytoskeleton, and some uncharacterized proteins, while the cement was, for the first time, reported to be composed by nearly 50% of proteins that are not canonical cement proteins, mainly unannotated proteins, chemical cues, and protease inhibitors, among others. Bulk adhesive proteins accounted for one-third of the cement proteome, with CP52k being the most abundant. Some unannotated proteins highly expressed in the proteomes, as well as at the transcriptomic level, showed similar physicochemical properties to the known surface-coupling barnacle adhesive proteins while the function of the others remains to be discovered. New quantitative and qualitative clues are provided to understand the diversity and function of proteins in the cement of stalked barnacles, contributing to the whole adhesion model in Cirripedia.

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          Thermostability and aliphatic index of globular proteins.

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          A statistical analysis shows that the aliphatic index, which is defined as the relative volume of a protein occupied by aliphatic side chains (alanine, valine, isoleucine, and leucine), of proteins of thermophilic bacteria is significantly higher than that of ordinary proteins. The index may be regarded as a positive factor for the increase of thermostability of globular proteins.
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            PredictProtein—an open resource for online prediction of protein structural and functional features

            PredictProtein is a meta-service for sequence analysis that has been predicting structural and functional features of proteins since 1992. Queried with a protein sequence it returns: multiple sequence alignments, predicted aspects of structure (secondary structure, solvent accessibility, transmembrane helices (TMSEG) and strands, coiled-coil regions, disulfide bonds and disordered regions) and function. The service incorporates analysis methods for the identification of functional regions (ConSurf), homology-based inference of Gene Ontology terms (metastudent), comprehensive subcellular localization prediction (LocTree3), protein–protein binding sites (ISIS2), protein–polynucleotide binding sites (SomeNA) and predictions of the effect of point mutations (non-synonymous SNPs) on protein function (SNAP2). Our goal has always been to develop a system optimized to meet the demands of experimentalists not highly experienced in bioinformatics. To this end, the PredictProtein results are presented as both text and a series of intuitive, interactive and visually appealing figures. The web server and sources are available at http://ppopen.rostlab.org.
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              Evaluation of FASP, SP3, and iST Protocols for Proteomic Sample Preparation in the Low Microgram Range

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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                05 April 2020
                April 2020
                : 21
                : 7
                : 2524
                Affiliations
                [1 ]CIIMAR–Interdisciplinary Centre of Marine and Environmental Research, University of Porto, Rua General Norton de Matos s/n, Terminal de Cruzeiros do Porto de Leixões, 4450-208 Matosinhos, Portugal; dany.perez@ 123456ciimar.up.pt (D.D.-P.); danielaalmeida23@ 123456gmail.com (D.A.); andre.machado@ 123456ciimar.up.pt (A.M.M.); filipe.castro@ 123456ciimar.up.pt (L.F.C.); aantunes@ 123456ciimar.up.pt (A.A.); vmvascon@ 123456fc.up.pt (V.V.); amoclclix@ 123456gmail.com (A.C.)
                [2 ]Cellular Proteomics Research, Helmholtz Centre for Infection Research, Inhoffenstraße. 7, 38124 Braunschweig, Germany; Josef.Wissing@ 123456helmholtz-hzi.de (J.W.); Lothar.Jaensch@ 123456Helmholtz-HZI.de (L.J.)
                [3 ]Biology Department, Faculty of Sciences, University of Porto, Rua do Campo Alegre, s/n, 4169-007 Porto, Portugal
                Author notes
                [* ]Correspondence: isabel.cunha@ 123456ciimar.up.pt ; Tel.: +351-22-340-1800; Fax: +351-22-339-0608
                [†]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0002-5211-972X
                https://orcid.org/0000-0002-9874-933X
                https://orcid.org/0000-0002-6857-7581
                https://orcid.org/0000-0002-1328-1732
                https://orcid.org/0000-0003-3585-2417
                https://orcid.org/0000-0003-4621-885X
                https://orcid.org/0000-0002-6149-9840
                Article
                ijms-21-02524
                10.3390/ijms21072524
                7177777
                32260514
                0b28ca66-f7e3-41f4-8e11-cf97a7b25836
                © 2020 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 19 February 2020
                : 01 April 2020
                Categories
                Article

                Molecular biology
                underwater adhesion,cement protein,q-exactive,proteogenomic,maxquant,ibaq,protein expression

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