@article{Semmler2010seque-9644,
  year={2010},
  doi={10.1016/j.jasms.2009.10.004},
  title={De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry},
  number={2},
  volume={21},
  issn={1044-0305},
  journal={Journal of the American Society for Mass Spectrometry},
  pages={215--219},
  author={Semmler, Angelika and Weber, Reinhold and Przybylski, Michael and Wittmann, Valentin}
}

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    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T18:13:24Z</dc:date>
    <dc:creator>Przybylski, Michael</dc:creator>
    <dc:contributor>Przybylski, Michael</dc:contributor>
    <dc:contributor>Semmler, Angelika</dc:contributor>
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    <dc:contributor>Weber, Reinhold</dc:contributor>
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    <dcterms:bibliographicCitation>First publ. in: Journal of the American Society for Mass Spectrometry ; 21 (2010), 2. - S. 215-219</dcterms:bibliographicCitation>
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    <dc:creator>Wittmann, Valentin</dc:creator>
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    <dcterms:title>De novo sequencing of peptides on single resin beads by MALDI-FTICR tandem mass spectrometry</dcterms:title>
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    <dc:creator>Semmler, Angelika</dc:creator>
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    <dcterms:abstract xml:lang="eng">An efficient approach in combinatorial chemistry is the synthesis of one-bead-one-compound peptide libraries. In contrast to synthesis and functional screening, which is performed in a largely automated manner, structure determination has been frequently laborious and time-consuming. Here we report an approach for de novo sequencing of peptides on single beads by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance (MALDI-FTICR) tandem mass spectrometry, using a resin with a photolinker for solid-phase peptide synthesis. Upon sorting out single beads, an efficient sample preparation on the MALDI target was developed that enables fragmentation upon irradiation of the bead-matrix mixture with the ultraviolet (UV)-MALDI laser, with enhanced yield of sequence-specific fragment ions at increased laser energy. This approach is illustrated by sequence determinations of two peptides from a library with sequences varying in a single amino acid; the feasibility with tandem-MS procedures and fragment ion assignment was ascertained by sustained off-resonance irradiation/collision induced dissociation (SORI/CID) and infrared multiphoton dissociation (IRMPD) fragmentation.</dcterms:abstract>
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