@article{Althaus2010Compu-17267,
  year={2010},
  doi={10.1186/1471-2105-11-424},
  title={Computing H/D-Exchange rates of single residues from data of proteolytic fragments},
  number={1},
  volume={11},
  journal={BMC Bioinformatics},
  author={Althaus, Ernst and Canzar, Stefan and Ehrler, Carsten and Emmett, Mark R. and Karrenbauer, Andreas and Marshall, Alan G. and Meyer-Bäse, Anke and Tipton, Jeremiah D. and Zhang, Hui-Min},
  note={Article Number: 424}
}

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    <dc:contributor>Zhang, Hui-Min</dc:contributor>
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    <dc:creator>Emmett, Mark R.</dc:creator>
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    <dc:creator>Marshall, Alan G.</dc:creator>
    <dc:contributor>Ehrler, Carsten</dc:contributor>
    <dc:creator>Canzar, Stefan</dc:creator>
    <dcterms:issued>2010</dcterms:issued>
    <dc:contributor>Meyer-Bäse, Anke</dc:contributor>
    <dc:contributor>Canzar, Stefan</dc:contributor>
    <dc:creator>Tipton, Jeremiah D.</dc:creator>
    <dc:creator>Karrenbauer, Andreas</dc:creator>
    <dc:language>eng</dc:language>
    <dc:contributor>Althaus, Ernst</dc:contributor>
    <dcterms:abstract xml:lang="eng">Background: Protein conformation and protein/protein interaction can be elucidated by solution-phase Hydrogen/&lt;br /&gt;Deuterium exchange (sHDX) coupled to high-resolution mass analysis of the digested protein or protein complex.&lt;br /&gt;In sHDX experiments mutant proteins are compared to wild-type proteins or a ligand is added to the protein and&lt;br /&gt;compared to the wild-type protein (or mutant). The number of deuteriums incorporated into the polypeptides&lt;br /&gt;generated from the protease digest of the protein is related to the solvent accessibility of amide protons within&lt;br /&gt;the original protein construct.&lt;br /&gt;Results: In this work, sHDX data was collected on a 14.5 T FT-ICR MS. An algorithm was developed based on&lt;br /&gt;combinatorial optimization that predicts deuterium exchange with high spatial resolution based on the sHDX data&lt;br /&gt;of overlapping proteolytic fragments. Often the algorithm assigns deuterium exchange with single residue&lt;br /&gt;resolution.&lt;br /&gt;Conclusions: With our new method it is possible to automatically determine deuterium exchange with higher&lt;br /&gt;spatial resolution than the level of digested fragments.</dcterms:abstract>
    <dc:contributor>Tipton, Jeremiah D.</dc:contributor>
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    <dc:contributor>Karrenbauer, Andreas</dc:contributor>
    <dc:creator>Zhang, Hui-Min</dc:creator>
    <dc:contributor>Emmett, Mark R.</dc:contributor>
    <dc:creator>Ehrler, Carsten</dc:creator>
    <dc:rights>terms-of-use</dc:rights>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-12-01T12:54:23Z</dc:date>
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    <dc:creator>Althaus, Ernst</dc:creator>
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    <dc:contributor>Marshall, Alan G.</dc:contributor>
    <dc:creator>Meyer-Bäse, Anke</dc:creator>
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    <dcterms:bibliographicCitation>First publ. in: BMC Bioinformatics ; 11 (2010). - 424</dcterms:bibliographicCitation>
    <dcterms:title>Computing H/D-Exchange rates of single residues from data of proteolytic fragments</dcterms:title>
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