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  <doc>
    <id>7164</id>
    <completedYear/>
    <publishedYear>2019</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>108</pageFirst>
    <pageLast>117</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>436</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Structural characterization of synthetic peptides using electronspray ion mobility spectrometry and molecular dynamics simulations</title>
    <abstract language="eng">Electrospray ionization-ion mobility spectrometry was employed for the determination of collision cross sections (CCS) of 25 synthetically produced peptides in the mass range between 540–3310 Da. The experimental measurement of the CCS is complemented by their calculation applying two different methods. One prediction method is the intrinsic size parameter (ISP) method developed by the Clemmer group. The second new method is based on the evaluation of molecular dynamics (MD) simulation trajectories as a whole, resulting in a single, averaged collision cross-section value for a given peptide in the gas phase. A high temperature MD simulation is run in order to scan through the whole conformational space. The lower temperature conformational distribution is obtained through thermodynamic reweighting. In the first part, various correlations, e.g. CCS vs. mass and inverse mobility vs. m/z correlations, are presented. Differences in CCS between peptides are also discussed in terms of their respective mass and m/z differences, as well as their respective structures. In the second part, measured and calculated CCS are compared. The agreement between the prediction results and the experimental values is in the same range for both calculation methods. While the calculation effort of the ISP method is much lower, the MD method comprises several tools providing deeper insights into the conformations of peptides. Advantages and limitations of both methods are discussed. Based on the separation of two pairs of linear and cyclic peptides of virtually the same mass, the influence of the structure on the cross sections is discussed. The shift in cross section differences and peak shape after transition from the linear to the cyclic peptide can be well understood by applying different MD tools, e.g. the root-mean-square deviation (RMSD) and the root mean square fluctuation (RMSF).</abstract>
    <parentTitle language="eng">International Journal of Mass Spectrometry</parentTitle>
    <identifier type="doi">10.1016/j.ijms.2018.10.036</identifier>
    <enrichment key="PeerReviewed">yes</enrichment>
    <enrichment key="AcceptedDate">2018/10/27</enrichment>
    <author>José Villatoro</author>
    <submitter>Marcus Weber</submitter>
    <author>Marcus Weber</author>
    <author>Martin Zühlke</author>
    <author>Andreas Lehmann</author>
    <author>Karl Zechiowski</author>
    <author>Daniel Riebe</author>
    <author>Toralf Beitz</author>
    <author>Hans-Gerd Löhmannsröben</author>
    <author>Oliver Kreuzer</author>
    <collection role="institutes" number="num">Numerical Mathematics</collection>
    <collection role="institutes" number="compmol">Computational Molecular Design</collection>
    <collection role="persons" number="weber">Weber, Marcus</collection>
    <collection role="projects" number="SALSA-IR-MALDI">SALSA-IR-MALDI</collection>
  </doc>
  <doc>
    <id>6053</id>
    <completedYear/>
    <publishedYear>2016</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>197</pageFirst>
    <pageLast>297</pageLast>
    <pageNumber/>
    <edition/>
    <issue>19/4</issue>
    <volume/>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">IR-MALDI ion mobility spectrometry: physical source characterization and application as HPLC detector</title>
    <parentTitle language="eng">International Journal for Ion Mobility Spectrometry</parentTitle>
    <identifier type="doi">10.1007/s12127-016-0208-1</identifier>
    <enrichment key="PeerReviewed">yes</enrichment>
    <author>José Villatoro</author>
    <submitter>Regine Kossick</submitter>
    <author>Martin Zühlke</author>
    <author>Daniel Riebe</author>
    <author>Toralf Beitz</author>
    <author>Marcus Weber</author>
    <author>Jens Riedel</author>
    <author>Hans-Gerd Löhmannsröben</author>
    <collection role="institutes" number="num">Numerical Mathematics</collection>
    <collection role="institutes" number="compmol">Computational Molecular Design</collection>
    <collection role="persons" number="weber">Weber, Marcus</collection>
    <collection role="projects" number="SALSA-IR-MALDI">SALSA-IR-MALDI</collection>
  </doc>
  <doc>
    <id>7959</id>
    <completedYear/>
    <publishedYear>2020</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>5247</pageFirst>
    <pageLast>5260</pageLast>
    <pageNumber/>
    <edition/>
    <issue/>
    <volume>412</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">Sub-ambient pressure IR-MALDI ion mobility spectrometer for the determination of low and high field mobilities</title>
    <abstract language="eng">A new ion mobility (IM) spectrometer, enabling mobility measurements in the pressure range between 5 and 500 mbar and in the reduced field strength range E/N of 5–90 Td, was developed and characterized. Reduced mobility (K0) values were studied under low E/N (constant value) as well as high E/N (deviation from low field K0) for a series of molecular ions in nitrogen. Infrared matrix-assisted laser desorption ionization (IR-MALDI) was used in two configurations: a source working at atmospheric pressure (AP) and, for the first time, an IR-MALDI source working with a liquid (aqueous) matrix at sub-ambient/reduced pressure (RP). The influence of RP on IR-MALDI was examined and new insights into the dispersion process were gained. This enabled the optimization of the IM spectrometer for best analytical performance. While ion desolvation is less efficient at RP, the transport of ions is more efficient, leading to intensity enhancement and an increased number of oligomer ions. When deciding between AP and RP IR-MALDI, a trade-off between intensity and resolving power has to be considered. Here, the low field mobility of peptide ions was first measured and compared with reference values from ESI-IM spectrometry (at AP) as well as collision cross sections obtained from molecular dynamics simulations. The second application was the determination of the reduced mobility of various substituted ammonium ions as a function of E/N in nitrogen. The mobility is constant up to a threshold at high E/N. Beyond this threshold, mobility increases were observed. This behavior can be explained by the loss of hydrated water molecules.</abstract>
    <parentTitle language="eng">Analytical and Bioanalytical Chemistry</parentTitle>
    <identifier type="doi">10.1007/s00216-020-02735-0</identifier>
    <enrichment key="PeerReviewed">yes</enrichment>
    <author>José Villatoro</author>
    <submitter>Marcus Weber</submitter>
    <author>Martin Zühlke</author>
    <author>Daniel Riebe</author>
    <author>Toralf Beitz</author>
    <author>Marcus Weber</author>
    <author>Hans-Gerd Löhmannsröben</author>
    <collection role="institutes" number="num">Numerical Mathematics</collection>
    <collection role="persons" number="weber">Weber, Marcus</collection>
    <collection role="projects" number="SALSA-IR-MALDI">SALSA-IR-MALDI</collection>
    <collection role="institutes" number="MSoCP">Modeling and Simulation of Complex Processes</collection>
  </doc>
  <doc>
    <id>6645</id>
    <completedYear/>
    <publishedYear>2016</publishedYear>
    <thesisYearAccepted/>
    <language>eng</language>
    <pageFirst>6259</pageFirst>
    <pageLast>6268</pageLast>
    <pageNumber/>
    <edition/>
    <issue>23</issue>
    <volume>408</volume>
    <type>article</type>
    <publisherName/>
    <publisherPlace/>
    <creatingCorporation/>
    <contributingCorporation/>
    <belongsToBibliography>0</belongsToBibliography>
    <completedDate>--</completedDate>
    <publishedDate>--</publishedDate>
    <thesisDateAccepted>--</thesisDateAccepted>
    <title language="eng">IR-MALDI ion mobility spectrometry</title>
    <parentTitle language="eng">Analytical and Bioanalytical Chemistry</parentTitle>
    <identifier type="doi">10.1007/s00216-016-9739-x</identifier>
    <enrichment key="PeerReviewed">yes</enrichment>
    <author>Jose Villatoro</author>
    <submitter>Marcus Weber</submitter>
    <author>Martin Zühlke</author>
    <author>Daniel Riebe</author>
    <author>Jens Riedel</author>
    <author>Toralf Beitz</author>
    <author>Hans-Gerd Löhmannsröben</author>
    <collection role="institutes" number="num">Numerical Mathematics</collection>
    <collection role="institutes" number="compmol">Computational Molecular Design</collection>
    <collection role="projects" number="SALSA-IR-MALDI">SALSA-IR-MALDI</collection>
  </doc>
</export-example>
