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  <item rdf:about="http://www.proteinscience.org/details/journalArticle/761691/In_This_Issue.html">
    <title>In This Issue</title>
    <link>http://www.proteinscience.org/details/journalArticle/761691/In_This_Issue.html</link>
    <description>No abstract.</description>
    <dc:date>2010-07-22T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/761727/The_24th_Symposium_of_The_Protein_Society_Abstracts.html">
    <title>The 24th Symposium of The Protein Society: Abstracts</title>
    <link>http://www.proteinscience.org/details/journalArticle/761727/The_24th_Symposium_of_The_Protein_Society_Abstracts.html</link>
    <description />
    <dc:date>2010-07-21T00:00:00Z</dc:date>
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  <item rdf:about="http://www.proteinscience.org/details/journalArticle/746433/In_this_issue.html">
    <title>In this issue</title>
    <link>http://www.proteinscience.org/details/journalArticle/746433/In_this_issue.html</link>
    <description>No abstract.</description>
    <dc:date>2010-06-23T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/699749/In_This_Issue.html">
    <title>In This Issue</title>
    <link>http://www.proteinscience.org/details/journalArticle/699749/In_This_Issue.html</link>
    <description>No abstract.</description>
    <dc:date>2010-05-24T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/746435/Peripatetic_proteins.html">
    <title>Peripatetic proteins</title>
    <link>http://www.proteinscience.org/details/journalArticle/746435/Peripatetic_proteins.html</link>
    <description>No abstract.</description>
    <dc:date>2010-05-24T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/689017/In_This_Issue.html">
    <title>In This Issue</title>
    <link>http://www.proteinscience.org/details/journalArticle/689017/In_This_Issue.html</link>
    <description>No abstract.</description>
    <dc:date>2010-04-27T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/699757/Physicalchemical_determinants_of_coil_conformations_in_globular_proteins.html">
    <title>Physical-chemical determinants of coil conformations in globular proteins</title>
    <link>http://www.proteinscience.org/details/journalArticle/699757/Physicalchemical_determinants_of_coil_conformations_in_globular_proteins.html</link>
    <description>We present a method with the potential to generate a library of coil segments from first principles. Proteins are built from -helices and/or -strands interconnected by these coil segments. Here, we investigate the conformational determinants of short coil segments, with particular emphasis on chain turns. Toward this goal, we extracted a comprehensive set of two-, three-, and four-residue turns from X-ray-elucidated proteins and classified them by conformation. A remarkably small number of...</description>
    <dc:date>2010-04-13T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/594367/In_this_issue.html">
    <title>In this issue</title>
    <link>http://www.proteinscience.org/details/journalArticle/594367/In_this_issue.html</link>
    <description>No abstract.</description>
    <dc:date>2010-03-24T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/689019/A_synergistic_approach_to_protein_crystallization_Combination_of_a_fixedarm_carr.html">
    <title>A synergistic approach to protein crystallization: Combination of a fixed-arm carrier with surface entropy reduction</title>
    <link>http://www.proteinscience.org/details/journalArticle/689019/A_synergistic_approach_to_protein_crystallization_Combination_of_a_fixedarm_carr.html</link>
    <description>Protein crystallographers are often confronted with recalcitrant proteins not readily crystallizable, or which crystallize in problematic forms. A variety of techniques have been used to surmount such obstacles: crystallization using carrier proteins or antibody complexes, chemical modification, surface entropy reduction, proteolytic digestion, and additive screening. Here we present a synergistic approach for successful crystallization of proteins that do not form diffraction quality crystals...</description>
    <dc:date>2010-03-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/555025/In_This_Issue.html">
    <title>In This Issue</title>
    <link>http://www.proteinscience.org/details/journalArticle/555025/In_This_Issue.html</link>
    <description>No abstract.</description>
    <dc:date>2010-01-21T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/594369/The_prolinerich_domain_of_TonB_possesses_an_extended_polyproline_IIlike_conforma.html">
    <title>The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria</title>
    <link>http://www.proteinscience.org/details/journalArticle/594369/The_prolinerich_domain_of_TonB_possesses_an_extended_polyproline_IIlike_conforma.html</link>
    <description>TonB from Escherichia coli and its homologues are critical for the uptake of siderophores through the outer membrane of Gram-negative bacteria using chemiosmotic energy. When different models for the mechanism of TonB mediated energy transfer from the inner to the outer membrane are discussed, one of the key questions is whether TonB spans the periplasm. In this article, we use long range distance measurements by spin-label pulsed EPR (Double Electron-Electron Resonance, DEER) and CD...</description>
    <dc:date>2010-01-21T00:00:00Z</dc:date>
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  <item rdf:about="http://www.proteinscience.org/details/journalArticle/536973/In_This_Issue.html">
    <title>In This Issue</title>
    <link>http://www.proteinscience.org/details/journalArticle/536973/In_This_Issue.html</link>
    <description>No abstract.</description>
    <dc:date>2010-01-06T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/573743/In_memoriam_Walter_Kauzmann_19162009.html">
    <title>In memoriam: Walter Kauzmann (1916-2009)</title>
    <link>http://www.proteinscience.org/details/journalArticle/573743/In_memoriam_Walter_Kauzmann_19162009.html</link>
    <description />
    <dc:date>2010-01-06T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/555027/Myoglobin_strikes_back.html">
    <title>Myoglobin strikes back</title>
    <link>http://www.proteinscience.org/details/journalArticle/555027/Myoglobin_strikes_back.html</link>
    <description>Over the last half century, myoglobin (Mb) has been an excellent model system to test a number of concepts, theories, and new experimental methods that proved valuable to investigate protein structure, function, evolution, and dynamics. Mb's function, most often considered just an oxygen repository, has considerably diversified over the last 15 years, especially because it was shown to have a role in the biochemistry of quenching and synthesizing nitric oxide in the red muscle, thereby...</description>
    <dc:date>2009-12-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://www.proteinscience.org/details/journalArticle/536975/In_memoriam_Reflections_on_Charles_Tanford_19212009.html">
    <title>In memoriam: Reflections on Charles Tanford (1921-2009)</title>
    <link>http://www.proteinscience.org/details/journalArticle/536975/In_memoriam_Reflections_on_Charles_Tanford_19212009.html</link>
    <description />
    <dc:date>2009-11-20T00:00:00Z</dc:date>
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