Conformational preludes to the latency transition in PAI-1 as determined by atomistic computer simul...
Conformational preludes to the latency transition in PAI-1 as determined by atomistic computer simulations and hydrogen/deuterium-exchange mass spectrometry
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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Both function and dysfunction of serine protease inhibitors (serpins) involve massive conformational change in their tertiary structure but the dynamics facilitating these events remain poorly understood. We have studied the dynamic preludes to conformational change in the serpin plasminogen activator inhibitor 1 (PAI-1). We report the first multi-...
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Conformational preludes to the latency transition in PAI-1 as determined by atomistic computer simulations and hydrogen/deuterium-exchange mass spectrometry
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TN_cdi_doaj_primary_oai_doaj_org_article_2be4f4e67be6467ca11b18fe2c3a033a
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_2be4f4e67be6467ca11b18fe2c3a033a
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ISSN
2045-2322
E-ISSN
2045-2322
DOI
10.1038/s41598-017-06290-0
