Extending fluorescence anisotropy to large complexes using reversibly switchable proteins
Extending fluorescence anisotropy to large complexes using reversibly switchable proteins
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New York: Nature Publishing Group US
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English
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Publisher
New York: Nature Publishing Group US
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Contents
The formation of macromolecular complexes can be measured by detection of changes in rotational mobility using time-resolved fluorescence anisotropy. However, this method is limited to relatively small molecules (~0.1–30 kDa), excluding the majority of the human proteome and its complexes. We describe selective time-resolved anisotropy with reversi...
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Full title
Extending fluorescence anisotropy to large complexes using reversibly switchable proteins
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TN_cdi_swepub_primary_oai_DiVA_org_kth_327930
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_kth_327930
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ISSN
1087-0156,1546-1696
E-ISSN
1546-1696
DOI
10.1038/s41587-022-01489-7
