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Its interaction with actin is mediated by a pair of conserved actin binding motifs (ABMs) at the WIP N\u2010terminus, a domain that has not been investigated in its unbound form. Here we use NMR to investigate the biophysical behavior of the N\u2010terminal ABM in WIP using protonless <jats:sup>13<\/jats:sup>C\u2032\u2010detected spectroscopy. Secondary chemical shifts, residual dipolar couplings and temperature effects identify residual structure throughout the ABM, which exhibits transient helical and \u03b2\u2010strand character for residues 30\u201342 and 44\u201362, respectively. These observed structural propensities echo the structure observed in the actin\u2010bound state of the ABM. Furthermore, residues preceding the canonical ABM (17\u201325) and conserved among WIP\u2010related proteins exhibit transient \u03b2\u2010strand character, suggesting that the WIP<jats:sup>N<\/jats:sup> interaction epitope extends towards the N\u2010terminal polyproline motif. This suggests a possible role for this region in mediating the WIP interaction with polyproline binders such as profilin. In revealing these features of the WIP ABM this study demonstrates the unique ability of NMR in characterizing unstructured domains and provides necessary information for further investigation of WIP\u2010mediated protein\u2013protein interactions.<\/jats:p>","DOI":"10.1111\/febs.13174","type":"journal-article","created":{"date-parts":[[2014,12,11]],"date-time":"2014-12-11T15:47:00Z","timestamp":1418312820000},"page":"700-714","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["New insights into the role of the disordered WIP N\u2010terminal domain revealed by <scp>NMR<\/scp> structural characterization"],"prefix":"10.1111","volume":"282","author":[{"given":"Hila","family":"Elazari\u2010Shalom","sequence":"first","affiliation":[{"name":"Department of Chemistry Bar Ilan University Ramat Gan 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