| First Author | Baran C | Year | 2010 |
| Journal | Biochem Biophys Res Commun | Volume | 391 |
| Issue | 1 | Pages | 224-9 |
| PubMed ID | 19903451 | Mgi Jnum | J:156735 |
| Mgi Id | MGI:4421279 | Doi | 10.1016/j.bbrc.2009.11.036 |
| Citation | Baran C, et al. (2010) Divalent cations induce a compaction of intrinsically disordered myelin basic protein. Biochem Biophys Res Commun 391(1):224-9 |
| abstractText | Central nervous system myelin is a dynamic entity arising from membrane processes extended from oligodendrocytes, which form a tightly-wrapped multilamellar structure around neurons. In mature myelin, the predominant splice isoform of classic MBP is 18.5kDa. In solution, MBP is an extended, intrinsically disordered protein with a large effective protein surface for myriad interactions, and possesses transient and/or induced ordered secondary structure elements for molecular association or recognition. Here, we show by nanopore analysis that the divalent cations copper and zinc induce a compaction of the extended protein in vitro, suggestive of a tertiary conformation that may reflect its arrangement in myelin. |
