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Folding of Spectrin's SH3 Domain in the Presence of Spectrin Repeats
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
Umeå University, Faculty of Science and Technology, Chemistry.
2005 (English)In: Cellular & Molecular Biology Letters, Vol. 10, 595-612 p.Article in journal (Refereed) Published
Abstract [en]

The multifunctional protein spectrin contains several different structural motifs, such as spectrin repeats and a SH3 domain. Both triple-helix spectrin repeats and the SH3 domain are believed to form independent structural entities. In a-spectrins the SH3 domain is localized to repeat 9, where it is positioned between helix B and helix C in the repeat unit. The presence of SH3 in repeat 9 decreases the thermal stability considerably of this repeat unit while another insert in helix C does not seem to affect the stability. Addition of one or two adjacent repeat units increases the thermal stability from ca 25°C to ~41 and ~48°C, respectively. Despite the differences in thermal stability, the folding properties of peptides comprising the SH3 domain only or together with one or more repeats are more or less the same.

Place, publisher, year, edition, pages
2005. Vol. 10, 595-612 p.
Identifiers
URN: urn:nbn:se:umu:diva-13232OAI: oai:DiVA.org:umu-13232DiVA: diva2:152903
Note
http://www.cmbl.org.pl/vol10_nr4.htmlAvailable from: 2007-06-12 Created: 2007-06-12 Last updated: 2011-01-12Bibliographically approved

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