A designed branched three-helix bundle protein dimer
2006 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, Vol. 128, no 22, 7287-7290 p.Article in journal (Refereed) Published
The ultimate goals of de novo protein design are the construction of novel tertiary structures and functions. Here is presented the design and synthesis of a uniquely branched three-helix bundle that folds into a well-folded dimeric protein. The branching of this protein was performed by the method of native chemical ligation, which provides a chemoselective and stable amide bond between the unprotected fragments. This ligation strategy was possible by the presented facile preparation of a peptide (43 amino acids) with a specific side chain thioester, which is synthesized by general Fmoc solid phase peptide synthesis. From the presented structural analysis, it is seen that the folded protein is present as a stable and highly helical dimer, thus forming a six-helix bundle. This unique tertiary structure, composed of a dimer of three individual a-helices branched together, offers different possibilities for protein engineering, such as metal and cofactor binding sites, as well as for the construction of novel functions. © 2006 American Chemical Society.
Place, publisher, year, edition, pages
2006. Vol. 128, no 22, 7287-7290 p.
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-50199DOI: 10.1021/ja060524kOAI: oai:DiVA.org:liu-50199DiVA: diva2:271095