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A designed branched three-helix bundle protein dimer
Linköpings universitet, Tekniska högskolan. Linköpings universitet, Institutionen för fysik, kemi och biologi.
2006 (Engelska)Ingår i: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 128, nr 22, s. 7287-7290Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

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.

Ort, förlag, år, upplaga, sidor
2006. Vol. 128, nr 22, s. 7287-7290
Nationell ämneskategori
Teknik och teknologier
Identifikatorer
URN: urn:nbn:se:liu:diva-50199DOI: 10.1021/ja060524kOAI: oai:DiVA.org:liu-50199DiVA, id: diva2:271095
Tillgänglig från: 2009-10-11 Skapad: 2009-10-11 Senast uppdaterad: 2017-12-12

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