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Engineered symmetric connectivity of secondary structure elements highlights malleability of protein folding pathways
University of Rome, La Sapienza. (Ivarsson)
2009 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 131, no 33, p. 11727-33Article in journal (Refereed) Published
Abstract [en]

To understand the role of sequence connectivity in protein folding pathways, we explored by Phi-value analysis the folding pathway of an engineered circularly permuted PDZ domain. This variant has the same sequence connectivity as naturally occurring circularly permuted PDZ domains and displays a symmetrical distribution of secondary structure elements (i.e., beta beta alpha beta beta alpha beta beta) while maintaining the same tertiary interactions of the well-characterized second PDZ domain from PTP-BL (PDZ2). Reliable Phi values were obtained for both a low-energy intermediate and the late rate-limiting transition state, allowing a description of both early and late events in folding. A comparison with Phi values obtained for wild-type PDZ2 reveals that while the structure of the late transition state is robust and unaffected by circular permutation, the folding intermediate is stabilized by a different nucleus involving residues located at the new N- and C-termini. The results suggest that folding is driven by competing nuclei whose stabilities may be selectively tuned by circular permutation.

Place, publisher, year, edition, pages
2009. Vol. 131, no 33, p. 11727-33
National Category
Natural Sciences
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URN: urn:nbn:se:uu:diva-203349DOI: 10.1021/ja900438bPubMedID: 19722594OAI: oai:DiVA.org:uu-203349DiVA, id: diva2:636250
Available from: 2013-07-09 Created: 2013-07-09 Last updated: 2017-12-06Bibliographically approved

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