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Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2008 (English)In: Protein Engineering Design & Selection, ISSN 1741-0126, E-ISSN 1741-0134, Vol. 21, no 3, 207-214 p.Article in journal (Refereed) Published
Abstract [en]

The role of intermediates in the folding reaction of single-domain proteins is a controversial issue. It was previously shown by different methods that an on-pathway intermediate is populated in the presence of sodium sulphate during the folding of the FF domain from HYPA/FBP11. Here we demonstrate using analysis of the amplitudes of kinetic traces that this burst-phase folding intermediate is present at different salt concentration and at various pH, and is also found in roughly 30 site-directed mutants. The intermediate appears robust to changing conditions and thus fulfils an important criterion for a productive molecular species on the folding reaction pathway.

Place, publisher, year, edition, pages
2008. Vol. 21, no 3, 207-214 p.
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Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-98286DOI: 10.1093/protein/gzm091ISI: 000253831300010PubMedID: 18239073OAI: oai:DiVA.org:uu-98286DiVA: diva2:174038
Available from: 2009-02-18 Created: 2009-02-18 Last updated: 2017-12-13Bibliographically approved

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