uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
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, p. 207-214Article 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, p. 207-214
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-98286DOI: 10.1093/protein/gzm091ISI: 000253831300010PubMedID: 18239073OAI: oai:DiVA.org:uu-98286DiVA, id: diva2:174038
Available from: 2009-02-18 Created: 2009-02-18 Last updated: 2017-12-13Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMed
By organisation
Department of Medical Biochemistry and Microbiology
In the same journal
Protein Engineering Design & Selection
Natural Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 552 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf