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Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
2000 (English)In: JOURNAL OF BIOTECHNOLOGY, ISSN 0168-1656, Vol. 79, no 3, 281-298 p.Article in journal (Refereed) Published
Abstract [en]

In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing so, three main spectroscopic techniques used to investigate protein folding and stability are briefly introduced.

Place, publisher, year, edition, pages
ELSEVIER SCIENCE BV , 2000. Vol. 79, no 3, 281-298 p.
Keyword [en]
circular dichroism; co-operative and non-co-operative transition; flavodoxin; fluorescence; NMR; equilibrium unfolding; three-state model; HYDROGEN-EXCHANGE; AZOTOBACTER-VINELANDII; STRUCTURAL CHARACTERIZATION; MOLTEN GLOBULE; INTERMEDIATE; APOFLAVODOXIN;
URN: urn:nbn:se:uu:diva-38004OAI: oai:DiVA.org:uu-38004DiVA: diva2:65903
Addresses: van Mierlo CPM, Agr Univ Wageningen, Dept Biomol Sci, Biochem Lab, Dreijenlaan 3, NL-6703 HA Wageningen, Netherlands. Agr Univ Wageningen, Dept Biomol Sci, Biochem Lab, NL-6703 HA Wageningen, Netherlands. Univ Uppsala, Dept Biochem, Uppsala, SwAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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