Prodan fluorescence mimics the GroEL folding cycle

The non-covalent fluorescent probe 6-propionyl-2-(dimethylamino) naphthalene sulfonate (prodan) binds to hydrophobic surfaces exposed on the surface of GroEL. Under identical experimental conditions free prodan exhibits a green emission peak of intensity 390,000 cps at 520 nm. However prodan bound t...

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Bibliographic Details
Published in:The Protein Journal 2004-10, Vol.23 (7), p.475-481
Main Authors: Kaur, Yogeet, Horowitz, Paul M
Format: Article
Language:English
Subjects:
2-Naphthylamine - analogs & derivatives
ATP
Bacterial Proteins - chemistry
Chaperonins
Emissions
Escherichia coli Proteins
Fluorescent Dyes
Heat-Shock Proteins - chemistry
Hydrophobic surfaces
Naphthalene
Protein Folding
Spectrometry, Fluorescence
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Summary:The non-covalent fluorescent probe 6-propionyl-2-(dimethylamino) naphthalene sulfonate (prodan) binds to hydrophobic surfaces exposed on the surface of GroEL. Under identical experimental conditions free prodan exhibits a green emission peak of intensity 390,000 cps at 520 nm. However prodan bound to GroEL, GroEL-ATP, and GroEL-ATP-GroES shows emission peaks of intensities 500,000, 540,000, and 480,000 cps at 515, 512 and 515 nm, respectively, thus mimicing the way hydrophobic surfaces on GroEL become exposed during the folding cycle. Other hydrophobic probes like bis-ANS and dansyl lysine were unable to detect the minor changes in hydrophobic exposure of GroEL after it binds to ATP, although they were able to detect hydrophobic exposure in GroEL itself.
ISSN:1572-3887
1875-8355
1573-4943
DOI:10.1007/s10930-004-5224-z