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Kinetics of Acrylodan-Labelled cAMP-Dependent Protein Kinase Catalytic Subunit Denaturation
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
2013 (English)In: The Protein Journal, ISSN 1572-3887, Vol. 32, no 7, 519-525 p.Article in journal (Refereed) Published
Abstract [en]

Fluorescence spectroscopy was used to study denaturation of cAMP-dependent protein kinase catalytic subunit labeled with an acrylodan moiety. The dye was covalently bound to a cystein residue introduced into the enzyme by replacement of arginine in position 326 in the native sequence, located near the enzyme active center. This labeling had no effect on catalytic activity of the enzyme, but provided possibility to monitor changes in protein structure through measuring the fluorescence spectrum of the dye, which is sensitive to changes in its environment. This method was used to monitor denaturation of the protein kinase catalytic subunit and study the kinetics of this process as well as influence of specific ligands on stability of the protein. Stabilization of the enzyme structure was observed in the presence of adenosine triphosphate, peptide substrate RRYSV and inhibitor peptide PKI[5-24].

Place, publisher, year, edition, pages
2013. Vol. 32, no 7, 519-525 p.
Keyword [en]
cAMP-dependent protein kinase catalytic subunit, Protein denaturation, Fluorescence spectroscopy, Ligand binding, Protein stabilization
National Category
Medical and Health Sciences
URN: urn:nbn:se:uu:diva-211037DOI: 10.1007/s10930-013-9511-4ISI: 000326081300003OAI: oai:DiVA.org:uu-211037DiVA: diva2:665272
Available from: 2013-11-19 Created: 2013-11-19 Last updated: 2013-11-19Bibliographically approved

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Jemth, Per
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