{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T00:38:38Z","timestamp":1760575118779,"version":"build-2065373602"},"reference-count":33,"publisher":"Wiley","issue":"21","license":[{"start":{"date-parts":[[2006,10,6]],"date-time":"2006-10-06T00:00:00Z","timestamp":1160092800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Electrophoresis"],"published-print":{"date-parts":[[2006,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Characterization of the unfolding dynamics of a recombinant type\u2005IA regulatory subunit (RI\u03b1) of cyclic adenosine monophosphate (cAMP)\u2010dependent protein kinase (cAPK) was examined by CE with UV detection. Electrophoretic separation of RI\u03b1 by CE in a buffer devoid of cAMP resulted in rapid dissociation of the complex from the original sample due to the high negative mobility of the ligand relative to receptor. This process enabled in\u2010capillary generation of cAMP\u2010stripped RI\u03b1, which was used to estimate the apparent dissociation constant (<jats:italic>K<\/jats:italic><jats:sub>d<\/jats:sub>) of 0.6\u00a0\u00b1\u00a00.2\u2005\u03bcM. A comparison of RI\u03b1 dynamic unfolding processes with urea denaturation was performed by CE with (<jats:italic>i.e.<\/jats:italic>, RI\u03b1\u2013cAMP) and without (<jats:italic>i.e.<\/jats:italic>, cAMP\u2010stripped RI\u03b1) excess cAMP in the buffer during electromigration. The presence of cAMP in the buffer confirmed greater stabilization of the protein, as reflected by a higher standard free energy change (\u0394<jats:italic>G<\/jats:italic><jats:sub>U<\/jats:sub>\u00b0) of 10.1\u00a0\u00b1\u00a00.5\u2005kcal\u00b7mol<jats:sup>+1<\/jats:sup> and greater cooperativity in unfolding (<jats:italic>m<\/jats:italic>) of \u22122.30\u00a0\u00b1\u00a00.11\u2005kcal\u00b7mol<jats:sup>\u22121<\/jats:sup>M<jats:sup>\u22121<\/jats:sup>. CE offers a rapid, yet versatile platform for probing the thermodynamics of cAPK and other types of receptor\u2013ligand complexes in free solution.<\/jats:p>","DOI":"10.1002\/elps.200600300","type":"journal-article","created":{"date-parts":[[2006,10,6]],"date-time":"2006-10-06T04:58:46Z","timestamp":1160110726000},"page":"4196-4204","source":"Crossref","is-referenced-by-count":8,"title":["Dynamic unfolding of a regulatory subunit of cAMP\u2010dependent protein kinase by capillary electrophoresis: Impact of cAMP dissociation on protein stability"],"prefix":"10.1002","volume":"27","author":[{"given":"Jennilee M. 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