1H, 13C, and 15N resonance assignment of the cAMP-regulated phosphoprotein endosulfine-alpha in free and micelle-bound states |
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| Authors: | John M Boettcher Kevin L Hartman Daniel T Ladror Zhi Qi Wendy S Woods Julia M George Chad M Rienstra |
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| Institution: | (1) Department of Chemistry, University of Illinois at Urbana-Champaign, 600 S Mathews Avenue, Box 50-6, Urbana, IL 61801, USA;(2) Center for Biophysics and Computational Biology, University of Illinois, Urbana, IL 61801, USA;(3) Department of Molecular and Integrative Physiology, University of Illinois, Urbana, IL 61801, USA;(4) Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA |
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| Abstract: | 13C, 15N, and 1H chemical shift assignments are presented for the cAMP-regulated phosphoprotein endosulfine-alpha in its free and micelle-bound
states. Secondary chemical shift analysis demonstrates formation of four helices in the micelle-bound state, which are not
present in the absence of detergent. |
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| Keywords: | Endosulfine alpha Intrinsically unstructured protein Protein folding |
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