1H, 13C, and 15N resonance assignment of the cAMP-regulated phosphoprotein endosulfine-alpha in free and micelle-bound states期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

1H, 13C, and 15N resonance assignment of the cAMP-regulated phosphoprotein endosulfine-alpha in free and micelle-bound states

Authors:	John M. Boettcher Kevin L. Hartman Daniel T. Ladror Zhi Qi Wendy S. Woods Julia M. George Chad M. Rienstra

Affiliation:	(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

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.

Keywords:	Endosulfine alpha Intrinsically unstructured protein Protein folding
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