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

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

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)167-169
Number of pages3
JournalBiomolecular NMR Assignments
Volume1
Issue number2
DOIs
StatePublished - Dec 1 2007

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Keywords

  • Endosulfine alpha
  • Intrinsically unstructured protein
  • Protein folding

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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