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

doi:10.1007/s12104-007-9063-7

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 journal › Article › peer-review

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 language	English (US)
Pages (from-to)	167-169
Number of pages	3
Journal	Biomolecular NMR Assignments
Volume	1
Issue number	2
DOIs	https://doi.org/10.1007/s12104-007-9063-7
State	Published - Dec 2007

Keywords

Endosulfine alpha
Intrinsically unstructured protein
Protein folding

ASJC Scopus subject areas

Structural Biology
Biochemistry

Online availability

10.1007/s12104-007-9063-7

Library availability

Discover UIUC Full Text

Cite this

@article{3b2e6883dd4c401c8a3cda9ebff68dfd,

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

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",

author = "Boettcher, {John M.} and Hartman, {Kevin L.} and Ladror, {Daniel T.} and Zhi Qi and Woods, {Wendy S.} and George, {Julia M.} and Rienstra, {Chad M.}",

note = "Funding Information: Acknowledgments This work was supported by the University of Illinois (startup funds to C.M.R.) and the Research Corporation (Cottrell Scholars Award to C.M.R.).",

year = "2007",

month = dec,

doi = "10.1007/s12104-007-9063-7",

language = "English (US)",

volume = "1",

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journal = "Biomolecular NMR Assignments",

issn = "1874-2718",

publisher = "Springer",

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T1 - 1H, 13C, and 15N resonance assignment of the cAMP-regulated phosphoprotein endosulfine-alpha in free and micelle-bound states

AU - Boettcher, John M.

AU - Hartman, Kevin L.

AU - Ladror, Daniel T.

AU - Qi, Zhi

AU - Woods, Wendy S.

AU - George, Julia M.

AU - Rienstra, Chad M.

N1 - Funding Information: Acknowledgments This work was supported by the University of Illinois (startup funds to C.M.R.) and the Research Corporation (Cottrell Scholars Award to C.M.R.).

PY - 2007/12

Y1 - 2007/12

N2 - 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.

AB - 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.

KW - Endosulfine alpha

KW - Intrinsically unstructured protein

KW - Protein folding

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