(1)H, (13)C, and (15)N resonance assignment of the cAMP-regulated phosphoprotein endosulfine-alpha in free and micelle-bound states.
(13)C, (15)N, and (1)H 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.
Boettcher
John M
JM
Department of Chemistry, University of Illinois at Urbana-Champaign, 61801, USA.
Hartman
Kevin L
KL
Ladror
Daniel T
DT
Qi
Zhi
Z
Woods
Wendy S
WS
George
Julia M
JM
Rienstra
Chad M
CM
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D000242:Cyclic AMP / Q000737:chemistry*; D036341:Intercellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008823:Micelles; D009587:Nitrogen Isotopes / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D010750:Phosphoproteins / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011522:Protons
D002247:Carbon Isotopes; D036341:Intercellular Signaling Peptides and Proteins; D008823:Micelles; D009587:Nitrogen Isotopes; D010455:Peptides; D010750:Phosphoproteins; D011522:Protons; C075663:endosulfine; D000242:Cyclic AMP