1H, 15N, 13C resonance assignment of folded and 8 M urea-denatured state of SUMO from Drosophila melanogaster.
SUMO, an important post-translational modifier of variety of substrate proteins, regulates different cellular functions. Here, we report the NMR resonance assignment of the folded and 8 M urea-denatured state of SUMO from Drosophila melanogaster (dsmt3).
Kumar
Dinesh
D
Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai, 400005, India.
Kumar
Ashutosh
A
Misra
Jyoti Ranjan
JR
Chugh
Jeetender
J
Sharma
Shilpy
S
Hosur
Ramakrishna V
RV
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D029721:Drosophila Proteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D011489:Protein Denaturation; D011522:Protons; D025842:SUMO-1 Protein / Q000737:chemistry*; D014508:Urea / Q000737:chemistry*
D002247:Carbon Isotopes; D029721:Drosophila Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D025842:SUMO-1 Protein; D014508:Urea