1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states.
The gelation factor from Dictyostelium discoideum (ABP-120) is an actin binding protein consisting of six immunoglobulin (Ig) domains in the C-terminal rod domain. We have recently used the pair of domains 5 and 6 of ABP-120 as a model system for studying multi-domain nascent chain folding on the ribosome. Here we present the NMR assignments of domain 5 in its native and 8M urea-denatured states.
Hsu
Shang-Te Danny
ST
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom. stdh2@cam.ac.uk
Cabrita
Lisa D
LD
Christodoulou
John
J
Dobson
Christopher M
CM
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008840:Microfilament Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D011522:Protons; D014508:Urea / Q000737:chemistry*
D002247:Carbon Isotopes; D002352:Carrier Proteins; D008840:Microfilament Proteins; D009587:Nitrogen Isotopes; D011522:Protons; C060680:abpC protein, Dictyostelium; D014508:Urea