1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states
- 18 December 2008
- journal article
- Published by Springer Nature in Biomolecular NMR Assignments
- Vol. 3 (1) , 29-31
- https://doi.org/10.1007/s12104-008-9134-4
Abstract
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.Keywords
This publication has 11 references indexed in Scilit:
- Structure and dynamics of a ribosome-bound nascent chain by NMR spectroscopyProceedings of the National Academy of Sciences, 2007
- Filamins: promiscuous organizers of the cytoskeletonPublished by Elsevier ,2006
- Molecular Structure of the Rod Domain of Dictyostelium FilaminJournal of Molecular Biology, 2004
- Mars – robust automatic backbone assignment of proteinsJournal of Biomolecular NMR, 2004
- Three-Dimensional Structures of Translating Ribosomes by Cryo-EMMolecular Cell, 2004
- A mechanical unfolding intermediate in an actin-crosslinking proteinNature Structural & Molecular Biology, 2003
- Structural and functional aspects of filaminsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2001
- Sequence-Dependent Correction of Random Coil NMR Chemical ShiftsJournal of the American Chemical Society, 2001
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- 1H, 13C and 15N chemical shift referencing in biomolecular NMRJournal of Biomolecular NMR, 1995