Abstract
As part of our NMR structure determination of the Human S100A1, we report nearly complete NMR chemical shift assignments for the 1H, 13C and 15N nuclei.
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Cornilescu G, Delagio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13:289–302
Ejchart A, Jaremko L, Jaremko M, Zhukov I, Agnieszka B, Bierzynski A (2011) Solution NMR structure and dynamics of human apo-S100A1 protein. J Struct Biol 171:391–399
Heizmann CW, Fritz G, Schafer BW (2004) S100 proteins: structure, functions and pathology. Front. Biosci 7:d1356–d1368
Leclerc E, Heizmann CW (2011) The importance of Ca2 +/Zn2 + signaling S100 proteins and RAGE in translational medicine. Front Biosci S3:1232–1262
Pietzsch J, Hoppmann S, Haase C, Richter S (2008) Expression, purification and fluorine-18 radiolabeling of recombinant S100 proteins—potential probes for molecular imaging of receptor for advanced glycation end products (RAGE) in vivo. Protein Expr Purif 57:143–152
Wishart DS, Sykes BD (1994) The 13C chemical shift index: as simple method for the identification of protein secondary structure using 13C chemical shift data. J Biomol NMR 4:171–180
Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD (1995) 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135–140
Acknowledgments
Work in our laboratory is supported by Grant from the National Science Council (NSC) Taiwan (NSC—100-2113-M007-012-MY3).
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Gupta, A.A., Mohan, S.K. & Chin, Y. 1H, 13C and 15N backbone and side chain resonance assignments of human halo S100A1. Biomol NMR Assign 6, 213–215 (2012). https://doi.org/10.1007/s12104-012-9360-7
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DOI: https://doi.org/10.1007/s12104-012-9360-7