Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop
Author:
Funder
National Institutes of Health
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/article/10.1007/s12104-018-9837-0/fulltext.html
Reference21 articles.
1. Banner DW, Kokkinidis M, Tsernoglou D (1987) Structure of the ColE1 Rop protein at 1.7 Å resolution. J Mol Biol 196:657–675. https://doi.org/10.1016/0022-2836(87)90039-8
2. Comolli LR, Pelton JG, Tinoco I (1998) Mapping of a protein-RNA kissing hairpin interface: Rom and Tar-Tar*. Nucleic Acids Res 26:4688–4695. https://doi.org/10.1093/nar/26.20.4688
3. Delaglio F, Grzesiek S, Vuister GW et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293. https://doi.org/10.1007/BF00197809
4. Eberle W, Pastore A, Sander C, Rösch P (1991) The structure of ColE1 rop in solution. J Biomol NMR 1:71–82. https://doi.org/10.1007/BF01874570
5. Hari SB, Byeon C, Lavinder JJ, Magliery TJ (2010) Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics. Protein Sci 19:670–679. https://doi.org/10.1002/pro.342
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