Accessibility of proteins in 50S ribosomal subunits of Escherichia coli to antibodies: An ultracentrifugation study
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics,Molecular Biology
Link
http://link.springer.com/content/pdf/10.1007/BF00268787.pdf
Reference40 articles.
1. Chang, F.N., Flaks, J.G.: Topography of the Escherichia coli ribosome. II. Preliminary sequence of 50S subunit protein attack by trypsin and its correlation with functional activities. J. molec. Biol. 61, 387–400 (1971)
2. Cotter, R.I., Gratzer, W.B.: Accessibility of RNA and protein in the ribosome. Investigation by hydrogen exchange and solvent perturbation. Europ. J. Biochem. 23, 468–474 (1971)
3. Crichton, R.R., Wittmann, H.G.: Trypsin digestion as a possible probe of the conformation of Escherichia coli ribosomes. Molec. gen. Genet. 114, 95–105 (1971)
4. Crichton, R.R., Wittmann, H.G.: A native ribonucleoprotein complex from Escherichia coli ribosomes. Proc. nat. Acad. Sci. (Wash.) 70, 665–668 (1973)
5. Highland, J.H., Gordon, J., Bodley, J., Hasenbank, R., Stöffler, G.: Inhibition of elongation factor G by antibodies specific for several ribosomal proteins. Proc. nat. Acad. Sci. (Wash.) 70, 147–150 (1973)
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