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. 1978 Oct;5(10):3579–3587. doi: 10.1093/nar/5.10.3579

Small-angle X-ray titration of the complex formed between the ribosomal protein S4 and its 16S binding site, S4-RNA: a central core in the 30S subunit.

R Osterberg, B Sjöberg, R A Garrett, J Littlechild
PMCID: PMC342696  PMID: 364415

Abstract

X-ray scattering titrations at 21 degree C and in ribosomal reconstitution buffer indicate that the S4-RNA and the protein S4 from a 1:1 complex with a stability constant, log K approximately 6.5. When the complex forms, there is only a limited change in the scattering curve indicating that S4-RNA essentially retains its conformation during the complex formation. The increase in the gyration radius as a result of the complex formation, delta R = 4 +/- 3 A, as well as the experimental scattering curve of the complex can be explained by models where the protein S4 is supposed to interact with the periphery of the S4-RNA.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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