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核糖体蛋白S4与其16S结合位点S4-RNA形成的复合物的小角X射线滴定:30S亚基中的一个核心。

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.

作者信息

Osterberg R, Sjöberg B, Garrett R A, Littlechild J

出版信息

Nucleic Acids Res. 1978 Oct;5(10):3579-87. doi: 10.1093/nar/5.10.3579.

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.

摘要

在21摄氏度以及核糖体重构缓冲液中进行的X射线散射滴定表明,S4-RNA与蛋白质S4形成了1:1复合物,其稳定常数log K约为6.5。当复合物形成时,散射曲线仅有有限的变化,这表明S4-RNA在复合物形成过程中基本保持其构象。复合物形成导致的回转半径增加,ΔR = 4 ± 3 Å,以及复合物的实验散射曲线,可以通过蛋白质S4与S4-RNA外周相互作用的模型来解释。

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引用本文的文献

本文引用的文献

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X-RAY SMALL ANGLE SCATTERING WITH SUBSTANCES OF BIOLOGICAL INTEREST IN DILUTED SOLUTIONS.
Prog Biophys Mol Biol. 1963;13:105-73. doi: 10.1016/s0079-6107(63)80015-2.
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[Small-angle x-ray scattering study of fatty acid synthetase from yeast].
Eur J Biochem. 1970 Mar 1;13(1):55-64. doi: 10.1111/j.1432-1033.1970.tb00898.x.
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Small angle x-ray scattering of a homogeneous gamm G-1 immunoglobulin.
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