Shapes of proteins L1, L9, L25, and L30 from the 50S subunit of the Escherichia coli ribosome, determined by hydrodynamic studies (original) (raw)
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Proteins L1, L9, L25, and L30 from the 50S ribosomal subunit of Escherichia coli A19 were purified and characterized through hydrodynamic studies. The research highlights the sedimentation coefficients, diffusion coefficients, and intrinsic viscosity values of these proteins, revealing L1 and L9 to be globular or slightly elongated, while L25 and L30 display distinctly globular shapes. The findings contribute to the understanding of ribosomal protein structures and their potential interactions with RNA.
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Shape of protein L11 from the 50S ribosomal subunit of Escherichia coli
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Effects of compact volume and chain stiffness on the conformations of native proteins
Proceedings of the National Academy of Sciences, 1992
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