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When urea-denatured preparations of protein L11 from the ribosome of Escherichia coli are introduced into physiological buffers, two completely different configurations can be obtained. One form, by NMR criteria, shows little evidence of stable tertiary interactions; the other shows strong indications of a distinctive folding pattern. The configuration obtained depends on minor details of the method used for returning samples to non-denaturing conditions.


Journal article


Eur J Biochem

Publication Date





493 - 498


Bacterial Proteins, Escherichia coli, Magnetic Resonance Spectroscopy, Protein Conformation, Protein Denaturation, Ribosomal Proteins, Ribosomes, Urea