A proton NMR study of ribosomal protein L25 from Escherichia coli.
A highly folded form of the ribosomal protein L25 from Escherichia coli can be obtained from urea-denatured preparations. Proton NMR data show that this form of the molecule must have a compact, globular tertiary structure. Spectroscopically it is indistinguishable from L25 prepared by methods which...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1981
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