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...

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Main Authors: Kime, M, Ratcliffe, R, Moore, P, Williams, R
格式: Journal article
语言:English
出版: 1981