A proton NMR study of ribosomal protein L25 from Escherichia coli.

Journal article

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 avoid denaturing solvents. Thus L25 is a protein which can be reversibly denatured. The stability and solubility of the folded form of the protein are discussed and primary assignments made for a ...

Expand abstract

Authors: Kime, M; Ratcliffe, R; Moore, P; Williams, R

• Publication status: Published
• Journal: European journal of biochemistry / FEBS
• Volume: 116
• Issue: 2
• Pages: 269-276
• Publication date: 1981-05-01
• DOI: 10.1111/j.1432-1033.1981.tb05329.x
• EISSN: 1432-1033
• ISSN: 0014-2956
• Language: English
• Keywords: Protein Denaturation; Escherichia coli; Drug Stability; Temperature; Hydrogen-Ion Concentration; Ribosomal Proteins; Magnetic Resonance Spectroscopy; Protein Conformation; Fourier Analysis