A Proton NMR Study of Ribosomal Protein L25 from Escherichia coli
- 1 May 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 116 (2) , 269-276
- https://doi.org/10.1111/j.1432-1033.1981.tb05329.x
Abstract
A highly folded form of the ribosomal protein L25 from E. coli can be obtained from unrea-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 number of resonances in its NMR spectrum. This folded form of the protein can be characterized using NMR spectroscopy. High-resolution NMR spectroscopy provides a sensitive and general way for the characterization of protein folds.This publication has 24 references indexed in Scilit:
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