- Abstract:
-
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 - Publication status:
- Published
- Publisher copy:
- 10.1111/j.1432-1033.1981.tb05329.x
-
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- Journal:
- European journal of biochemistry / FEBS
- Volume:
- 116
- Issue:
- 2
- Pages:
- 269-276
- Publication date:
- 1981-05-05
- DOI:
- EISSN:
-
1432-1033
- ISSN:
-
0014-2956
- URN:
-
uuid:b8721e1a-340f-4bde-a3eb-463c7a2564c9
- Source identifiers:
-
42010
- Local pid:
- pubs:42010
- Copyright date:
- 1981
Journal article
A proton NMR study of ribosomal protein L25 from Escherichia coli.
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