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

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 ...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MPLS, Plant Sciences
Role:
Author
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

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