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On the renaturation of ribosomal protein L11.

Abstract:
When urea-denatured preparations of protein L11 from the ribosome of Escherichia coli are introduced into physiological buffers, two completely different configurations can be obtained. One form, by NMR criteria, shows little evidence of stable tertiary interactions; the other shows strong indications of a distinctive folding pattern. The configuration obtained depends on minor details of the method used for returning samples to non-denaturing conditions.
Publication status:
Published

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Institution:
University of Oxford
Division:
MPLS
Department:
Plant Sciences
Role:
Author
Journal:
European journal of biochemistry / FEBS
Volume:
110
Issue:
2
Pages:
493-498
Publication date:
1980-09-01
DOI:
EISSN:
1432-1033
ISSN:
0014-2956
Source identifiers:
41889
Language:
English
Keywords:
Pubs id:
pubs:41889
UUID:
uuid:031d8cf0-d3d8-4bfd-984b-e7e272f9f599
Local pid:
pubs:41889
Deposit date:
2012-12-19

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