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Secondary structure and topology of human interleukin 4 in solution.

Abstract:

Human interleukin 4 (IL-4) has been studied by 2D and 3D NMR techniques using uniformly 15N-labeled recombinant protein. Assignment of resonances for all but 3 of the 130 residues of the recombinant protein has been achieved, enabling the secondary structure of the protein to be defined. This consists of four major alpha-helical regions and one short section of double-stranded antiparallel beta-sheet. Analysis of distance and angle restraints derived from NMR experiments has enabled the overa...

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Publication status:
Published

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Publisher copy:
10.1021/bi00110a004

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
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Journal:
Biochemistry
Volume:
30
Issue:
46
Pages:
11029-11035
Publication date:
1991-11-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:6cdc837c-42ac-4157-a75a-05c341a55880
Source identifiers:
43772
Local pid:
pubs:43772

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