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Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.

Abstract:

15N NOE, T1, and T2 measurements have been carried out on uniformly 15N-labeled human interleukin-4. Analysis of the results in terms of order parameters (S2) shows that although the helical core of this four-helix-bundle protein exists as a well-defined structure with limited conformational flexibility (S2 congruent to 0.9), other regions of the molecule experience substantial fluctuations in the conformation of the main chain (S2 = 0.3-0.8). These regions include both the N- and C-termini a...

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Publication status:
Published

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Publisher copy:
10.1021/bi00158a003

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Biochemistry
Volume:
31
Issue:
43
Pages:
10431-10437
Publication date:
1992-11-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:952ab4f7-974c-490a-9d8b-921df3026893
Source identifiers:
32487
Local pid:
pubs:32487

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