- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi00158a003
-
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- 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
- Language:
- English
- Keywords:
- Copyright date:
- 1992
Journal article
Loop mobility in a four-helix-bundle protein: 15N NMR relaxation measurements on human interleukin-4.
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