at Google ScholarTitle data
Sticht, Heinrich ; Willbold, Dieter ; Bayer, Peter ; Ejchart, Andrzej ; Herrmann, Franz ; Rosin-Arbesfeld, Rina ; Gazit, Arnona ; Yaniv, Abraham ; Frank, Rainer ; Rösch, Paul:
Equine infectious anemia virus Tat is a predominantly helical protein.
In: European Journal of Biochemistry.
Vol. 218
(1993)
Issue 3
.
- pp. 973-976.
ISSN 1432-1033
DOI: https://doi.org/10.1111/j.1432-1033.1993.tb18455.x
Abstract in another language
Nuclear magnetic resonance (NMR) spectroscopy revealed features of the secondary structure of the equine infectious anemia virus (EIAV) Tat protein in solution. We could show that this protein, which is required in the replication cycle of lentiviruses, forms a predominantly helical structure in trifluoroethanol/water (40% by vol.) solution. In particular, the basic RNA-binding region and the adjacent core domain, which are highly conserved among lentiviral Tat proteins, show helix-type secondary structure under these conditions. Our observations, in concert with recent biochemical data from other laboratories, suggest that the core sequence region and the basic sequence region form interdependent structural domains, both possibly necessary for correct RNA binding.
Further data
| Item Type: | Article in a journal |
|---|---|
| Refereed: | Yes |
| Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry |
| Result of work at the UBT: | Yes |
| DDC Subjects: | 500 Science > 540 Chemistry 500 Science > 570 Life sciences, biology |
| Date Deposited: | 09 Jan 2019 08:33 |
| Last Modified: | 31 Mar 2022 13:13 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/46836 |