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Equine infectious anemia virus Tat is a predominantly helical protein

Title 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 (December 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 Biopolymers
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: 16 May 2019 05:37
URI: https://eref.uni-bayreuth.de/id/eprint/46836