Title data
Klostermeier, Dagmar ; Bayer, Peter ; Kraft, Margot ; Frank, Rainer W. ; Rösch, Paul:
Spectroscopic investigations of HIV-1 trans-activator and related peptides in aqueous solutions.
In: Biophysical Chemistry.
Vol. 63
(1997)
Issue 2-3
.
- pp. 87-96.
ISSN 1873-4200
DOI: https://doi.org/10.1016/S0301-4622(96)02243-0
Abstract in another language
The 86 amino acid trans-activator (Tat) protein of human immunodeficiency virus type 1 (HIV-1) is an RNA-binding transcriptional regulator. HIV-1 Tat proteins (wild type and Thr40Lys mutant) and the HIV-1 Tat peptide fragments Tat(32-48) and Tat(32-72) were chemically synthesized. One- and two-dimensional nuclear magnetic resonance spectroscopy experiments were performed to elucidate the structural features of these proteins. In fluorescence quenching studies of the full-length Tat protein (Thr40Lys), Trp11 was found to be only partially protected against solvent accessibility. Circular dichroism melting studies monitored a slight cooperative change in the conformation of the Tat with increasing temperature. Backbone NH protons of amino acids located in the main core element of the protein are partially protected against exchange.
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: | 15 Jan 2019 13:24 |
Last Modified: | 31 Mar 2022 13:37 |
URI: | https://eref.uni-bayreuth.de/id/eprint/46901 |