at Google ScholarTitle data
Lauber, Thomas ; Marx, Ute C.:
Prosequence-mediated disulfide coupled folding of the peptide hormones guanylin and uroguanylin.
In: Protein & Peptide Letters.
Vol. 12
(2005)
Issue 2
.
- pp. 153-158.
ISSN 1875-5305
DOI: https://doi.org/10.2174/0929866053005836
Abstract in another language
In contrast to their prohormones the mature peptide hormones guanylin and uroguanylin are not able to fold to their native disulfide connectivities upon oxidative folding. Structural properties of both peptide hormones and their precursor proteins as well as the role of their prosequences in proper disulfide coupled folding are reviewed. In addition, the structural behavior of a proguanylin mutant that closely resembles prouroguanylin has been investigated to gain further insight into structural properties of this homologous precursor protein.
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: | 28 Jan 2019 13:12 |
| Last Modified: | 05 Sep 2022 11:48 |
| URI: | https://eref.uni-bayreuth.de/id/eprint/47067 |