Abstract
Recent advances in biophysical methods have been able to shed more light on the structures of helical bundles formed by the transmembrane segments of bitopic membrane proteins. In this manuscript, I attempt to review the biological importance and diversity of these interactions, the energetics of bundle formation, motifs capable of inducing oligomerization and methods capable of detecting, solving and predicting the structures of these oligomeric bundles. Finally, the structures of the best characterized instances of transmembrane α-helical bundles formed by bitopic membrane proteins are described in detail. © 2002 Elsevier Science B.V. All rights reserved.
| Original language | English |
|---|---|
| Pages (from-to) | 347-363 |
| Journal | Biochimica et Biophysica Acta - Biomembranes |
| Volume | 1565 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 11 Oct 2002 |
| Externally published | Yes |
Bibliographical note
Publication details (e.g. title, author(s), publication statuses and dates) are captured on an “AS IS” and “AS AVAILABLE” basis at the time of record harvesting from the data source. Suggestions for further amendments or supplementary information can be sent to [email protected].Research Keywords
- α-Helix
- Bitopic membrane protein
- Oligomerization
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