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GXXXG-Mediated Parallel and Antiparallel Dimerization of Transmembrane Helices and Its Inhibition by Cholesterol: Single-Pair FRET and 2D IR Studies
| Content Provider | Scilit |
|---|---|
| Author | Yano, Yoshiaki Kondo, Kotaro Watanabe, Yuta Zhang, Tianqi O. Ho, Jia-Jung Oishi, Shinya Fujii, Nobutaka Zanni, Martin T. Matsuzaki, Katsumi |
| Copyright Year | 2017 |
| Description | Journal: Angewandte Chemie International Edition Small‐residue‐mediated interhelical packings are ubiquitously found in helical membrane proteins, although their interaction dynamics and lipid dependence remain mostly uncharacterized. We used a single‐pair FRET technique to examine the effect of a GXXXG motif on the association of de novo designed $(AALALAA)_{3}$ helices in liposomes. Dimerization occurred with sub‐second lifetimes, which was abolished by cholesterol. Utilizing the nearly instantaneous time‐resolution of 2D IR spectroscopy, parallel and antiparallel helix associations were identified by vibrational couplings across helices at their interface. Taken together, the data illustrate that the GXXXG motif controls helix packing but still allows for a dynamic and lipid‐regulated oligomeric state. |
| Related Links | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5507574/pdf |
| Ending Page | 1759 |
| Page Count | 4 |
| Starting Page | 1756 |
| ISSN | 14337851 |
| e-ISSN | 15213773 |
| DOI | 10.1002/anie.201609708 |
| Journal | Angewandte Chemie International Edition |
| Issue Number | 7 |
| Volume Number | 56 |
| Language | English |
| Publisher | Wiley-Blackwell |
| Publisher Date | 2017-01-10 |
| Access Restriction | Open |
| Subject Keyword | Journal: Angewandte Chemie International Edition Gxxxg Motif Ir Spectroscopy Membrane Proteins Single-molecule Studies |
| Content Type | Text |
| Resource Type | Article |
| Subject | Chemistry Catalysis |
