Do Small Headgroups of Phosphatidylethanolamine and Phosphatidic Acid Lead to a Similar Folding Pattern of the K+ Channel?
| Autor: | Mobeen Raja |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Hydrogen bonding
Protein Folding Potassium Channels Lipid bilayers Physiology Biophysics KcsA potassium channel Protein–lipid interaction Phosphatidic Acids Article chemistry.chemical_compound Bacterial Proteins Phosphatidic acid Escherichia coli Lipid bilayer Phosphatidylethanolamine Quenching (fluorescence) Chemistry Phosphatidylethanolamines Membrane Proteins Cell Biology Folding (chemistry) Assembly and stability Biochemistry Protein folding lipids (amino acids peptides and proteins) |
| Zdroj: | The Journal of Membrane Biology |
| ISSN: | 1432-1424 0022-2631 |
| Popis: | Phospholipid headgroups act as major determinants in proper folding of oligomeric membrane proteins. The K(+)-channel KcsA is the most popular model protein among these complexes. The presence of zwitterionic nonbilayer lipid phosphatidylethanolamine (PE) is crucial for efficient tetramerization and stabilization of KcsA in a lipid bilayer. In this study, the influence of PE on KcsA folding properties was analyzed by tryptophan fluorescence and acrylamide quenching experiments and compared with the effect of anionic phosphatidic acid (PA). The preliminary studies suggest that the small size and hydrogen bonding capability of the PE headgroup influences KcsA folding via a mechanism quite similar to that observed for anionic PA. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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