Lipids do influence protein function-the hydrophobic matching hypothesis revisited
| Autor: | Ole G. Mouritsen, Morten Ø. Jensen |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Protein Folding
Trans-membrane peptide Lipid Bilayers Biophysics Water channel protein Lipid order parameter Chain tilt Curvature Molecular Dynamics Biochemistry Structure–function relationship Lipid bilayer Integral membrane protein Molecular dynamics Membrane Lipids Gramicidin A Lipid domain Curvature stress Water transport Chemistry Membrane raft Membrane Proteins Hydrophobic thickness Cell Biology Models Theoretical Crystallography Theory of lipid–protein interactions Membrane Hydrophobic matching Protein folding lipids (amino acids peptides and proteins) Protein insertion Hydrophobic and Hydrophilic Interactions Protein Binding |
| Zdroj: | Biochimica et biophysica acta. 1666(1-2) |
| ISSN: | 0006-3002 |
| Popis: | A topical review of the current state of lipid–protein interactions is given with focus on the physical interactions between lipids and integral proteins in lipid-bilayer membranes. The concepts of hydrophobic matching and curvature stress are revisited in light of recent data obtained from experimental and theoretical studies which demonstrate that not only do integral proteins perturb the lipids, but the physical state of the lipids does also actively influence protein function. The case of the trans-membrane water-channel protein aquaporin GlpF from E. coli imbedded in lipid-bilayer membranes is discussed in some detail. Numerical data obtained from Molecular Dynamics simulations show on the one side that the lipid bilayer adapts to the channel by a hydrophobic matching condition which reflects the propensity of the lipid molecules for forming curved structures. On the other side, it is demonstrated that the transport function of the channel is modulated by the matching condition and/or the curvature stress in a lipid-specific manner. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|