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Biophysical studies of membrane proteins/peptides. Interaction with ...

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2.2. – Peptides as models<br />

2.3. – Amphipatic helix<br />

2.4. – Peptide partitioning to the <strong>membrane</strong><br />

2.5. – Anchoring <strong>of</strong> trans<strong>membrane</strong> domains<br />

2.6. – Lipid-protein hydrophobic mismatch<br />

2.7. – Trans<strong>membrane</strong> protein-lipid interface<br />

2.8. – Lipid selectivity at protein interfaces<br />

2.9. – Lipid phase preferential partition <strong>of</strong> <strong>membrane</strong> <strong>proteins</strong><br />

2.10. – Lipid sorting by <strong>proteins</strong> and formation <strong>of</strong> lipid domains<br />

2.11. – Lipid-mediation <strong>of</strong> protein-protein interactions<br />

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II – PROTEIN-PROTEIN AND PROTEIN-LIPID INTERACTIONS<br />

OF M13 MAJOR COAT PROTEIN<br />

1. – Introduction<br />

2. – Dependence <strong>of</strong> M13 Major Coat Protein Oligomerization and Lateral<br />

Segregation on Bilayer Composition<br />

3. – Quantification <strong>of</strong> Protein-Lipid Selectivity Using FRET: Application to<br />

the M13 MCP<br />

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III – BINDING OF INHIBITORS TO A PUTATIVE BINDING<br />

DOMAIN OF V-ATPase<br />

1. – Introduction<br />

2. – <strong>Interaction</strong> <strong>of</strong> the Indole Class <strong>of</strong> Vacuolar H + -ATPase Inhibitors <strong>with</strong><br />

Lipid Bilayers<br />

3. – Binding Assays <strong>of</strong> Inhibitors Towards Selected V-ATPase Domains<br />

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IV – BINDING OF A QUINOLONE ANTIBIOTIC TO BACTERIAL<br />

PORIN OmpF<br />

1. – Introduction<br />

2. – Cipr<strong>of</strong>loxacin <strong>Interaction</strong>s With Bacterial Protein OmpF: Modelling <strong>of</strong><br />

FRET From a Multi-Tryptophan Protein Trimer<br />

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