BIBLIOGRAPHY Sperotto, M. M., and Mouritsen, O. G.(1991). Monte Carlo Simulation Studies <strong>of</strong> Lipid Order Parameter Pr<strong>of</strong>iles Near Integral Membrane Proteins. Biochemistry 59: 261-270. Spruijt, R., and Hemminga, M. A. (1991). The in Situ Aggregational and Conformational State <strong>of</strong> the Major Coat Protein <strong>of</strong> Bacteriophage M13 in Phospholipid Bilayers Mimicking the Inner Membrane <strong>of</strong> Host Escherichia Coli. Biochemistry 30: 11147-11154. Spruijt, R., Wolfs, C., and Hemminga, M. (1999). M13 Phage. in “Encyclopedia <strong>of</strong> Molecular Biology.” (Ed. Creighton, T. E.), Wiley-Interscience, New York, U.S.A. Spuijt, R. B., Wolfs, C. J. A. M., Verveer, J. W. G., and Hemminga, M. (1996). Putative Trans<strong>membrane</strong> Domain <strong>of</strong> the Major Coat Protein <strong>of</strong> Bacteriophage M13. Biochemistry 35: 10383-10391. Stahlmannn, R., and Lode, H. (1999). Toxicity <strong>of</strong> Quinolones. Drugs 58: 37-42. Stopar, D., Jansen, K. A. J., Páli, T., Marsh, D., and Hemminga, M. A. (1997a). Membrane Location <strong>of</strong> Spin-Labeled M13 Major Coat Proteins Determined by Paramagnetic Relaxation Agents. Biochemistry 36: 8261-8268. Stopar, D., Spruijt, R., Wolfs, C. J. A. M., and Hemminga, M. A. (1997b). In Situ Aggregational State <strong>of</strong> M13 Bacteriophage Major Coat Protein in Sodium Cholate and Lipid Bilayers. Biochemistry 36: 12268- 12275. Stopar, D., Spruijt, R., Wolfs, C. J. A. M., and Hemminga, M. A. (1998). Mimicking Initial <strong>Interaction</strong>s <strong>of</strong> Bacteriophage M13 Coat Protein Disassembly in Model Membrane Systems. Biochemistry 37: 10181- 10187. Stopar, D., Spruijt, R., Wolfs, C. J. A. M., and Hemminga, M. A. (2003). Protein-Lipid <strong>Interaction</strong>s <strong>of</strong> Bacteriophage M13 Major Coat Protein. Biochim. Biophys. Acta 78451: 1-11. Takei, K., Haucke, V., Slepnev, V., Farsad, K., Salazar, M., Chen, H. and De Camilli, P. (1998). Generation <strong>of</strong> Coated Intermediates <strong>of</strong> Clathrin-Mediated Endocytosis on Protein-Free Liposomes. Cell 94: 131-141. Takei, K., Slepnev, V. I., Haucke, V., and De Camilli, P. (1999). Functional Partnership Between Amphiphysin and Dynamin in Clathrin-Mediated Endocytosis. Nat. Cell Biol. 1:33-39. Tanford, C. (1980). The Hydrophobic Effect. Wiley, New York, USA. Taylor, J. W. (1990). Peptide Models <strong>of</strong> dynorphin A(1-17) Incorporating Minimally Homologous Substitutes for the Potential Amphiphilic β-Strand in Residues 7-15. Biochemistry 29: 5364-5373 Taylor, A. H., Heavner, G., Nedelman, M., Sherris, D., Brunt, E., Knight, D., and Ghrayeb, J. (1995). Lipopolysaccharide (LPS) Neutralizing Peptides Reveal a Lipid A Binding Site <strong>of</strong> LPS Binding Protein. 203
J. Biol. Chem. 270: 17934-17938. Teitelbaum, S. L. (2000). Bone Resorption by Osteoclasts. Science 289: 1504-1508. van Rheenen, J., Achame, M. E., Janssen, H., Calafat, J., and Jalink, K. (2005). PIP 2 Signaling in Lipid Domains: A Critical Re-evaluation. EMBO J. 24: 1664-1673. Väänänen, K. (2005). Mechanism <strong>of</strong> osteoclast mediated bone resorption—rationale for the design <strong>of</strong> new therapeutics. Adv. Drug Deliv. Rev. 57: 959-971 Vázquez, J. L., Merino, S., Domenech, Ò, Berlanga, M., Viñas, M., Montero, M. T., and Hernández- Borrell, J. (2001). Determination <strong>of</strong> the Partition Coefficients <strong>of</strong> a Homologous Series <strong>of</strong> Cipr<strong>of</strong>loxacin: Influence <strong>of</strong> the N-4 Piperazinyl Alkylation on the Antimicrobial Activity. Int. J. Pharm. 220: 53-62. Visentin, L., Dodds, L. A., Valente, M., Misiano, P., Bradbeer, J. N., Oneta, S., Liang, X., Gowen, M., and Farina, C. (2000). A Selective Inhibitor <strong>of</strong> the Osteoclastic V-H + -ATPase Prevents Bone Loss in Both Thyroparathyroidectomized and Ovariectomized Rats. J. Clin. Invest. 103: 309-318. Wallin, E., Tsukihara, T., Yoshikawa, S., von Heijne, G., and El<strong>of</strong>sson, A. (1997). Architecture <strong>of</strong> Helix Bundle Membrane Proteins. An Analysis <strong>of</strong> Cytochrome c Oxidase from Bovine Mitochondria. Protein Sci. 6: 808-815. Wang, J., Arbuzova, A., Hangyás-Milhályné, G., and McLaughlin, S. (2001). The Effector Domain <strong>of</strong> Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-Bisphosphate. J. Biol. Chem. 276: 5012-5019. Webb, M. S., Hui, S. W., and Steponkus, P. L. (1993). Dehydration Induced Lamellar-to-Hexagonal-II Phase Transitions in DOPE/DOPC Mixtures. Biochim. Biophys. Acta. 1145:93-104. Weiss, T. M., van der Wel, P. C. A., Killian, J. A., Koeppe II, R. E., and Huang, H. W. (2003). Hydrophobic Mismatch between Helices and Lipid Bilayers. Biophys. J. 84: 379-385. White, S. H., and Wimley, W. C. (1999). Membrane Protein Folding and Stability: Physical Principles. Annu. Rev. Biophys. Biomol. Struct. 28: 319-365. Whyteside, G., Meek, P. J., Ball, S. K., Dixon, N., Finbow, M. E., Kee, T. P., Findlay, J. B. C., and Harrison, M .A. (2005). Concanamycin and Indolyl Pentadieneamide Inhibitors <strong>of</strong> the Vacuolar H+- ATPase Bind <strong>with</strong> High Affinity to the Purified Proteolipid Subunit <strong>of</strong> the Membrane Domain. Biochemistry. 44: 15024-15031. Wiener, M. C., and White, S. H. (1992). Structure <strong>of</strong> a Fluid Dioleoylphosphatidylcholine Bilayer Determined by Joint Refinement <strong>of</strong> X-Ray and Neutron Diffraction Data. III. Complete Structure. Biophys. J. 61:434-447. 204
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UNIVERSIDADE TÉCNICA DE LISBOA INS
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Fernandes, F., Loura, L. M. S., Fed
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Ao Pedro e Hugo, amigos de longa da
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2.2. - Peptides as models 2.3. - Am
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ABBREVIATIONS AND SYMBOL LIST ABBRE
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RESUMO RESUMO As biomembranas são
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SINOPSE SINOPSE Nas últimas duas d
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SINOPSE podem fornecer informação
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SINOPSE aceitantes. Dadores mais pr
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OUTLINE OUTLINE The last two decade
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OUTLINE membranes with a distributi
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OUTLINE BAR domains (tubulation of
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ion diffusion, as the energy requir
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acid. If no more groups are linked
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sphingomyelin, the most abundant sp
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signal for neighbouring cells to ph
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functional role in process such as
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in the L α phase, while lateral di
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1.7. Lateral heterogeneity in lipid
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the vesicle through bilayer deforma
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Figure I.9 - Depiction of the sever
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Figure I.11 - Experimentally obtain
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drying into a film and ressuspensio
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deactivating agents. Zwitterionic d
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amphipatic helices (see Section 2.3
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size corresponding to the hydrophob
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changes abruptly in the interfacial
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thickness of the bilayer (Section 1
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some α-helical membrane proteins a
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The formation of a lipid population
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homogeneous distribution of lipids
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Figure I.20 - Relative binding cons
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2.9. Lipid phase preferential parti
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In Figure I.21, theoretical simulat
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PROTEIN-PROTEIN AND PROTEIN-LIPID I
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PROTEIN-PROTEIN AND PROTEIN-LIPID I
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PROTEIN-PROTEIN AND PROTEIN-LIPID I
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2430 Biophysical Journal Volume 85
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2432 Fernandes et al. Coat protein
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2434 Fernandes et al. leads to an a
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2436 Fernandes et al. FIGURE 4 (A)
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2438 Fernandes et al. section of th
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2440 Fernandes et al. tein oligomer
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QUANTIFICATION OF PROTEIN-LIPID SEL
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FRET Study of Protein-Lipid Selecti
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FRET Study of Protein-Lipid Selecti
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FRET Study of Protein-Lipid Selecti
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FRET Study of Protein-Lipid Selecti
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BINDING OF INHIBITORS TO A PUTATIVE
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BINDING OF INHIBITORS TO A PUTATIVE
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INTERACTION OF THE INDOLE CLASS OF
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5272 Biochemistry, Vol. 45, No. 16,
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5274 Biochemistry, Vol. 45, No. 16,
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5276 Biochemistry, Vol. 45, No. 16,
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5278 Biochemistry, Vol. 45, No. 16,
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BINDING ASSAYS OF INHIBITORS TOWARD
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1778 F. Fernandes et al. / Biochimi
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1780 F. Fernandes et al. / Biochimi
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1782 F. Fernandes et al. / Biochimi
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1784 F. Fernandes et al. / Biochimi
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1786 F. Fernandes et al. / Biochimi
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apparently the most significant as
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110
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Introduction Quinolones are broad-s
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[9-12]. Having this into considerat
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any case, very similar, probably wi
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placement of the protein around the
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⎛ II t ⎛ R ⎞ 0 ρ () t = exp
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APPENDIX - Derivation of the FRET r
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2 2w J ( t) = '2 R − R + w / 1
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[14] L. Plançon, M. Chami, L. Lete
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acceptors) (Eqs. 4-6) (⋅-⋅-⋅)
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FIGURE 1A FIGURE 1B 130
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FIGURE 4A FIGURE 4B 132
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FIGURE 6A FIGURE 6B 134
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136
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dynamin. Soon after, the same group
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140
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142
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Introduction Control of membrane re
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Steady-state fluorescence measureme
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Rho-DOPE (acceptor). The increase o
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- Page 216 and 217: BIBLIOGRAPHY IX BIBLIOGRAPHY Albert
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- Page 224 and 225: BIBLIOGRAPHY Mishra, V. K., Palguna
- Page 226 and 227: BIBLIOGRAPHY Pluschke, G., Hirota,
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