Experimentally determined hydrophobicity scale for proteins at membrane interfaces (original) (raw)
Shai, Y. Pardaxin: Channel formation by a shark repellant peptide from fish. Toxicology87, 109–129 (1994). ArticleCAS Google Scholar
Maloy, W.L. & Kari, U.P. Structure-activity studies on magainins and other host defense peptides. Biopolymers37, 105–122 (1995). ArticleCAS Google Scholar
Wickner, W. Mechanisms of membrane assembly: general lessons from the study of M13 coat protein and escherichia coli leader peptidase. Biochemistry27, 1081–1086 (1988). ArticleCAS Google Scholar
Schatz, G. & Dobberstein, B. Common principles of protein translocation across membranes. Science271, 1519–1526 (1996). ArticleCAS Google Scholar
Jacobs, R.E. & White, S.H. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry28, 3421–3437 (1989). ArticleCAS Google Scholar
Wimley, W.C., Creamer, T.P. & White, S.H. Solvation energies of amino acid sidechains and backbone in a family of host-guest pentapeptides. Biochemistry35, 5109–5124 (1996). ArticleCAS Google Scholar
Wimley, W.C., Gawrisch, K., Creamer, T.P. & White, S.H. A direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability. Proc. Natl. Acad. Sci. USA93, 2985–2990 (1996). ArticleCAS Google Scholar
Fauchère, J.-L. & Pliska, V. Hydrophobic parameters of pi amino-acid side chains from the partitioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem. Chim. Ther.18, 369–375 (1983). Google Scholar
Radzicka, A. & Wolfenden, R. Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, l-octanol, and neutral aqueous solution. Biochemistry27, 1664–1670 (1988). ArticleCAS Google Scholar
Kim, A. & Szoka, F.C. Amino acid side-chain contributions to free energy of transfer of tripeptides from water to octanol. Pharm. Res.9, 504–514 (1992). ArticleCAS Google Scholar
Wiener, M.C. & White, S.H. Structure of a fluid dioleoylphospha tidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys. J.61, 434–447 (1992). ArticleCAS Google Scholar
Brown, J.W. & Huestis, W.H. Structure and orientation of a bilayer-bound model tripeptide: A 1H NMR study. J. Phys. Chem.97, 2967–2973 (1993). ArticleCAS Google Scholar
Roseman, M.A. Hydrophobicity of the peptide C=O…H-N Hydrogen-bonded Group. J. Mol. Biol.201, 621–625 (1988). ArticleCAS Google Scholar
Wimley, W.C. & White, S.H. Quantitation of electrostatic and hydrophobic membrane interactions by equilibrium dialysis and reverse-phase HPLC. Anal. Biochem.213, 213–217 (1993). ArticleCAS Google Scholar
Wimley, W.C. & White, S.H. Membrane partitioning: Distinguishing bilayer effects from the hydrophobic effect. Biochemistry32, 6307–6312 (1993). ArticleCAS Google Scholar
Segrest, J.P. et al. The amphipathic helix in the exchangeable apolipoproteins - A review of secondary structure and function. J. Lipid Res.33, 141–166 (1992). CASPubMed Google Scholar
Schwyzer, R. Conformations and orientations of amphiphilic peptides induced by artificial lipid membranes: Correlations with biological activity. Chemtracts-Biochem. Mol. Biol.3, 347–379 (1992). CAS Google Scholar
Killian, J.A., Timmermans, J.W., Keur, S. & DeKruiff, B. The tryptophans of gramicidin are essential for the lipid structure modulating effect of the peptide. Biochim. Biophys. Acta820, 154–156 (1985). ArticleCAS Google Scholar
Hu, W., Lee, K.C. & Cross, T.A. Tryptophans in membrane proteins -indole ring orientations and functional implications in the gramicidin channel. Biochemistry32, 7035–7047 (1993). ArticleCAS Google Scholar
Koeppe, R.E., Killian, J.A. & Greathouse, D.V. Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy. Biophys. J.66, 14–24 (1994). ArticleCAS Google Scholar
Landolt-Marticorena, C., Williams, K.A., Deber, C.M. & Reithmeier, R.A.F. Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J. Mol. Biol.229, 602–608 (1993). ArticleCAS Google Scholar
Schiffer, M., Chang, C.H. & Stevens, F.J. The functions of tryptophan residues in membrane proteins. Protein Eng.5, 213–214 (1992). ArticleCAS Google Scholar
Kyte, J. & Doolittle, R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol.157, 105–132 (1982). ArticleCAS Google Scholar
Engelman, D.M., Steitz, T.A. & Goldman, A. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys, Biophys. Chem.15, 321–353 (1986). ArticleCAS Google Scholar
Eisenberg, D. & McLachlan, A.D. Solvation energy in protein folding and binding. Nature319, 199–203 (1986). ArticleCAS Google Scholar
Ben-Tal, N., Ben-Shaul, A., Nicholls, A. & Honig, B. Free-energy determinants of alpha-helix insertion into lipid bilayers. Biophys. J.70, 1803–1812 (1996). ArticleCAS Google Scholar
Jähnig, F. Thermodynamics and kinetics of protein incorporation into membranes. Proc. Natl. Acad. Sci. USA80, 3691–3695 (1983). Article Google Scholar
Ben-Shaul, A., Ben-Tal, N. & Honig, B. Statistical thermodynamic analysis of protein insertion into lipid membranes. Biophys. J.71, 130–137 (1996). ArticleCAS Google Scholar
Peitzsch, R.M. & McLaughlin, S. Binding of acylated peptides and fatty acids to phospholipid vesicles - pertinence to myristoylated proteins. Biochemistry32, 10436–10443 (1993). ArticleCAS Google Scholar
Flewelling, R.F. & Hubbell, W.L. Hydrophobic ion interactions with membranes. Thermodynamic analysis of tetraphenylphosphonium binding to vesicles. Biophys. J.49, 531–540 (1986). ArticleCAS Google Scholar
Franks, N.P., Abraham, M.H. & Lieb, W.R. Molecular organization of liquid n-octanol - an x-ray diffraction analysis. J. Pharm. Sci.82, 466–470 (1993). ArticleCAS Google Scholar
von Heijne, G. & Blomberg, C. Trans-membrane translocation of proteins: The direct transfer model. Eur. J. Biochem.97, 175–181 (1979). ArticleCAS Google Scholar
Roseman, M.A. Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds. J. Mol. Biol.200, 513–523 (1988). ArticleCAS Google Scholar
Thorgeirsson, T.E., Russell, C.J., King, D.S. & Shin, Y.-K. Direct determination of the membrane affinities of individual amino acids. Biochemistry35, 1803–1809 (1996). ArticleCAS Google Scholar
Thorgeirsson, T.E., Yu, Y.G. & Shin, Y.-K. A limiting law for the electrostatics of the binding of polypeptides to phospholipid bilayers. Biochemistry34, 5518–5522 (1995). ArticleCAS Google Scholar
Selsted, M.E., Novotny, M.J., Morris, W.L., Tang, Y.-Q., Smith, W. & Cullor, J.S. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem.267, 4292–4295 (1992). CASPubMed Google Scholar
Ladokhin, A.S., Selsted, M.E. & White, S.H. Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys. J, submitted.
Tretyachenko-Ladokhina, V.G., Ladokhin, A.S., Wang, L.M., Steggles, A.W. & Holloway, P.W. Amino acid substitutions in the membrane-binding domain of cytochrome b(5) alter its membrane-binding properties. Biochim. Biophys. Acta1153, 163–169 (1993). ArticleCAS Google Scholar
Nakajima, K. et al. Membrane-assisted receptor subtype selection: Synthesis, membrane structure, and opioid receptor affinity of [Phe8,12]-and [Phe8,12,Lys10]-Dynorphin-(1-13)-tridecapeptide. Tetrahedron44, 721–732 (1988). ArticleCAS Google Scholar
Li, S.C. & Deber, C.M. A measure of helical propensity for amino acids in membrane environments. Nature Struct. Biol.1, 368–373 (1994). ArticleCAS Google Scholar
Deber, C.M. & Li, S.-C. Peptides in membranes: Helicity and hydrophobicity. Biopolymers37, 295–318 (1995). ArticleCAS Google Scholar
Ben-Tal, N., Honig, B., Peitzsch, R.M., Denisov, G. & McLaughlin, S. Binding of small basic peptides to membranes containing acidic lipids: Theoretical models and experimental results. Biophys. J.71, 561–575 (1996). ArticleCAS Google Scholar
Engelman, D.M. & Steitz, T.A. The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis. Cell23, 411–422 (1981). ArticleCAS Google Scholar
Mayer, L.D., Hope, M.J. & Cullis, P.R. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim. Biophys. Acta858, 161–168 (1986). ArticleCAS Google Scholar
Park, K., Perczel, A. & Fasman, G.D. Differentiation between transmembrane helices and peripheral helices by the deconvolution of circular dichroism spectra of membrane proteins. Protein Sci.1, 1032–1049 (1992). ArticleCAS Google Scholar