Chapter 7 Interaction of Natural and Model Peptides with Membranes

Current Topics in Membranes and Transport

Volumn 48, Issue C, 1999, Pages 197-228

  Cafiso, David S ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0001506668     PISSN: 00702161     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2161(08)61045-X     Document Type: Article

References (149)

1. Akerfeldt K.S., Kim R.M., Camac D., Groves J.T., Lear J.D., and Degrado W.F. Tetraphilin: A four-helix proton channel built on a tetraphenylporphyrin framework. J. Am. Chem. Soc. 114 (1992) 9656-9657
2. + on the translocation of charged residues explain the 'positive inside' rule. EMBO J. 13 (1994) 2267-2272
3. Arbuzova A., Wang J., Murray D., Jacob J., Cafiso D.S., and McLaughlin S. Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin. J. Biol. Chem. 272 (1997) 27167-27177
4. Archer S.J., Ellena J.F., and Cafiso D.S. Dynamics and aggregation of the peptide ion channel alamethicin. Biophys. J. 60 (1991) 389-398
5. Arumugam S., Pascal S., North C.L., Hu W., Lee K.-C., Cotten M., Ketchem R.R., Xu F., Brenneman M., Kovacs F., Tian F., Wany A., Huo S., and Cross T.A. Conformational trapping in a membrane environment: A regulatory mechanism for protein activity. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 5872-5876
6. Axelsen P.H., Kaufman B.K., McElhaney R.N., and Lewis R.N. The infrared dichroism of transmembrane helical polypeptides. Biophys. J. 69 (1995) 2770-2781
7. Barranger-Mathys M., and Cafiso D.S. Collisions between helical peptides in membranes monitored using electron paramagnetic resonance. Evidence that alamethicin is monomeric in the absence of a membrane potential. Biophys. J. 67 (1994) 172-176
8. Barranger-Mathys M., and Cafiso D.S. Membrane structure of voltage-gated channel forming peptides revealed by site-directed spin labeling. Biochemistry 35 (1996) 498-505
9. Batenburg A.M., and de Kruijff B. Modulation of membrane surface curvature by peptide-lipid interactions. Biosci. Rep. 8 (1988) 299-307
10. Bechinger B. Structure and functions of channel-forming peptides: Magainins, cecropins, mellitin and alamethicin. J. Membr. Biol. 156 (1997) 197-211
11. Ben-Tal N., Honig B., Peitzsch R.M., Denisov G., and McLaughin S. Binding of small basic peptides to membranes containing acid lipids: Theoretical models and experimental results. Biophys. J. 71 (1996) 561-575
12. Ben-Tal N., Ben-Shaul A., Nicholls A., and Honig B. Free-energy determinants of alpha-helix insertion into lipid bilayers. Biophys J. 70 (1996) 1803-1812
13. Ben-Tal N., Honig B., Miller C., and McLaughlin S. Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles. Biophys. J. 73 (1997) 1717-1727
14. Brockman H. Dipole potential of lipid membranes. Chem. Phys. Lipids 73 (1994) 57-79
15. 1H-NMR studies of self-aggregation of melittin in aqueous solution. Biochim. Biophys. Acta. 622 (1980) 231-244
16. Brown M.F. Modulation of rbdopsin function by properties of the membrane bilayer. Chem. Phys. Lipids 73 (1994) 159-180
17. 2 terminus of Src. Biochemistry 33 (1994) 13093-13101
18. Cafiso D.S. Lipid bilayers: Membrane-protein electrostatic interactions. Curr. Opin. Struct. Biol. 1 (1991) 185-190
19. Cafiso D.S. Alamethicin: A peptide model for voltage-gating and protein membrane electrostatic interactions. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 141-165
20. Cafiso D., McLaughlin A., McLaughlin S., and Winiski A. Measuring electrostatic potentials adjacent to membranes. In: Fleischer S., and Fleischer B. (Eds). Methods in Enzymology 171 (1989), Academic Press, San Diego 342-364
21. Chan H.S., Wattenbarger M.R., Evans D.F., Bloomfield V.A., and Dill K.A. Enhanced structure of polymers at interfaces. J. Chem. Phys. 94 (1991) 8542-8557
22. Chernomordik L.V., Frolov V.A., Leikina E., Bronk P., and Zimmerberg J. The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pare formation. J. Cell Biol. 140 (1998) 1369-1382
23. Chung L.A., and Thompson T.E. Design of membrane inserting peptides: Spectroscopic characterization with and without lipid bilayers. Biochemistry 35 (1996) 11343-11354
24. Cramer W.A., Heymann J.B., Schendel S.L., Deriy B.N., Cohen F.S., Elkins P.A., and Stauffacher C.V. Structure-function of the channel-forming colicins. Annu. Rev. Biophys. Biomol. Struct. 24 (1995) 611-641
25. Cross F.R., Garber E.A., Pellman D., and Hanafusa H. A short sequence in the pp60src N-terminus is required for pp60src myristylation and membrane association and for cell transformation. Mol. Cell. Biol. 4 (1984) 1834-1842
26. Cross T.A. Solid-state nuclear magnetic resonance characterization of gramicidin channel structure. In: Fields G.B. (Ed). Methods in Enzymology 289 (1997), Academic Press, San Diego 672-696
27. Dalbey R.E. Positively charged residues are important determinants of membrane protein topology. Trends Biochem. Sci. 15 (1990) 253-257
28. DeGrado W.F., Wasserman Z.R., and Lear J.D. Protein design, a minimalist approach. Science 243 (1989) 622-628
29. DeGrado W.F., and Lear J.D. Conformationally constrained alpha-helical peptide models for protein ion channels. Biopolymers 29 (1990) 205-213
30. de Kroon A.I., de Gier J., and de Kruijff B. Association of synthetic model peptides with phospholipid vesicles induced by a membrane potential. Biochim. Biophys. Acta. 981 (1989) 371-373
31. de Kroon A.I., Vogt B., van't Hof R., de Kruijff B., and de Gier J. Ion gradient-induced membrane translocation of model peptides. Biophys. J. 60 (1991) 525-537
32. de Kruijff B., Rietveld A., Telders N., and Vaandrager B. Molecular aspects of bilayer stabilization induced by poly(L-lysines) of varying size in cardiolipin liposomes. Biochim. Biophys. Acta 820 (1985) 295-304
33. Dempsey C.E. The actions of melittin on membranes. Biochim. Biophys. Acta 1031 (1990) 143-161
34. Dempsey C.E., and Butler G.S. Helical structure and orientation of melittin in dispersed phospholipid membranes from amide exchange analysis in situ. Biochemistry 31 (1992) 11973-11977
35. Denisov G., Wanaski S., Luan P., Glaser M., and McLaughlin S. Binding of basic peptides to membranes produces lateral domains enriched in the acid lipids phosphatidylserine and phosphatidylinositol 4, 5-bisphosphate: An electrostatic model and experimental results. Biophys. J. 74 (1998) 731-744
36. De Young L.R., and Dill K.A. Partitioning of non-polar solutes into lipid bilayers and amorphous normal alkanes. J. Phys. Chem. 94 (1990) 801-809
37. Dufourcq J., Faucon J.F., Maget-Dana R., Pileni M.P., and Helene C. A fluroescence study of the binding of oligopeptides containing aromatic and basic residues to phospholipid vesicles. Biochem. Biophys. Acta 649 (1981) 67-75
38. Eisenberg D. Three-dimensional structure of membrane and surface proteins. Annu. Rev. Biochem. 53 (1984) 595-623
39. Eisenberg D., and McLachlan A.D. Solvation energy in protein folding and binding. Nature (London) 319 (1986) 199-203
40. 1H nuclear Overhauser effect spectroscopy. Biochemistry 26 (1987) 4584-4592
41. Engleman D.M., and Steiz T.A. The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis. Cell (Cambridge, Mass.) 23 (1981) 411-422
42. Engleman D., Steitz T.A., and Goldman A. Identifying non-polar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15 (1986) 321-353
43. Epand R.F., Moroder L., Lutz J., Flanagan T.D., Nir S., and Epand R.M. Lipogastrins as potent inhibitors of viral fusion. Biochim. Biophys. Acta 1327 (1997) 259-268
44. Fattal E., Nir S., Parente R.A., and Szoka Jr. F.C. Pore-forming peptides induce rapid phospholipid flip-flop in membranes. Biochemistry 33 (1994) 6721-6731
45. Flewelling R.F., and Hubbell W.L. The membrane dipole potential in a total membrane potential model. Biophys. J. 49 (1986) 541-552
46. Frey S., and Tamm L.K. Membrane insertion and lateral diffusion of fluorescence-labelled cytochrome c oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers. Biochem. J. 272 (1990) 713-719
47. Frey S., and Tamm L.K. Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study. Biophys. J. 60 (1991) 922-930
48. Gazit E., Miller I.R., Biggin P.C., Sansom M.S., and Shai Y. Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J. Mole. Biol. 258 (1996) 860-870
49. Glaser M., Wanaski S., Buser C.A., Boguslavsky V., Rashidzada W., Morris A., Rebecchi M., Scarlata S.F., Runnels L.W., Prestwich G.D., Chen J., Aderem A., Ahn J., and McLaughlin S. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4, 5-bisphosphate in lateral domains. J. Biol. Chem. 271 (1996) 26187-26193
50. Golding C., Senior S., Wilson M.T., and O'Shea P. Time resolution of binding and membrane insertion of a mitochondrial signal peptide: Correlation with structural changes and evidence for cooperativity. Biochemisrry 35 (1996) 10931-10937
51. Gruner S.M. Stability of lyotropic phases with curved interfaces. J. Phys. Chem. 93 (1989) 7562-7570
52. Hartsel S.C., and Cafiso D.S. A test of discreteness-of-charge effects in phospholipid vesicles: Measurements using paramagnetic amphiphiles. Biochemistry 25 (1986) 8214-8219
53. He K., Ludtke S.J., Heller W.T., and Huang H.W. Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71 (1996) 2669-2679
54. He K., Ludtke S.J., Worcester D.L., and Huang H.W. Neutron scattering in the plane of membranes: Structure of alamethicin pores. Biophys. J. 70 (1996) 2659-2666
55. Holtzer A. The use of Flory-Huggins theory in interpreting partitioning of solutes between organic liquids and water. Biopolymers 32 (1992) 711-715
56. Holtzer A. Does Flory-Huggins theory help in interpreting solute partitioning experiments?. Biopolymers 34 (1994) 315-320
57. Huang C.-H., and Charlton J.P. Interactions of phosphatidylcholine vesicles with 2-p-toluidinylnaphthalene-6-sulfonate. Biochemistry 11 (1972) 735-740
58. Hunt J.F., Rath P., Rothschild C.J., and Engelman D.M. Spontaneous, pH-dependent membrane insertion of a transbilayer alpha-helix. Biochemistry 36 (1997) 15177-15192
59. Iwamoto T., Grove A., Montal M.O., Montal M., and Tomich J.M. Chemical synthesis and characterization of peptides and oligomeric proteins designed to form transmembrane ion channels. Int. J. Pept. Protein Res. 43 (1994) 597-607
60. Jacobs R.E., and White S.H. The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices. Biochemistry 28 (1989) 3421-3437
61. Jahnig F. Thermodynamics and kinetics of protein incorporation into membranes. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 3691-3695
62. John E., and Jahnig F. Dynabics of melittin in water and membranes as determined by fluorescence anisotropy decay. Biophys. J. 54 (1988) 817-827
63. Kagan B.L., Ganz T., and Lehrer R.I. Defensins: A family of antimicrobial and cytotoxic peptides. Toxicology 87 (1994) 131-149
64. Kaiser E.T., and Kezdy F.J. Secondary structures of proteins and peptides in amphiphilic environments. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 1137-1143
65. 2-terminal glycine of p60src prevents both myristoylation and morphological transformation. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 4625-4628
66. Keller S.L., Bezrukov S.M., Gruner S.M., Tate M.W., Vodyanoy I., and Parsegian V.A. Probablilty of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Biophys. J. 65 (1993) 23-27
67. Keller S.L., Gruner S.M., and Gawrisch K. Small concentrations of alamethicin induce a cubic phase in bulk phosphatidylethanolamine mixtures. Biochim. Biophys. Acta 1278 (1996) 241-246
68. Kienker P.K., DeGrado W.F., and Lear J.D. A helical-dipole model describes the single-channel current rectification of an uncharged peptide ion channel. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 4859-4863
69. Killian J.A., de Jong A.M., Bijvelt J., Verkleij A.J., and de Kruijff B. Induction of non-bilayer lipid structures by functional signal peptides. EMBO J. 9 (1990) 815-819
70. Kim J., Mosior M., Chung L.A., Wu H., and McLaughlin S. Binding of peptides with basic residues to membranes containing acidic phospholipids. Biophys. J. 60 (1991) 135-148
71. Kim J., Blackshear P.J., Johnson J.D., and McLaughlin S. Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin. Biophys J. 67 (1994) 227-237
72. Kiyota T., Lee S., and Sugihara G. Design and synthesis of amphiphilic-helical model peptides with systematically varied hydrophobic-hydrophilic balance and their interaction with lipid- and bio-membranes. Biochemistry 35 (1996) 13196-13204
73. Koeppe R.E.N., and Anderson O.S. Engineering the gramicidin channel. Annu. Rev. Biophys. Biomol. Struct. 25 (1996) 231-258
74. Langner M., Cafiso D., Marcelja S., and McLaughlin S. Electrostatics of phosphoinositide bilayer membranes. Theoretical and experimental results. Biophys. J. 57 (1990) 335-349
75. Lear J.D., Wasserman Z.R., and DeGrado W.F. Synthetic amphiphilic peptide models for protein ion channels. Science 240 (1988) 1177-1181
76. Lewis J.R., and Cafiso D.S. Binding energy of the channel forming peptide alamethicin varies with membrane spontaneous curvature. Biophys. J. 76 (1999) A18
77. Liu L.P., and Deber C.M. Anionic phospholipids modulate peptide insertion into membranes. Biochemistry 36 (1997) 5476-5482
78. Lu Y., Bazzi M.D., and Nelsestuen G.L. Kinetics of annexin VI, calcium, and phospholipid association and dissociation. Biochemistry 34 (1995) 10777-10785
79. Ludtke S.J., He K., Heller W.T., Harroun T.A., Yang L., and Huang H.W. Membrane pores induced by magainin. Biochemistry 35 (1996) 13723-13728
80. Lundbaek J.A., Maer A.M., and Andersen O.S. Lipid bilayer electrostatic energy, curvature stress, and assembly of gramicidin channels. Biochemistry 36 (1997) 5695-5701
81. McIlroy B.K., Walters J.D., Blackshear P.J., and Johnson J.D. Phosphorylationdependent binding of a synthetic MARCKS peptide to calmodulin. J. Biol. Chem. 266 (1991) 4959-4964
82. McLaughlin S.A. The electrostatic properties of membranes. Annu. Rev. Biophys. Biophys. Chem. 18 (1989) 113-136
83. McLaughlin S., and Aderem A. The myristoyl-electrostatic switch A modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20 (1995) 272-276
84. Maduke M., and Roise D. Import of a mitochondrial presequence into protein-free phospholipid vesicles. Science 260 (1993) 364-367
85. Maloy W.L., and Kari U.P. Structure-activity studies on magainins and other host defense peptides. Biopolymers 37 (1995) 105-122
86. Matsuzaki K. Molecular action mechanisms and membrane recognition of membrane-acting antimicrobial peptides. Yakugaka Zasshi (J. Pharm. Soc. Jpn.) 117 (1997) 253-264
87. Matsuzaki K., Murase O., Tokuda H., Funakoshi S., Fujii N., and Miyajima K. Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry 33 (1994) 3342-3349
88. Moll T.S., and Thompson T.E. Semisynthetic proteins: Model systems for the study of the insertion of hydrophobic peptides into preformed lipid bilayers. Biochemistry 33 (1994) 15469-15482
89. Morein S., Anderson A., Rilfors L., and Lindhlom G. Wild-type Escherichiu coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures. J. Biol. Cham. 271 (1996) 6801-6809
90. Mosior M., and McLaughlin S.A. Binding of basic peptides to acidic lipids in membranes: Effects of inserting alanine(s) between the basic residues. Biochemistry 31 (1992) 1767-1773
91. Mosior M., and McLaughlin S.A. Electrostatics and Dimensionality Can Produce Apparent Cooperativity when Protein Kinase C and Its Substrates Bind to Acidic Lipids in Membranes. (1992), Ellis Horwood, Chester, England
92. Murray D., Hennida-Matsumoto L., Buser C.A., Tsang J., Sigal C.T., Ben-Tal, Honig N.B., Resh M.D., and McLaughlin S. Electrostatics and the membrane association of src: Theory and experiment. Biochemistry 37 (1998) 2145-2159
93. 15N NMR. Biophys. J. 69 (1995) 2392-2397
94. Oblatt-Montal M., Buhler L.K., Iwrimoto T., Tomich J.M., and Montal M. Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. I. Transmembrane segment M2 of the nicotinic cholinergic receptor channel is a key pore-lining structure. J. Biol Chem. 268 (1993) 14601-14607
95. Osterberg F., Rilfors L., Wieslander A., Lindblom G., and Gruner S.M. Lipid extracts from membranes of Acholeplusmu luidluwii A grown with different fatty acids have a nearly constant spontaneous curvature. Biochim. Biophys. Acta 1257 (1995) 18-24
96. Parente R.A., Nadasdi L., Subbargo N.K., and Szoka Jr. F.C. Association of a pH-sensitive peptide with membrane vesicles: Role of amino acid sequence. Biochemistry 29 (1990) 8713-8719
97. Pawlak M., Meseth U., Dhanapal B., Mutter M., and Vogel H. Template-assembled melittin: Structural and functianal characterization of a designed, synthetic channel-forming protein. Protein Sci. 3 (1994) 1788-1805
98. Peitzsch R.M., and McLaughlin S.M. Binding of acylated peptides and fatty acids to phospholipid vesicles: Pertinence to myristoyated proteins. Biochemistry 32 (1993) 10426-10443
99. Polozov I.V., Polozova A.I., Mishra V.K., Anantharamaiah G.M., Segrest J.P., and Epand R.M. Studies of kinetics and equilibrium membrane binding of class A and class L model amphipathic peptides. Riochim. Biophys. Acta 1368 (1998) 343-354
100. Qin Z., and Cafiso D.S. Membrane structure of the PKC and calmodulin binding domain of MARCKS determined by site-directed spin-labeling. Biochemistry 35 (1996) 2917-2925
101. Reddy G.L., Iwamoto T., Tomich J.M., and Montal M. Synthetic peptides and four-helix bundle proteins as model systems for the pore-forming structure of channel proteins. II. Transmembrane segment M2 of the brain glycine receptor is a plausible candidate for the pore-lining structure. J. Biol. Chem. 268 (1993) 14608-14615
102. Ren J., Lew S., Wang Z., and London E. Transmembrane orientation of hydrophobic alpha-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration. Biochemistry 36 (1997) 10213-10220
103. Rosen A., Keenan K.F., Thelen M., Nairn A.C., and Aderem A. Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. J. Exp. Med. 172 (1990) 1211-1215
104. Roux B., and Karplus M. Molecular dynamics simulations of the gramicidin channel. Annu. Rev. Biophys. Biomol. Struct. 23 (1994) 731-761
105. 31P NMR study of pentalysine interaction with headgroup deuterated phosphatidylcholine and phosphatidylserine. Eur. Biophys. J. 16 (1988) 267-273
106. Sansom M.S.P. Alamethicin and related peptaibols-model ion channels. Eur. Biophys. J. 22 (1993) 105-124
107. Schwarz G., and Beschiaschvili G. Thermodynamic and kinetic studies on the association of melittin with a phospholipid bilayer. Biochim. Biophys. Acta 979 (1989) 82-90
108. Schwarz G., Gerke H., Rizzo V., and Stankowski S. Incorporation kinetics in a membrane, studied with the pore-forming peptide alamethicin. Biophys. J. 52 (1987) 685-692
109. Seelig J., and Ganz P. Nonclassical hydrophobic effect in membrane binding equilibria. Biochemistry 30 (1991) 9354-9359
110. Sharp K.A., Nicholls A., Friedman R., and Honig B. Extracting hydrophobic free energies from experimental data: Relationship to protein folding and theoretical models. Biochemistry 30 (1991) 9686-9697
111. Shirley B.A., Stanssens P., Hahn U., and Pace C.N. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry 31 (1992) 725-732
112. 2-terminal membrane targeting motif for myristoylated pp60v-src. J. Cell Biol. 119 (1992) 415-425
113. Simon S.A., and McIntosh T.J. Magnitude of the solvation pressure depends on dipole potential. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 9263-9267
114. Skehel J.J., Bizebard T., Bullough P.A., Hughson F.M., Knossow M., Steinhauer D.A., Wharton S.A., and Wiley D.C. Membrane fusion by influenza hemagglutinin. Cold Spring Harbor Symp. Quant. Biol. 60 (1995) 573-580
115. Slater S.J., Kelly M.B., Yeager M.D., Larkin J., Ho C., and Stubbs C.D. Polyunsaturation in cell membranes and lipid bilayers and its effects on membrane proteins. Lipids 31 (1996) S189-S192
116. Tamm L.K. Membrane insertion and lateral mobility of synthetic amphiphilic signal peptides in lipid model membranes. Biochim. Biophys. Acta 1071 (1991) 123-148
117. Tanford C. The hydrophobic effect and the organization of living matter. Science 200 (1978) 1012-1018
118. Taniguchi H., and Manenti S. Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. J. Biol. Chem. 268 (1993) 9960-9963
119. Thorgeirsson T.E., Yu Y.G., and Shin Y.K. A limiting law for the electrostatics of the binding of polypeptides to phospholipid bilayers. Biochemistry 34 (1995) 5518-5522
120. Thorgeirsson T.E., Russell C.J., King D.S., and Shin Y.K. Direct determination of the membrane affinities of individual amino acids. Biochemistry 35 (1996) 1803-1809
121. Towler D.A., Gordon J.I., Adams S.P., and Glaser L. The biology and enzymology or eukaryotic protein acylation. Ann. Rev. Biochem. 57 (1988) 69-99
122. van Klompenburg W., Nilsson I., von Heijne G., and de Kruijff B. Anionic phospholipids are determinants of membrane protein topology. EMBO J. 16 (1997) 4261-4266
123. Veatach W.R., Fossel E.T., and Blout E.R. The conformation of gramicidin A. Biochemistry 37 (1974) 5249-5256
124. Victor K., and Cafiso D.S. Structure and position of the N-terminal membrane-binding domain of pp60src at the membrane interface. Biochemistry 37 (1998) 3402-3410
125. Vogel H., and Jahnig F. The structure of melittin in membranes. Biophys. J. 50 (1986) 573-582
126. Vogt T.C., Killian J.A., and de Kruijff B. The influence of acylation on the lipid structure modulating properties of the transmembrane polypeptide gramicidin. Biochim. Biophys. Acta 1193 (1994) 55-61
127. von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225 (1992) 487-494
128. von Heijne G. Membrane protein assembly: rules of the game. BioEssays 17 (1995) 25-30
129. von Heijne G., and Gavel Y. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174 (1988) 671-678
130. Wade D., Andreu D., Mitchell S.A., Silveira A.M., Boman A., Boman H.G., and Merifield R.B. Antibacterial peptides designed as analogs or hybrids of cecropins and melittin. Int. J. Pept. Proteiv. Res. 40 (1992) 429-436
131. Wallace B.A. The roles of tryptophan residues in the structure, function, and folding of the gramicidin transmembrane ion channel. Adv. Exp. Med. Biol. 398 (1996) 607-614
132. Wang Y., and Weiner H. Evaluation of electrostatic and hydrophobic effects on the interaction of mitochondrial signal sequences with phospholipid bilayers. Biochemistry 33 (1994) 12860-12867
133. Wattenbarger M.R., Chan H.S., Evans D.R., Bloomfield V.A., and Dill K.A. Surface-induced enhancement of internal structure in polymers and proteins. J. Chem. Phys. 93 (1990) 8343-8351
134. Wertz S.L., Savino Y., and Cafiso D.S. Solution and membrane bound structure of a peptide derived from the PKC substrate domain of neuromodulin. Biochemistry 35 (1996) 11104-11112
135. Westerhoff H.V., Zasloff M., Rosner J.L., Hendler R.W., De Waal A., Van Comes A., Jongsma P.M., Riethorst A., and Juretic D. Functional synergism of the magainins PGLa and magainin-2 in Escherichia coli. tumor cells and liposomes. Eur. J. Biochem. 228 (1995) 257-264
136. White S.H., and Wimley W.C. Peptides in lipid bilayers: Structural and thermodynamic basis for partitioning and folding. Curr. Opin. Struct. Biol. 4 (1994) 79-86
137. Wimley W.C., and White S.H. Partitioning of tryptophan side-chain analogs between water and cyclohexane. Biochemistry 31 (1992) 12813-12818
138. Wimley W.C., and White S.H. Membrane partitioning: Distinguishing bilayer effects from the hydrophobic effect. Biochemistry 32 (1993) 6307-6312
139. Wimley W.C., and White S.H. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 2 (1996) 842-848
140. Wimley W.C., Creamer T.P., and White S.W. Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry 35 (1996) 5109-5124
141. Winiski A.P., McLaughlin A.C., McDaniel R.V., Eisenberg M., and McLaughlin S.A. An experimental test of the discreteness-of-charge effect in positive and negative lipid bilayers. Biochemistry 25 (1986) 8206-8214
142. Wooley G.A., and Wallace B.A. Model ion channels: Gramicidin and alamethicin. J. Membr. Biol. 129 (1992) 109-136
143. Wyman T.B., Nicol F., Zelphati O., Scaria P.V., Plank C., and Szoka Jr. F.C. Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers. Biochemistry 36 (1997) 3008-3017
144. Yang L., and Glaser M. Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry 34 (1995) 1500-1506
145. You S., Peng S., Lien L., Breed J., Sansom M.S., and Woolley G.A. Engineering stabilized ion channels: Covalent dimers of alamethicin. Biochemistry 35 (1996) 6225-6232
146. Yu Y.G., Thorgeirsson T.E., and Shin Y.-K. Topology of an amphipathic mitochon-drial signal sequence in the membrane-inserted state. A spin labeling study. Biochemistry 33 (1994) 14221-14226
147. Zhang Y.P., Lewis R.N., Hodges R.S., and McElhaney R.N. Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylcholine bilayers: Differential scanning calorimetric and FTIR spectroscopic studies. Biochemistry 31 (1992) 11579-11588
148. Zhang Y.P., Lewis R.N., Hodges R.S., and McElhaney R.N. Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylethanolamine bilayers: Differential scanning calorimetric and Fourier transform infrared spectroscopic studies. Biophys. J. 68 (1995) 847-857
149. Zheng N., and Gierasch L.M. Signal sequences: The same yet different. Cell. (Cumbridge, Muss.) 86 (1996) 849-852