메뉴 건너뛰기




Volumn 71, Issue 6, 1996, Pages 3046-3050

Helix-helix interactions in lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

ALKANE; LIPID; MEMBRANE PROTEIN; SOLVENT;

EID: 0029768644     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79498-5     Document Type: Article
Times cited : (62)

References (41)
  • 1
    • 0019886270 scopus 로고
    • The molecular organization of biomolecular lipid membranes. The dielectric structure of the hydrophilic/hydrophobic interface
    • Ashcroft, R. G., H. G. L. Coster, and J. R. Smith. 1981. The molecular organization of biomolecular lipid membranes. The dielectric structure of the hydrophilic/hydrophobic interface. Biochm. Biophys. Acta. 643: 191-204.
    • (1981) Biochm. Biophys. Acta , vol.643 , pp. 191-204
    • Ashcroft, R.G.1    Coster, H.G.L.2    Smith, J.R.3
  • 2
    • 0028244098 scopus 로고
    • Collisions between helical peptides in membranes monitored using electron paramagnetic resonance: Evidence that alamethicin is monomeric in the absence of a membrane potential
    • Barranger-Mathys, M., and D. S. Cafiso. 1994. 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. 67:172-176.
    • (1994) Biophys. J. , vol.67 , pp. 172-176
    • Barranger-Mathys, M.1    Cafiso, D.S.2
  • 3
    • 77957046824 scopus 로고
    • Molecular theory of chain packing, elasticity and lipid-protein interaction in lipid membranes
    • R. Lipowsky and E. Sackmann, editors. Elsevier Science, Amsterdam
    • Ben-Shaul, A. 1995. Molecular theory of chain packing, elasticity and lipid-protein interaction in lipid membranes. In Handbook of Biological Physics: Structure and Dynamics of Membranes, Vol. 1. R. Lipowsky and E. Sackmann, editors. Elsevier Science, Amsterdam. 359-401.
    • (1995) Handbook of Biological Physics: Structure and Dynamics of Membranes , vol.1 , pp. 359-401
    • Ben-Shaul, A.1
  • 4
    • 0029938187 scopus 로고    scopus 로고
    • Statistical thermodynamic analysis of protein insertion into lipid membranes
    • Ben-Shaul, A., N. Ben-Tal, and B. Honig. 1996. Statistical thermodynamic analysis of protein insertion into lipid membranes. Biophvs. J. 71: 130-138.
    • (1996) Biophvs. J. , vol.71 , pp. 130-138
    • Ben-Shaul, A.1    Ben-Tal, N.2    Honig, B.3
  • 5
    • 33751156674 scopus 로고
    • The energetics of colloids: Do oppositely charged particles necessary attract each other?
    • Ben-Tal, N. 1995. The energetics of colloids: do oppositely charged particles necessary attract each other? J. Phys. Chem. 99:9642-9645.
    • (1995) J. Phys. Chem. , vol.99 , pp. 9642-9645
    • Ben-Tal, N.1
  • 6
    • 0029669955 scopus 로고    scopus 로고
    • Free energy determinants of α-helix insertion into lipid bilayers
    • Ben-Tal, N., A. Ben-Shaul, A. Nicholls, and B. Honig. 1996a. Free energy determinants of α-helix insertion into lipid bilayers. Biophys. J. 70: 1803-1812.
    • (1996) Biophys. J. , vol.70 , pp. 1803-1812
    • Ben-Tal, N.1    Ben-Shaul, A.2    Nicholls, A.3    Honig, B.4
  • 7
    • 0000312402 scopus 로고
    • Dielectric constant effects on the energetics of oppositely charged colloids: A lattice field theory study
    • Ben-Tal, N., and R. D. Coalson. 1994. Dielectric constant effects on the energetics of oppositely charged colloids: a lattice field theory study. J. Chem. Phys. 101:5148-5166.
    • (1994) J. Chem. Phys. , vol.101 , pp. 5148-5166
    • Ben-Tal, N.1    Coalson, R.D.2
  • 8
    • 0029757155 scopus 로고    scopus 로고
    • Binding of small basic peptides to membranes containing acidic lipids: Theoretical models and experimental results
    • Ben-Tal, N., B. Honig, R. M. Peitzsch, G. Denisov, and S. McLaughlin. 1996b. Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results. Biophys. J. 71: 561-575.
    • (1996) Biophys. J. , vol.71 , pp. 561-575
    • Ben-Tal, N.1    Honig, B.2    Peitzsch, R.M.3    Denisov, G.4    McLaughlin, S.5
  • 9
    • 0026694442 scopus 로고
    • Intramembrane helix-helix association in oligomerization and transmembrane signaling
    • Bormann, B. J., and D. M. Engelman. 1992. Intramembrane helix-helix association in oligomerization and transmembrane signaling. Annu. Rev. Biophys. Biomol. Struct. 21:223-242.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 223-242
    • Bormann, B.J.1    Engelman, D.M.2
  • 10
    • 0027080146 scopus 로고
    • Forces involved in the assembly and stabilization of membrane proteins
    • Cramer, W. A., D. M. Engelman, G. Von Heijne, and D. C. Rees. 1992. Forces involved in the assembly and stabilization of membrane proteins. FASEB J. 6:3397-3402.
    • (1992) FASEB J. , vol.6 , pp. 3397-3402
    • Cramer, W.A.1    Engelman, D.M.2    Von Heijne, G.3    Rees, D.C.4
  • 11
    • 0027143565 scopus 로고
    • Val→Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein
    • Deber, C. M., A. R. Khan, Z. Li, C. Joensson, M. Glibowicka, and J. Wang. 1993. Val→Ala mutations selectively alter helix-helix packing in the transmembrane segment of phage M13 coat protein. Proc. Natl. Acad. Sci. USA. 90:11648-11652.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11648-11652
    • Deber, C.M.1    Khan, A.R.2    Li, Z.3    Joensson, C.4    Glibowicka, M.5    Wang, J.6
  • 12
    • 0029153215 scopus 로고
    • Peptides in membranes: Helicity and hydrophobicity
    • Deber, C. M. and S-C. Li. 1995. Peptides in membranes: helicity and hydrophobicity. Biopolymers. 37:295-318.
    • (1995) Biopolymers , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.-C.2
  • 13
    • 0027362726 scopus 로고
    • A molecular model for lipid-protein interaction in membranes: The role of hydrophobic mismatch
    • Fattal, D. R., and A. Ben-Shaul. 1993. A molecular model for lipid-protein interaction in membranes: the role of hydrophobic mismatch. Biophys. J. 65:1795-1809.
    • (1993) Biophys. J. , vol.65 , pp. 1795-1809
    • Fattal, D.R.1    Ben-Shaul, A.2
  • 14
    • 0024638539 scopus 로고
    • Destabilization of an α-helix-bunde protein by helix dipoles
    • Gilson, M. K., and B. Honig. 1989. Destabilization of an α-helix-bunde protein by helix dipoles. Proc. Natl. Acad. Sci. USA. 86:1524-1528.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1524-1528
    • Gilson, M.K.1    Honig, B.2
  • 15
    • 0016399124 scopus 로고
    • Energy functions for peptides and proteins. I. Derivation of a consistent forcefield including the hydrogen bond from amide crystals
    • Hagler, A. T., E. Haler, and S. Lifson. 1974. Energy functions for peptides and proteins. I. Derivation of a consistent forcefield including the hydrogen bond from amide crystals. J. Am. Chem. Soc. 96:5319-5327.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 5319-5327
    • Hagler, A.T.1    Haler, E.2    Lifson, S.3
  • 16
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch, Z. S., and B. Tidor. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3:211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 17
    • 0021978310 scopus 로고
    • The role of the α-helix dipole in protein function and structure
    • Hol, W. G. 1985. The role of the α-helix dipole in protein function and structure. Prog. Biophys. Mol. Biol. 45:149-195.
    • (1985) Prog. Biophys. Mol. Biol. , vol.45 , pp. 149-195
    • Hol, W.G.1
  • 18
    • 0019776488 scopus 로고
    • Dipoles of the α-helix and β-sheet: Their role in protein folding
    • Hol, W. G., L. M. Halie, and C. Sander. 1981. Dipoles of the α-helix and β-sheet: their role in protein folding. Nature. 294:532-536.
    • (1981) Nature , vol.294 , pp. 532-536
    • Hol, W.G.1    Halie, L.M.2    Sander, C.3
  • 20
    • 0000176654 scopus 로고
    • Stability of "salt bridges" in membrane proteins
    • Honig, B., and W. L. Hubbell. 1984. Stability of "salt bridges" in membrane proteins. Proc. Natl. Acad. Sci. USA. 81:5412-5416.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5412-5416
    • Honig, B.1    Hubbell, W.L.2
  • 21
    • 0029016182 scopus 로고
    • Classical electrostatic in biology and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatic in biology and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 22
    • 33751385054 scopus 로고
    • Macroscopic models of aqueous solutions: Biological and chemical applications
    • Honig, B., K. Sharp, and A.-S. Yang. 1993. Macroscopic models of aqueous solutions: biological and chemical applications. J. Phys. Chem. 97:1101-1109.
    • (1993) J. Phys. Chem. , vol.97 , pp. 1101-1109
    • Honig, B.1    Sharp, K.2    Yang, A.-S.3
  • 23
    • 0000963997 scopus 로고
    • Helix-helix interactions inside lipid bilayers
    • Lemmon, M. A., and D. M. Engelman. 1992. Helix-helix interactions inside lipid bilayers. Curr. Opin. Struct. Biol. 2:511-518.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 511-518
    • Lemmon, M.A.1    Engelman, D.M.2
  • 25
    • 0017304621 scopus 로고
    • Lipid-mediated protein interaction in membranes
    • Marcelja, S. 1976. Lipid-mediated protein interaction in membranes. Biochim. Biophys. Acta. 455:1-7.
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 1-7
    • Marcelja, S.1
  • 26
    • 0026438116 scopus 로고
    • Electrostatic fields in antibodies and antibody/antigen complexes
    • Novotny, J., and K. Sharp. 1992. Electrostatic fields in antibodies and antibody/antigen complexes. Prog. Biophys. Mol. Biol. 58:203-224.
    • (1992) Prog. Biophys. Mol. Biol. , vol.58 , pp. 203-224
    • Novotny, J.1    Sharp, K.2
  • 27
    • 0014481138 scopus 로고
    • Energy of ion crossing a low dielectric membrane: Solution to four relevant electrostatic problems
    • Parsegian, A. 1969. Energy of ion crossing a low dielectric membrane: solution to four relevant electrostatic problems. Nature. 221:844-846.
    • (1969) Nature , vol.221 , pp. 844-846
    • Parsegian, A.1
  • 28
    • 0027264459 scopus 로고
    • Integral membrane protein structure: Transmembrane α-helices as autonomous folding domains
    • Popot. J.-L. 1993. Integral membrane protein structure: transmembrane α-helices as autonomous folding domains. Curr. Opin. Struct. Biol. 3:532-540.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 532-540
    • Popot, J.-L.1
  • 29
    • 0020172455 scopus 로고
    • α-Helix dipole model and electrostatic stabilization of 4-α-helical proteins
    • Sheridan, R. P., R. M. Levy, and F. R. Salemme. 1982. α-Helix dipole model and electrostatic stabilization of 4-α-helical proteins. Proc. Natl. Acad. Sci. USA. 79:4545-4549.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4545-4549
    • Sheridan, R.P.1    Levy, R.M.2    Salemme, F.R.3
  • 30
    • 33748640631 scopus 로고    scopus 로고
    • Calculation of alkane to water solvation free energies using continuum solvent models
    • Sitkoff, D., N. Ben-Tal, and B. Honig. 1996. Calculation of alkane to water solvation free energies using continuum solvent models. J. Phys. Chem. 100:2744-1252.
    • (1996) J. Phys. Chem. , vol.100 , pp. 2744-11252
    • Sitkoff, D.1    Ben-Tal, N.2    Honig, B.3
  • 31
    • 32844457567 scopus 로고
    • Accurate calculations of hydration free energies using macroscopic solvent models
    • Sitkoff, D., K. Sharp, and B. Honig. 1994. Accurate calculations of hydration free energies using macroscopic solvent models. J. Phys. Chem. 98:1978-1988.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.2    Honig, B.3
  • 32
    • 0028814024 scopus 로고
    • Determination of helix-helix interaction in membranes by rotational resonance NMR
    • Smith, S. O., and B. J. Bormann. 1995. Determination of helix-helix interaction in membranes by rotational resonance NMR. Proc. Natl. Acad. Sci. USA. 92:488-491.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 488-491
    • Smith, S.O.1    Bormann, B.J.2
  • 33
    • 0001383488 scopus 로고
    • Energetics of electron transfer reaction in polar solvents
    • Tachiya, M. 1994. Energetics of electron transfer reaction in polar solvents. Chem. Phys. Lett. 230:491-494.
    • (1994) Chem. Phys. Lett. , vol.230 , pp. 491-494
    • Tachiya, M.1
  • 34
    • 0028304680 scopus 로고
    • Membrane proteins: From sequence to structure
    • von Heijne, G. 1994. Membrane proteins: from sequence to structure. Annu. Rev. Biophys. Biomol. Struct. 23:167-192.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 167-192
    • Heijne, G.1
  • 35
    • 0017292056 scopus 로고
    • The α-helix as an electric macro-dipole
    • Wada, A. 1976. The α-helix as an electric macro-dipole. Adv. Biophys. 9:1-63.
    • (1976) Adv. Biophys. , vol.9 , pp. 1-63
    • Wada, A.1
  • 36
    • 0000467270 scopus 로고
    • Electrostatic basis of structure-function correlation in proteins
    • Warshel, A. 1981. Electrostatic basis of structure-function correlation in proteins. Acc. Chem. Res. 14:284-290.
    • (1981) Acc. Chem. Res. , vol.14 , pp. 284-290
    • Warshel, A.1
  • 37
    • 0021476470 scopus 로고
    • Calculations of electrostatic interactions in biological systems and in solutions
    • Warshel, A., and S. T. Russell. 1984. Calculations of electrostatic interactions in biological systems and in solutions. Q. Rev. Biophys. 17: 283-422.
    • (1984) Q. Rev. Biophys. , vol.17 , pp. 283-422
    • Warshel, A.1    Russell, S.T.2
  • 38
    • 0019815621 scopus 로고
    • Electrostatic control of the efficiency of light-induced electron transfer across membranes
    • Warshel, A., and D. W. Schlosser. 1981. Electrostatic control of the efficiency of light-induced electron transfer across membranes. Proc. Natl. Acad. Sci. USA. 78:5564-5568.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5564-5568
    • Warshel, A.1    Schlosser, D.W.2
  • 39
    • 0029164701 scopus 로고
    • Packing of coat protein amphipathic and transmembrane helices in filamentous bacteriophage M13: Role of small residues in protein oligomerization
    • Williams, K. A., M. Glibowicka, Z. Li, H. Li, A. R. Khan, Y. M. Chen, J. Wang, D. A. Marvin, and C. M. Deber. 1995. Packing of coat protein amphipathic and transmembrane helices in filamentous bacteriophage M13: role of small residues in protein oligomerization. J. Mol. Biol. 252:6-14.
    • (1995) J. Mol. Biol. , vol.252 , pp. 6-14
    • Williams, K.A.1    Glibowicka, M.2    Li, Z.3    Li, H.4    Khan, A.R.5    Chen, Y.M.6    Wang, J.7    Marvin, D.A.8    Deber, C.M.9
  • 40
    • 0023410587 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: Membrane-protein interactions
    • Yeates, T. O., H. Komiya, D. C. Rees, J. P. Allen, and G. Feher. 1987. Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions. Proc. Natl. Acad. Sci. USA. 84: 6438-6442.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6438-6442
    • Yeates, T.O.1    Komiya, H.2    Rees, D.C.3    Allen, J.P.4    Feher, G.5
  • 41
    • 0026619551 scopus 로고
    • Poisson-Boltzmann analysis of the λ repressor-operator interaction
    • Zacharias, M., B. A. Luty, M. E. Davis, and J. A. McCammon. 1992. Poisson-Boltzmann analysis of the λ repressor-operator interaction. Biophys. J. 63:1280-1285.
    • (1992) Biophys. J. , vol.63 , pp. 1280-1285
    • Zacharias, M.1    Luty, B.A.2    Davis, M.E.3    McCammon, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.