메뉴 건너뛰기




Volumn 76, Issue 3, 1999, Pages 1213-1227

Molecular dynamics study of substance P peptides partitioned in a sodium dodecylsulfate micelle

Author keywords

[No Author keywords available]

Indexed keywords

DODECYL SULFATE SODIUM; SUBSTANCE P; TYROSINE DERIVATIVE;

EID: 0033047067     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77285-1     Document Type: Article
Times cited : (42)

References (64)
  • 2
    • 0030733344 scopus 로고    scopus 로고
    • Structure and dynamics of an amphiphilic peptide in a lipid bilayer: A molecular dynamics study
    • Belohorcova, K., J. H. Davis, T. B. Woolf, and B. Roux. 1997. Structure and dynamics of an amphiphilic peptide in a lipid bilayer: a molecular dynamics study. Biophys. J. 73:3039-3055.
    • (1997) Biophys. J. , vol.73 , pp. 3039-3055
    • Belohorcova, K.1    Davis, J.H.2    Woolf, T.B.3    Roux, B.4
  • 3
    • 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. 1996. 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
  • 4
    • 0030736114 scopus 로고    scopus 로고
    • Free energy of amide hydrogen bond formation in vacuum, in water, and in liquid alkane solution
    • Ben-Tal, N., D. Sitkoff, I. Topol, A. Yang, S. Burt, and B. Honig. 1997. Free energy of amide hydrogen bond formation in vacuum, in water, and in liquid alkane solution. J. Phys. Chem. B. 101:450-457.
    • (1997) J. Phys. Chem. B. , vol.101 , pp. 450-457
    • Ben-Tal, N.1    Sitkoff, D.2    Topol, I.3    Yang, A.4    Burt, S.5    Honig, B.6
  • 7
    • 0024846405 scopus 로고
    • Use of restrained molecular dynamics in water to determine three-dimensional protein structure: Prediction of the three-dimensional structure of ecballium elaterium trypsin inhibitor II
    • Chiche, L., C. Gaboriaud, A. Heitz, J.-P. Mornon, B. Castro, and P. Kollman. 1989. Use of restrained molecular dynamics in water to determine three-dimensional protein structure: prediction of the three-dimensional structure of ecballium elaterium trypsin inhibitor II. Proteins: Struct., Funct., Genet. 6:405-417.
    • (1989) Proteins: Struct., Funct., Genet. , vol.6 , pp. 405-417
    • Chiche, L.1    Gaboriaud, C.2    Heitz, A.3    Mornon, J.-P.4    Castro, B.5    Kollman, P.6
  • 8
    • 0029099308 scopus 로고
    • Incorporation of surface tension into molecular dynamics simulation of an interface: A fluid phase lipid bilayer membrane
    • Chiu, S.-W., M. Clark, V. Balaji, S. Subramaniam, H. L. Scott, and E. Jakobsson. 1995. Incorporation of surface tension into molecular dynamics simulation of an interface: a fluid phase lipid bilayer membrane. Biophys. J. 69:1230-1245.
    • (1995) Biophys. J. , vol.69 , pp. 1230-1245
    • Chiu, S.-W.1    Clark, M.2    Balaji, V.3    Subramaniam, S.4    Scott, H.L.5    Jakobsson, E.6
  • 9
    • 0025776306 scopus 로고
    • Influence of the replacement of amino acid by its D-enantiomer in the sequence of substance P. 2. Conformational analysis by nmr and energy calculations
    • Convert, O., H. Duplaa, S. Lavielle, and G. Chassaing. 1991. Influence of the replacement of amino acid by its D-enantiomer in the sequence of substance P. 2. Conformational analysis by nmr and energy calculations. Neuropeptides. 19:259-270.
    • (1991) Neuropeptides , vol.19 , pp. 259-270
    • Convert, O.1    Duplaa, H.2    Lavielle, S.3    Chassaing, G.4
  • 10
    • 0001497127 scopus 로고
    • Influence of salt, detergent concentration, and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecylsulfate with m-dichlorobenxene
    • Croonen, Y., E. Gelade, M. Van der Ziegel, H. Van der Auweraer, F. C. Vandendriessche, and F. C. DeSchryver. 1983. Influence of salt, detergent concentration, and temperature on the fluorescence quenching of 1-methylpyrene in sodium dodecylsulfate with m-dichlorobenxene. J. Phys. Chem. 87:1426.
    • (1983) J. Phys. Chem. , vol.87 , pp. 1426
    • Croonen, Y.1    Gelade, E.2    Van Der Ziegel, M.3    Van Auweraer, H.D.4    Vandendriessche, F.C.5    DeSchryver, F.C.6
  • 11
    • 0028807770 scopus 로고
    • Interaction of the fusion inhibiting peptide carbobenzxy-D-Phe-L-Phe-Gly with N-methyldioleoylphosphatidylethanolamine lipid bilayers
    • Damodaran, K. V., and K. M. Merz. 1995. Interaction of the fusion inhibiting peptide carbobenzxy-D-Phe-L-Phe-Gly with N-methyldioleoylphosphatidylethanolamine lipid bilayers. J. Am. Chem. Soc. 117: 6561-6571.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6561-6571
    • Damodaran, K.V.1    Merz, K.M.2
  • 12
    • 0029100115 scopus 로고
    • Interaction of small peptides with lipid bilayers
    • Damodaran, K. V., K. M. Merz, and B. P. Gaber. 1995. Interaction of small peptides with lipid bilayers. Biophys. J. 69:1299-1308.
    • (1995) Biophys. J. , vol.69 , pp. 1299-1308
    • Damodaran, K.V.1    Merz, K.M.2    Gaber, B.P.3
  • 13
    • 0027048485 scopus 로고
    • Discovery of a potent substance P antagonist: Recognition of the key molecular determinant
    • Desai, V. C., S. L. Lefkowitz, P. F. Thadeio, K. P. Longo, and R. M. Snider. 1992. Discovery of a potent substance P antagonist: recognition of the key molecular determinant. J. Med. Chem. 35:4911-4913.
    • (1992) J. Med. Chem. , vol.35 , pp. 4911-4913
    • Desai, V.C.1    Lefkowitz, S.L.2    Thadeio, P.F.3    Longo, K.P.4    Snider, R.M.5
  • 14
    • 0026653453 scopus 로고
    • Binding of substance P to monolayers and vesicles made of phosphatidykholine and/or phosphatidyiserine
    • Duplaa, H., O. Convert, A.-M. Sautereau, J.-F. Tocanne, and G. Chassaing. 1992. Binding of substance P to monolayers and vesicles made of phosphatidykholine and/or phosphatidyiserine. Biochim. Biophys. Acta. 1107:12-22.
    • (1992) Biochim. Biophys. Acta. , vol.1107 , pp. 12-22
    • Duplaa, H.1    Convert, O.2    Sautereau, A.-M.3    Tocanne, J.-F.4    Chassaing, G.5
  • 15
    • 0030844208 scopus 로고    scopus 로고
    • Molecular dynamics simulation of unsaturated lipid bilayers at low hydration: Parametrization and comparison with diffraction studies
    • Feller, S. E., D. Yin, R. W. Pastor, and A. D. MacKerell, Jr. 1997. Molecular dynamics simulation of unsaturated lipid bilayers at low hydration: parametrization and comparison with diffraction studies. Biophys. J. 73:2269-2279.
    • (1997) Biophys. J. , vol.73 , pp. 2269-2279
    • Feller, S.E.1    Yin, D.2    Pastor, R.W.3    MacKerell A.D., Jr.4
  • 16
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • Feller, S. E., Y. Zhang, R. W. Pastor, and B. R. Brooks. 1995. Constant pressure molecular dynamics simulation: the Langevin piston method. J. Chem. Phys. 103:4613-4621.
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 17
    • 0017279976 scopus 로고
    • Synthesis and some biological activities of the tyrosine-8 analog of substance P
    • Fisher, G., K. Folkers, B. Pernow, and C. Bowers. 1976. Synthesis and some biological activities of the tyrosine-8 analog of substance P. J. Med. Chem. 19:325-328.
    • (1976) J. Med. Chem. , vol.19 , pp. 325-328
    • Fisher, G.1    Folkers, K.2    Pernow, B.3    Bowers, C.4
  • 18
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers: A polarized attenuated total reflection infrared study
    • Frey, S., and L. K. Tamm. 1991. Orientation of melittin in phospholipid bilayers: a polarized attenuated total reflection infrared study. Biophys. J. 60:922-930.
    • (1991) Biophys. J. , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 20
    • 0028340334 scopus 로고
    • Comparison of the conformation of active and nonactive backbone cyclic analogs of substance P as a tool to elucidate features of the bioactive conformation: NMR and molecular dynamics in DMSO and water
    • Grdadolnik, S. G., D. F. Mierke, G. Byk, I. Zeltser, C. Gilon, and H. Kessler, 1994. Comparison of the conformation of active and nonactive backbone cyclic analogs of substance P as a tool to elucidate features of the bioactive conformation: NMR and molecular dynamics in DMSO and water. J. Med Chem. 37:2145-2152.
    • (1994) J. Med Chem. , vol.37 , pp. 2145-2152
    • Grdadolnik, S.G.1    Mierke, D.F.2    Byk, G.3    Zeltser, I.4    Gilon, C.5    Kessler, H.6
  • 21
    • 0028103947 scopus 로고
    • Combined approach of NMR and molecular dynamics within a biphasic membrane mimetic. Conformation and orientation of the bradykinin antagonist Hoe. 140
    • Guba, W., R. Haessner, G. Breipohl, S. Henke, J. Knolle, V. Samagada, and H. Kessler. 1994. Combined approach of NMR and molecular dynamics within a biphasic membrane mimetic. Conformation and orientation of the bradykinin antagonist Hoe. 140. J. Am. Chem. Soc. 116:7532-7540.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 7532-7540
    • Guba, W.1    Haessner, R.2    Breipohl, G.3    Henke, S.4    Knolle, J.5    Samagada, V.6    Kessler, H.7
  • 22
    • 0003084634 scopus 로고
    • A novel computational mimetic of biological membranes in molecular dynamics simulations
    • Guba, W., and H. Kessler. 1994. A novel computational mimetic of biological membranes in molecular dynamics simulations. J. Phys. Chem. 98:23-27.
    • (1994) J. Phys. Chem. , vol.98 , pp. 23-27
    • Guba, W.1    Kessler, H.2
  • 23
    • 0029038366 scopus 로고
    • Interaction of an amphiphilic peptide with a phospho-lipid bilayer surface by molecular dynamics simulation study
    • Huang, P., and G. H. Loew. 1995. Interaction of an amphiphilic peptide with a phospho-lipid bilayer surface by molecular dynamics simulation study. J. Biomol. Struct. Dyn. 12:937-956.
    • (1995) J. Biomol. Struct. Dyn. , vol.12 , pp. 937-956
    • Huang, P.1    Loew, G.H.2
  • 24
    • 0028293626 scopus 로고
    • Interaction of substance P with the second and seventh transmembrane domains of the neurokinin-1 receptor
    • Huang, R. R. C., H. Yu, C. Strader, and T. M. Fong. 1994. Interaction of substance P with the second and seventh transmembrane domains of the neurokinin-1 receptor. Biochemistry. 33:3007-3013.
    • (1994) Biochemistry , vol.33 , pp. 3007-3013
    • Huang, R.R.C.1    Yu, H.2    Strader, C.3    Fong, T.M.4
  • 25
    • 0001404190 scopus 로고
    • Distance distribution function of sodium dodecylsulfate micelles by x-ray scattering
    • Itri, R., and L. Q. Amaral. 1991. Distance distribution function of sodium dodecylsulfate micelles by x-ray scattering. J. Phys. Chem. 95:423-427.
    • (1991) J. Phys. Chem. , vol.95 , pp. 423-427
    • Itri, R.1    Amaral, L.Q.2
  • 26
    • 0024558250 scopus 로고
    • The nature of the hydrophobic binding of small peptides at the bilayer interface: Implications for the insertion of transbilayer helices
    • Jacobs, R., and S. H. White. 1989. The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices. Biochemistry. 28:3421-3437.
    • (1989) Biochemistry , vol.28 , pp. 3421-3437
    • Jacobs, R.1    White, S.H.2
  • 29
    • 0028362891 scopus 로고
    • Design and synthesis of side-chain conformationally restricted phenylalanines and their use for structure-activity studies on tachykinin NK-1 receptor
    • Josien, H., S. Lavielle, A. Brunissen, M. Saffroy, Y. Torrens, J.-C. Beaujouan, J. Glowinski, and G. Chassaing, 1994. Design and synthesis of side-chain conformationally restricted phenylalanines and their use for structure-activity studies on tachykinin NK-1 receptor. J. Med. Chem. 37:1586-1601.
    • (1994) J. Med. Chem. , vol.37 , pp. 1586-1601
    • Josien, H.1    Lavielle, S.2    Brunissen, A.3    Saffroy, M.4    Torrens, Y.5    Beaujouan, J.-C.6    Glowinski, J.7    Chassaing, G.8
  • 30
    • 0029981186 scopus 로고    scopus 로고
    • The conformation of substance P in lipid environments
    • Keire, D., and T. Fletcher. 1996. The conformation of substance P in lipid environments. Biophys. J. 70:1716-1727.
    • (1996) Biophys. J. , vol.70 , pp. 1716-1727
    • Keire, D.1    Fletcher, T.2
  • 31
    • 0029930028 scopus 로고    scopus 로고
    • 260 ps molecular dynamics simulation of substance P with hydrated dimyristoylphosphatidyl choline bilayer
    • Kothekar, V. 1996. 260 ps molecular dynamics simulation of substance P with hydrated dimyristoylphosphatidyl choline bilayer. J. Biomol. Struct. Dyn. 13:601-613.
    • (1996) J. Biomol. Struct. Dyn. , vol.13 , pp. 601-613
    • Kothekar, V.1
  • 32
    • 0347963579 scopus 로고
    • Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution: Decreased fluidity of the micelle hydrocarbon interior
    • MacKerell, Jr., A. D. 1995. Molecular dynamics simulation analysis of a sodium dodecyl sulfate micelle in aqueous solution: decreased fluidity of the micelle hydrocarbon interior. J. Phys. Chem. 99:1846-1855.
    • (1995) J. Phys. Chem. , vol.99 , pp. 1846-1855
    • MacKerell A.D., Jr.1
  • 35
    • 0001013607 scopus 로고    scopus 로고
    • How does the electrostatic force cut-off generate non-uniform temperature distributions in proteins?
    • Oda, K., H. Miyagawa, and K. Kitamura. 1996. How does the electrostatic force cut-off generate non-uniform temperature distributions in proteins? Mol. Sim. 16:167-177.
    • (1996) Mol. Sim. , vol.16 , pp. 167-177
    • Oda, K.1    Miyagawa, H.2    Kitamura, K.3
  • 36
    • 0030861070 scopus 로고    scopus 로고
    • NMR and membrane proteins
    • Opella, S. J. 1997. NMR and Membrane Proteins. Nat. Struct. Biol., NMR Suppl. 845-848.
    • (1997) Nat. Struct. Biol., NMR , Issue.SUPPL. , pp. 845-848
    • Opella, S.J.1
  • 37
    • 0000385768 scopus 로고
    • STRIPS: An algorithm for generating two-dimensional hydrogen-bond topology diagrams for proteins
    • The American Chemical Society, Washington. DC
    • Ravishanker, G., S. Vijakumar, and D. L. Beveridge. 1994. STRIPS: An algorithm for generating two-dimensional hydrogen-bond topology diagrams for proteins. In Modeling the Hydrogen Bond. The American Chemical Society, Washington. DC. 209-219.
    • (1994) Modeling the Hydrogen Bond , pp. 209-219
    • Ravishanker, G.1    Vijakumar, S.2    Beveridge, D.L.3
  • 38
    • 0024278757 scopus 로고
    • Hydrophobicity of the peptide C=O-H-N hydrogen bonded group
    • Roseman, M. A. 1988. Hydrophobicity of the peptide C=O-H-N hydrogen bonded group. J. Mol. Biol. 201:621-625.
    • (1988) J. Mol. Biol. , vol.201 , pp. 621-625
    • Roseman, M.A.1
  • 39
    • 0002937720 scopus 로고    scopus 로고
    • Molecular dynamics of Pf1 coat protein in a phospholipid bilayer
    • K. M. Merz, Jr., and B. Roux, editors. Birkhäuser, Boston
    • Roux, B., and T. B. Woolf. 1996. Molecular dynamics of Pf1 coat protein in a phospholipid bilayer. In Biological Membranes: A Molecular Perspective from Computation and Experiment. K. M. Merz, Jr., and B. Roux, editors. Birkhäuser, Boston. 555-587.
    • (1996) Biological Membranes: A Molecular Perspective from Computation and Experiment , pp. 555-587
    • Roux, B.1    Woolf, T.B.2
  • 40
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J.-P., G. Cicotti, and H. J. C. Berendsen 1977. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23: 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Cicotti, G.2    Berendsen, H.J.C.3
  • 41
    • 0028947465 scopus 로고
    • Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for nmr studies
    • Sanders, C. R., and G. C. Landis. 1995. Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for nmr studies. Biochemistry. 43:4030-4040.
    • (1995) Biochemistry , vol.43 , pp. 4030-4040
    • Sanders, C.R.1    Landis, G.C.2
  • 43
    • 0000404051 scopus 로고
    • Conformations and orientations of amphiphilic peptides induced by artificial lipid membranes: Correlations with biological activity
    • Schwyzer, R. 1992. Conformations and orientations of amphiphilic peptides induced by artificial lipid membranes: correlations with biological activity. Chemtracts-Biochem. and Mol. Biol. 3:347-379.
    • (1992) Chemtracts-Biochem. and Mol. Biol. , vol.3 , pp. 347-379
    • Schwyzer, R.1
  • 44
    • 0028903022 scopus 로고
    • 100-Year lock-and-key concept: Are peptide keys shaped and guided to their receptors by the target cell membrane?
    • Schwyzer, R. 1995. 100-Year lock-and-key concept: are peptide keys shaped and guided to their receptors by the target cell membrane? Biopolymers. 37:5-16.
    • (1995) Biopolymers , vol.37 , pp. 5-16
    • Schwyzer, R.1
  • 45
    • 0029989652 scopus 로고    scopus 로고
    • Binding of substance P agonists to lipid membranes and to the neurokinin-1 receptor
    • Seelig, A., T. Alt, S. Lotz, and G. Holzemann. 1996. Binding of substance P agonists to lipid membranes and to the neurokinin-1 receptor. Biochemistry. 35:4365-4374.
    • (1996) Biochemistry , vol.35 , pp. 4365-4374
    • Seelig, A.1    Alt, T.2    Lotz, S.3    Holzemann, G.4
  • 46
    • 0024571766 scopus 로고
    • Binding of a neuropeptide, substance P, to neutral and negatively charged lipids
    • Seelig, A., and P. M. Macdonald. 1989. Binding of a neuropeptide, substance P, to neutral and negatively charged lipids. Biochemistry. 28: 2490-2496.
    • (1989) Biochemistry , vol.28 , pp. 2490-2496
    • Seelig, A.1    Macdonald, P.M.2
  • 48
    • 0030966534 scopus 로고    scopus 로고
    • Transmembrane helix structure, dynamics, and interactions: Multi-nanosecond molecular dynamics simulations
    • Shen, L., D. Bassolino, and T. Stouch. 1997. Transmembrane helix structure, dynamics, and interactions: multi-nanosecond molecular dynamics simulations. Biophys. J. 73:3-20.
    • (1997) Biophys. J. , vol.73 , pp. 3-20
    • Shen, L.1    Bassolino, D.2    Stouch, T.3
  • 51
    • 84986534166 scopus 로고
    • New spherical-cutoff methods for long range forces in macromolecular simulation
    • Steinbach, P., and B. R. Brooks. 1994. New spherical-cutoff methods for long range forces in macromolecular simulation. J. Camp. Chem. 15: 667-683.
    • (1994) J. Camp. Chem. , vol.15 , pp. 667-683
    • Steinbach, P.1    Brooks, B.R.2
  • 52
    • 0030031374 scopus 로고    scopus 로고
    • Molecular dynamics investigation of the structure of a fully hydrated gel-phase dipalmitoylphosphatidylcholine bilayer
    • Tu, K., D. J. Tobias, J. K. Blasie, and M. L. Klein. 1996. Molecular dynamics investigation of the structure of a fully hydrated gel-phase dipalmitoylphosphatidylcholine bilayer. Biophys. J. 70:595-608.
    • (1996) Biophys. J. , vol.70 , pp. 595-608
    • Tu, K.1    Tobias, D.J.2    Blasie, J.K.3    Klein, M.L.4
  • 53
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphospatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure
    • Weiner, M. C., and S. H. White. 1992. Structure of a fluid dioleoylphospatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure. Biophys J. 61: 434-447.
    • (1992) Biophys J. , vol.61 , pp. 434-447
    • Weiner, M.C.1    White, S.H.2
  • 54
    • 0028013531 scopus 로고
    • Peptides in lipid bilayers: Structural and thermodynamic basts for partitioning and folding
    • White, S., and W. C. Wimley. 1994. Peptides in lipid bilayers: structural and thermodynamic basts for partitioning and folding. Curr. Opin. Struct. Biol. 4:79-86.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 79-86
    • White, S.1    Wimley, W.C.2
  • 55
    • 0025306162 scopus 로고
    • Secondary structure of substance P bound to liposomes in organic solvents and in solution from Raman and CD spectroscopy
    • Williams, R. W., and J. L. Weaver. 1990. Secondary structure of substance P bound to liposomes in organic solvents and in solution from Raman and CD spectroscopy. J. Biol. Chem. 265:2505-2513.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2505-2513
    • Williams, R.W.1    Weaver, J.L.2
  • 56
    • 0025113022 scopus 로고
    • β-Turns and their distortions: A proposed new nomenclature
    • Wilmot, C. M., and J. M, Thorton. 1990. β-Turns and their distortions: a proposed new nomenclature. Protein Eng. 3:479-493.
    • (1990) Protein Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thorton, J.M.2
  • 57
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 58
    • 0032048510 scopus 로고    scopus 로고
    • The temperature dependence and thermodynamic functions of partitioning of substance P peptides in dodecylphosphocholine micelles
    • Wong, T. C., and X. Gao. 1998. The temperature dependence and thermodynamic functions of partitioning of substance P peptides in dodecylphosphocholine micelles. Biopolymers. 45:395-403.
    • (1998) Biopolymers , vol.45 , pp. 395-403
    • Wong, T.C.1    Gao, X.2
  • 59
    • 0031961813 scopus 로고    scopus 로고
    • Molecular-dynamics simulations of individual α-helices of bacteriorhodopsin in dimyristoylphosphatidylcholine. II. Interaction energy analysis
    • Woolf, T. B. 1998. Molecular-dynamics simulations of individual α-helices of bacteriorhodopsin in dimyristoylphosphatidylcholine. II. Interaction energy analysis. Biophys. J. 74:115-131.
    • (1998) Biophys. J. , vol.74 , pp. 115-131
    • Woolf, T.B.1
  • 60
    • 0344054203 scopus 로고    scopus 로고
    • Helix:Lipid interactions in glycophorin dimerization: Molecular dynamics calculations
    • Woolf, T. B., A. Grossfield, K. MacKenzie, and D. Engelman. 1998. Helix:lipid interactions in glycophorin dimerization: molecular dynamics calculations. Biophys. J. 74:A15.
    • (1998) Biophys. J. , vol.74
    • Woolf, T.B.1    Grossfield, A.2    MacKenzie, K.3    Engelman, D.4
  • 61
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetic, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer
    • Woolf, T. B. and B. Roux. 1996. Structure, energetic, and dynamics of lipid-protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins: Struct., Funct., Genet. 24:92-114.
    • (1996) Proteins: Struct., Funct., Genet. , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 62
    • 0001536504 scopus 로고
    • Peptides in membranes: Lipid-induced secondary structure of substance P
    • Woolley, G. A., and C. M. Deber. 1987. Peptides in membranes: lipid-induced secondary structure of substance P. Biopolymers. 26: S109-S121.
    • (1987) Biopolymers , vol.26
    • Woolley, G.A.1    Deber, C.M.2
  • 63
    • 0028019634 scopus 로고
    • NMR and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles
    • Young, J. K., C. Anklin, and R. P. Hicks. 1994. NMR and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles. Biopolymers. 34:1449-1462.
    • (1994) Biopolymers , vol.34 , pp. 1449-1462
    • Young, J.K.1    Anklin, C.2    Hicks, R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.