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Volumn 76, Issue 3, 1999, Pages 1199-1212

Molecular dynamics study of substance P peptides in a biphasic membrane mimic

Author keywords

[No Author keywords available]

Indexed keywords

SUBSTANCE P; TYROSINE DERIVATIVE;

EID: 0032982468     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77284-X     Document Type: Article
Times cited : (34)

References (73)
  • 1
    • 33751155832 scopus 로고
    • Molecular dynamics simulations of signal sequences at a membrane/water interface
    • Area, E. P., P. G. Pascutti, S. Schreier, K. Mundim, and P. M. Bisch. 1995. Molecular dynamics simulations of signal sequences at a membrane/water interface. J. Phys. Chem. 99:14885-14892.
    • (1995) J. Phys. Chem. , vol.99 , pp. 14885-14892
    • Area, E.P.1    Pascutti, P.G.2    Schreier, S.3    Mundim, K.4    Bisch, P.M.5
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0011613265 scopus 로고    scopus 로고
    • Molecular dynamics simulation of melittin in a dimyristoylphosphaddylcholine bilayer membrane
    • Beraéche, S., M. Nina, and B. Roux. 1998. Molecular dynamics simulation of melittin in a dimyristoylphosphaddylcholine bilayer membrane. Biophys. J. 75:1603-1618.
    • (1998) Biophys. J. , vol.75 , pp. 1603-1618
    • Beraéche, S.1    Nina, M.2    Roux, B.3
  • 5
    • 0031022167 scopus 로고    scopus 로고
    • Simulation studies of alamethicin-bilayer interactions
    • Biggin, P. C., J. Breed, H. S. Son, and M. S. P. Sansom. 1997. Simulation studies of alamethicin-bilayer interactions. Biophys. J. 72:627-636.
    • (1997) Biophys. J. , vol.72 , pp. 627-636
    • Biggin, P.C.1    Breed, J.2    Son, H.S.3    Sansom, M.S.P.4
  • 6
    • 0343697622 scopus 로고    scopus 로고
    • A protocol for the interpretation of side-chain dynamics based on NMR relaxation: Application to phenylalanines in antamanide
    • Bremi, T., R. Bruschweiler, and R. R. Ernst. 1997. A protocol for the interpretation of side-chain dynamics based on NMR relaxation: application to phenylalanines in antamanide. J. Am. Chem. Soc. 119: 4272-4284.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4272-4284
    • Bremi, T.1    Bruschweiler, R.2    Ernst, R.R.3
  • 8
    • 0001031179 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure, and thermodynamics
    • Brooks, C. L. III, M. Karplus, and B. M. Pettitt. 1988. Proteins: a theoretical perspective of dynamics, structure, and thermodynamics. Adv. Chem. Phys. Vol. 71.
    • (1988) Adv. Chem. Phys. , vol.71
    • Brooks C.L. III1    Karplus, M.2    Pettitt, B.M.3
  • 10
    • 0030573120 scopus 로고    scopus 로고
    • 4 liquid-liquid interface with polarizable potential models
    • 4 liquid-liquid interface with polarizable potential models. Chem. Phys. Lett. 263: 39-45.
    • (1996) Chem. Phys. Lett. , vol.263 , pp. 39-45
    • Chang, T.-M.1    Dang, L.X.2
  • 11
    • 33748569506 scopus 로고    scopus 로고
    • Investigation of surfactant conformation and order at the liquid-liquid interface by total internal reflection sum-frequency vibrational spectroscopy
    • Conboy, J. C., M. C. Messmer, and G. L. Richmond. 1996. Investigation of surfactant conformation and order at the liquid-liquid interface by total internal reflection sum-frequency vibrational spectroscopy. J. Phys. Chem. 100:7617-7622.
    • (1996) J. Phys. Chem. , vol.100 , pp. 7617-7622
    • Conboy, J.C.1    Messmer, M.C.2    Richmond, G.L.3
  • 12
    • 0028807770 scopus 로고
    • Interaction of the fusion inhibiting peptide carbobenzoxy-D-Phe-L-Phe-Gly with N-methyldioleoylphosphatidylethanolamine lipid bilayers
    • Damodaran, K. V., and K. M. Merz. 1995. Interaction of the fusion inhibiting peptide carbobenzoxy-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
  • 13
    • 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
  • 14
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • Dathe. M., M. Schumann, T. Wieprecht, A. Winkler, M. Beyermann, E. Krause, K. Matsuzaki, O. Murase, and M. Bienert. 1996. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry. 35:12612-12622.
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Schumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9
  • 15
    • 0026653453 scopus 로고
    • Binding of substance P to monolayers and vesicles made of phosphatidylcholine and/or phophatidylserine
    • Duplaa, H., O. Convert, A.-M. Sautereau, J.-F. Tocanne, and G. Chassaing. 1992. Binding of substance P to monolayers and vesicles made of phosphatidylcholine and/or phophatidylserine. 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
  • 16
    • 0022913431 scopus 로고
    • Membrane structure of substance P III. Secondary structure of substance P in 2,2,2-trifluoroethanol, methanol, and on flat lipid membrane studied by infrared spectroscopy
    • Erne, D., K. Rolka, and R. Schwyzer. 1986. Membrane structure of substance P III. Secondary structure of substance P in 2,2,2-trifluoroethanol, methanol, and on flat lipid membrane studied by infrared spectroscopy. Helv. Chim. Acta. 69:1807-1816.
    • (1986) Helv. Chim. Acta. , vol.69 , pp. 1807-1816
    • Erne, D.1    Rolka, K.2    Schwyzer, R.3
  • 17
    • 0042943378 scopus 로고
    • Theoretical determination of partition coefficients
    • Essex, J. W., C. A. Reynolds, and W. G. Richards. 1992. Theoretical determination of partition coefficients. J. Am. Chem. Soc. 114: 3634-3639.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3634-3639
    • Essex, J.W.1    Reynolds, C.A.2    Richards, W.G.3
  • 18
    • 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
  • 19
    • 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
    • 0031920741 scopus 로고    scopus 로고
    • Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion
    • Gao, X.-F., and T. C. Wong. 1998. Studies of the binding and structure of adrenocorticotropin peptides in membrane mimics by NMR spectroscopy and pulsed-field gradient diffusion. Biophys. J. 74:1871-1888.
    • (1998) Biophys. J. , vol.74 , pp. 1871-1888
    • Gao, X.-F.1    Wong, T.C.2
  • 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. Santagada, 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    Santagada, 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
    • 0029959846 scopus 로고    scopus 로고
    • Mechanism of alamethicin insertion into lipid bilayers
    • He, K., S. J. Ludtke, W. T. Heller, and H. W. Huang. 1996. Mechanism of alamethicin insertion into lipid bilayers. Biophys. J. 71:2669-2679.
    • (1996) Biophys. J. , vol.71 , pp. 2669-2679
    • He, K.1    Ludtke, S.J.2    Heller, W.T.3    Huang, H.W.4
  • 24
    • 0026510813 scopus 로고
    • The interactions of neuropeptides with membrane model systems: A case study
    • Hicks, R. P., D. J. Beard, and J. K. Young. 1992. The interactions of neuropeptides with membrane model systems: a case study. Biopolymers. 32:85-96.
    • (1992) Biopolymers , vol.32 , pp. 85-96
    • Hicks, R.P.1    Beard, D.J.2    Young, J.K.3
  • 25
    • 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
  • 26
    • 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
  • 27
    • 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
    • 0013358476 scopus 로고
    • Secondary structure of proteins and peptides in amphiphilic environments
    • Kaiser, E. T., and F. J. Kezdy. 1983. Secondary structure of proteins and peptides in amphiphilic environments. Proc. Natl. Acad. Sci. USA. 80:1137-1140.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1137-1140
    • Kaiser, E.T.1    Kezdy, F.J.2
  • 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 dimyristoyl phosphatidyl choline bilayer
    • Kothekar, V. 1996. 260-ps molecular dynamics simulation of substance P with hydrated dimyristoyl phosphatidyl choline bilayer. J. Biomol. Struct. Dyn. 13:601-613.
    • (1996) J. Biomol. Struct. Dyn. , vol.13 , pp. 601-613
    • Kothekar, V.1
  • 34
    • 0031542249 scopus 로고    scopus 로고
    • Structure, dynamics, and topological orientation of the polyether, ionophore antibiotic monensin, in a micellar environment
    • Mercurio, E., M. Pellegrini, and D. F. Mierke. 1997. Structure, dynamics, and topological orientation of the polyether, ionophore antibiotic monensin, in a micellar environment. Biopolymers. 42:759-769.
    • (1997) Biopolymers , vol.42 , pp. 759-769
    • Mercurio, E.1    Pellegrini, M.2    Mierke, D.F.3
  • 37
    • 0001036148 scopus 로고
    • Liquid carbon tetrachloride: Atom pair correlation functions from neutron and x-ray diffraction
    • Narten, A. H. 1976. Liquid carbon tetrachloride: atom pair correlation functions from neutron and x-ray diffraction. J. Chem Phys. 65:573-579.
    • (1976) J. Chem Phys. , vol.65 , pp. 573-579
    • Narten, A.H.1
  • 39
    • 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
  • 40
    • 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
  • 41
    • 0030217514 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of biopolymer dynamics
    • Palmer III, A. G., J. Williams, and A. McDermott. 1996. Nuclear magnetic resonance studies of biopolymer dynamics. J. Phys. Chem. 100: 13293-13310.
    • (1996) J. Phys. Chem. , vol.100 , pp. 13293-13310
    • Palmer A.G. III1    Williams, J.2    McDermott, A.3
  • 42
    • 0003088538 scopus 로고    scopus 로고
    • Second-harmonic generation measurements of electrostatic biopolymer-surfactant coadsorption at the water/1,2-dichloroethane interface
    • Paul, H. J., and R. M. Corn. 1997. Second-harmonic generation measurements of electrostatic biopolymer-surfactant coadsorption at the water/1,2-dichloroethane interface. J. Phys. Chem. B. 101:4494-4497.
    • (1997) J. Phys. Chem. B. , vol.101 , pp. 4494-4497
    • Paul, H.J.1    Corn, R.M.2
  • 43
    • 0030614857 scopus 로고    scopus 로고
    • 6-bradykinin: Molecular dynamics simulation in a biphasic membrane mimetic
    • 6-bradykinin: molecular dynamics simulation in a biphasic membrane mimetic. J. Med. Chem. 40:99-104.
    • (1997) J. Med. Chem. , vol.40 , pp. 99-104
    • Pellegrini, M.1    Mierke, D.F.2
  • 44
    • 0006619522 scopus 로고    scopus 로고
    • Investigations of peptide hydration using NMR and molecular dynamics simulation: A study of effects of water on the conformation and dynamics of antamanide
    • Peng, J., C. Schiffer, P. Xu, W. F. van Gunsteren, and R. R. Ernst. 1996. Investigations of peptide hydration using NMR and molecular dynamics simulation: a study of effects of water on the conformation and dynamics of antamanide. J. Biomol. NMR. 8:453-456.
    • (1996) J. Biomol. NMR , vol.8 , pp. 453-456
    • Peng, J.1    Schiffer, C.2    Xu, P.3    Van Gunsteren, W.F.4    Ernst, R.R.5
  • 45
    • 0030877076 scopus 로고    scopus 로고
    • Accuracy and precision of NMR relaxation experiments and MD simulations for characterizing protein dynamics
    • Philippopoulos, M., A. Mandel, A. G. Palmer III, and C. Lim. 1997. Accuracy and precision of NMR relaxation experiments and MD simulations for characterizing protein dynamics. Proteins: Struct., Funct., Genet. 28:481-493.
    • (1997) Proteins: Struct., Funct., Genet. , vol.28 , pp. 481-493
    • Philippopoulos, M.1    Mandel, A.2    Palmer A.G. III3    Lim, C.4
  • 46
    • 0030112112 scopus 로고    scopus 로고
    • Interactions of anesthetics with the membrane-water interface
    • Pohorille, A., P. Cieplak, and M. A. Wilson. 1996. Interactions of anesthetics with the membrane-water interface. Chem. Phys. 204:337-345.
    • (1996) Chem. Phys. , vol.204 , pp. 337-345
    • Pohorille, A.1    Cieplak, P.2    Wilson, M.A.3
  • 47
    • 0000385768 scopus 로고
    • STRIPS: An algorithm for generating two-dimensional hydrogen-bond topology diagrams for proteins
    • 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. 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
  • 48
    • 0028589913 scopus 로고
    • Receptors and antagonists for substance P and related peptides
    • Regoli, D., A. Bouden, and J. L. Fauchere. 1994. Receptors and antagonists for substance P and related peptides. Pharmacol. Rev. 46:551-599.
    • (1994) Pharmacol. Rev. , vol.46 , pp. 551-599
    • Regoli, D.1    Bouden, A.2    Fauchere, J.L.3
  • 50
    • 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
  • 51
    • 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
  • 52
    • 0038757797 scopus 로고
    • Membrane lipid phase as catalyst for peptide-receptor interactions
    • Sargent, D. F., and R. Schwyzer. 1986. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc. Natl. Acad. Sci. USA. 83: 5774-5778.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5774-5778
    • Sargent, D.F.1    Schwyzer, R.2
  • 53
    • 0000404051 scopus 로고
    • Conformations and orientations of araphiphilic peptides induced by artificial lipid membranes: Correlations with biological activity
    • Schwyzer, R. 1992. Conformations and orientations of araphiphilic 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
  • 54
    • 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
  • 55
    • 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
  • 57
    • 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
  • 59
    • 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. Comp. Chem. 15: 667-683.
    • (1994) J. Comp. Chem. , vol.15 , pp. 667-683
    • Steinbach, P.1    Brooks, B.R.2
  • 60
    • 0030029471 scopus 로고    scopus 로고
    • Direct determination of membrane affinities of individual amino acids
    • Thorgeirsson, T. E., C. J. Russell, D. S. King, and Y. K. Shin. 1996. Direct determination of membrane affinities of individual amino acids. Biochemistry. 35:1803-1809.
    • (1996) Biochemistry , vol.35 , pp. 1803-1809
    • Thorgeirsson, T.E.1    Russell, C.J.2    King, D.S.3    Shin, Y.K.4
  • 61
    • 0041785053 scopus 로고    scopus 로고
    • A molecular dynamics simulation study of liquid carbon tetrachloride
    • Tironi, I. G., P. Fontana, and W. F. van Gunsteren. 1996. A molecular dynamics simulation study of liquid carbon tetrachloride. Mol. Sim. 18:1-11.
    • (1996) Mol. Sim. , vol.18 , pp. 1-11
    • Tironi, I.G.1    Fontana, P.2    Van Gunsteren, W.F.3
  • 62
    • 0029769798 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a protein on hydrophobic and hydrophilic surfaces
    • Tobias, D. J., W. Mar, J. K. Blasie, and M. L. Klein. 1996. Molecular dynamics simulations of a protein on hydrophobic and hydrophilic surfaces. Biophys. J. 71:2933.
    • (1996) Biophys. J. , vol.71 , pp. 2933
    • Tobias, D.J.1    Mar, W.2    Blasie, J.K.3    Klein, M.L.4
  • 63
    • 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
  • 64
    • 0028013531 scopus 로고
    • Peptides in lipid bilayers: Structural and thermodynamic basis for partitioning and folding
    • White, S., and W. C. Wimley. 1994. Peptides in lipid bilayers: structural and thermodynamic basis 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
  • 65
    • 0001274118 scopus 로고
    • Origin of the stability of carbon tetrafluoride: Negative hyperconjugation reexamined
    • Wiberg, K. B., and P. R. Rablen. 1993. Origin of the stability of carbon tetrafluoride: negative hyperconjugation reexamined. J. Am. Chem. Soc. 115:614-625.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 614-625
    • Wiberg, K.B.1    Rablen, P.R.2
  • 66
    • 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
  • 67
    • 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
  • 68
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley, W. C., T. P. Creamer, and S. H. White. 1996. Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry. 35:5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 69
    • 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
  • 70
    • 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
  • 71
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, 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, energetics, and dynamics of lipid-protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins: Struct., Fund, Genet. 24: 92-114.
    • (1996) Proteins: Struct., Fund, Genet. , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 72
    • 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
  • 73
    • 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


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