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Volumn 72, Issue 1, 2008, Pages 299-312

How to lose a kink and gain a helix: PH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers

Author keywords

Conformational change; Folding in lipid bilayers; Influenza fusion peptide; Lipid protein interactions; Mixed lipid bilayer; Thermodynamics of membrane fusion

Indexed keywords

HEMAGGLUTININ; LIPID;

EID: 44949233215     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21925     Document Type: Article
Times cited : (20)

References (61)
  • 1
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DC. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 2000;69:531-569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 2
    • 0026492542 scopus 로고
    • Membrane fusion
    • White JM. Membrane fusion. Science 1992;258:917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 4
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion
    • Stegmann T, Delfino JM, Richards FM, Helenius A. The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. J Biol Chem 1991;266:18404-18410.
    • (1991) J Biol Chem , vol.266 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, F.M.3    Helenius, A.4
  • 5
    • 0036231335 scopus 로고    scopus 로고
    • New insights into the spring-loaded conformational change of influenza virus hemagglutinin
    • Gruenke JA, Armstrong RT, Newcomb WW, Brown JC, White JM. New insights into the spring-loaded conformational change of influenza virus hemagglutinin. J Virol 2002;76:4456-4466.
    • (2002) J Virol , vol.76 , pp. 4456-4466
    • Gruenke, J.A.1    Armstrong, R.T.2    Newcomb, W.W.3    Brown, J.C.4    White, J.M.5
  • 6
    • 0031793435 scopus 로고    scopus 로고
    • pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers
    • Gray C, Tamm LK. pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers. Protein Sci 1998;7:2359-2373.
    • (1998) Protein Sci , vol.7 , pp. 2359-2373
    • Gray, C.1    Tamm, L.K.2
  • 7
    • 0035950593 scopus 로고    scopus 로고
    • Role of the Glu residues of the influenza hemagglutinin fusion peptide in the pH dependence of fusion activity
    • Korte T, Epand RF, Epand RM, Blumenthal R. Role of the Glu residues of the influenza hemagglutinin fusion peptide in the pH dependence of fusion activity. Virology 2001;289:353-361.
    • (2001) Virology , vol.289 , pp. 353-361
    • Korte, T.1    Epand, R.F.2    Epand, R.M.3    Blumenthal, R.4
  • 8
    • 0035979369 scopus 로고    scopus 로고
    • Membrane interactions of mutated forms of the influenza fusion peptide
    • Epand RM, Epand RF, Martin I, Ruysschaert JM. Membrane interactions of mutated forms of the influenza fusion peptide. Biochemistry 2001;40:8800-8807.
    • (2001) Biochemistry , vol.40 , pp. 8800-8807
    • Epand, R.M.1    Epand, R.F.2    Martin, I.3    Ruysschaert, J.M.4
  • 9
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer DA, Wharton SA, Skehel JJ, Wiley DC. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J Virol 1995;69:6643-6651.
    • (1995) J Virol , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 10
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
    • Qiao H, Armstrong RT, Melikyan GB, Cohen FS, White JM. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. Mol Biol Cell 1999;10:2759-2769.
    • (1999) Mol Biol Cell , vol.10 , pp. 2759-2769
    • Qiao, H.1    Armstrong, R.T.2    Melikyan, G.B.3    Cohen, F.S.4    White, J.M.5
  • 11
    • 0034671359 scopus 로고    scopus 로고
    • pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers
    • Han X, Tamm LK. pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers. J Mol Biol 2000;304:953-965.
    • (2000) J Mol Biol , vol.304 , pp. 953-965
    • Han, X.1    Tamm, L.K.2
  • 12
    • 0038131038 scopus 로고    scopus 로고
    • Thermodynamics of fusion peptide-membrane interactions
    • Li Y, Han X, Tamm LK. Thermodynamics of fusion peptide-membrane interactions. Biochemistry 2003;42:7245-7251.
    • (2003) Biochemistry , vol.42 , pp. 7245-7251
    • Li, Y.1    Han, X.2    Tamm, L.K.3
  • 13
    • 0034700147 scopus 로고    scopus 로고
    • A host-guest system to study structure-function relationships of membrane fusion peptides
    • Han X, Tamm LK. A host-guest system to study structure-function relationships of membrane fusion peptides. Proc Natl Acad Sci USA 2000;97:13097-13102.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13097-13102
    • Han, X.1    Tamm, L.K.2
  • 14
    • 0033539603 scopus 로고    scopus 로고
    • Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: Probing the role of hydrophobic residue size in the central region of the fusion peptide
    • Han X, Steinhauer DA, Wharton SA, Tamm LK. Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: probing the role of hydrophobic residue size in the central region of the fusion peptide. Biochemistry 1999;38:15052-15059.
    • (1999) Biochemistry , vol.38 , pp. 15052-15059
    • Han, X.1    Steinhauer, D.A.2    Wharton, S.A.3    Tamm, L.K.4
  • 15
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han X, Bushweller JH, Cafiso DS, Tamm LK. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat Struct Biol 2001;8:715-720.
    • (2001) Nat Struct Biol , vol.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 16
    • 33646831343 scopus 로고    scopus 로고
    • Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity
    • Lai AL, Park H, White JM, Tamm LK. Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity. J Biol Chem 2006;281:5760-5770.
    • (2006) J Biol Chem , vol.281 , pp. 5760-5770
    • Lai, A.L.1    Park, H.2    White, J.M.3    Tamm, L.K.4
  • 17
    • 31544474848 scopus 로고    scopus 로고
    • pH-induced helix-coil transition of amphipathic polypeptide and its association with the lipid bilayer: Electrostatic energy calculation
    • Choi HS, Huh J, Jo WH. pH-induced helix-coil transition of amphipathic polypeptide and its association with the lipid bilayer: electrostatic energy calculation. Biomacromolecules 2006;7:403-406.
    • (2006) Biomacromolecules , vol.7 , pp. 403-406
    • Choi, H.S.1    Huh, J.2    Jo, W.H.3
  • 18
    • 3042857547 scopus 로고    scopus 로고
    • Bilayer conformation of fusion peptide of influenza virus hemagglutinin: A molecular dynamics simulation study
    • Huang Q, Chen CL, Herrmann A. Bilayer conformation of fusion peptide of influenza virus hemagglutinin: a molecular dynamics simulation study. Biophys J 2004;87:14-22.
    • (2004) Biophys J , vol.87 , pp. 14-22
    • Huang, Q.1    Chen, C.L.2    Herrmann, A.3
  • 20
    • 28144436374 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the influenza hemagglutinin fusion peptide in micelles and bilayers: Conformational analysis of peptide and lipids
    • Lague P, Roux B, Pastor RW. Molecular dynamics simulations of the influenza hemagglutinin fusion peptide in micelles and bilayers: conformational analysis of peptide and lipids. J Mol Biol 2005;354:1129-1141.
    • (2005) J Mol Biol , vol.354 , pp. 1129-1141
    • Lague, P.1    Roux, B.2    Pastor, R.W.3
  • 22
    • 0032714393 scopus 로고    scopus 로고
    • Factors important for fusogenic activity of peptides: Molecular modeling study of analogs of fusion peptide of influenza virus hemagglutinin
    • Efremov RG, Nolde DE, Volynsky PE, Chernyavsky AA, Dubovskii PV, Arseniev AS. Factors important for fusogenic activity of peptides: molecular modeling study of analogs of fusion peptide of influenza virus hemagglutinin. FEBS Lett 1999;462:205-210.
    • (1999) FEBS Lett , vol.462 , pp. 205-210
    • Efremov, R.G.1    Nolde, D.E.2    Volynsky, P.E.3    Chernyavsky, A.A.4    Dubovskii, P.V.5    Arseniev, A.S.6
  • 23
    • 0030041468 scopus 로고    scopus 로고
    • Structural study of the interaction between the SIV fusion peptide and model membranes
    • Colotto A, Martin I, Ruysschaert JM, Sen A, Hui SW, Epand RM. Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry 1996;35:980-989.
    • (1996) Biochemistry , vol.35 , pp. 980-989
    • Colotto, A.1    Martin, I.2    Ruysschaert, J.M.3    Sen, A.4    Hui, S.W.5    Epand, R.M.6
  • 24
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand RM. Lipid polymorphism and protein-lipid interactions. Biochim Biophys Acta 1998;1376:353-368.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 25
    • 0034730436 scopus 로고    scopus 로고
    • Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: Implications for membrane fusion mechanisms
    • Siegel DP, Epand RM. Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: implications for membrane fusion mechanisms. Biochim Biophys Acta 2000;1468:87-98.
    • (2000) Biochim Biophys Acta , vol.1468 , pp. 87-98
    • Siegel, D.P.1    Epand, R.M.2
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 27
    • 84986512474 scopus 로고    scopus 로고
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. Charmm - a program for macromolecular energy, minimization, and dynamics calculations. J Comp Chem 1983;4:187-217.
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. Charmm - a program for macromolecular energy, minimization, and dynamics calculations. J Comp Chem 1983;4:187-217.
  • 28
    • 0022583145 scopus 로고
    • A simple way to calculate the axis of an alpha helix
    • Aqvist J. A simple way to calculate the axis of an alpha helix. Comput Chem 1986;10:97-99.
    • (1986) Comput Chem , vol.10 , pp. 97-99
    • Aqvist, J.1
  • 30
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • Frishman D, Argos P. Knowledge-based protein secondary structure assignment. Proteins 1995;23:566-579.
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 32
    • 0000945413 scopus 로고    scopus 로고
    • Conformational sampling with Poisson-Boltzmann forces and a stochastic dynamics Monte Carlo method: Application to alanine dipeptide
    • Smart JL, Marrone TJ, McCammon JA. Conformational sampling with Poisson-Boltzmann forces and a stochastic dynamics Monte Carlo method: application to alanine dipeptide. J Comp Chem 1997;18:1750-1759.
    • (1997) J Comp Chem , vol.18 , pp. 1750-1759
    • Smart, J.L.1    Marrone, T.J.2    McCammon, J.A.3
  • 33
    • 33745911151 scopus 로고    scopus 로고
    • Multiple pathways in conformational transitions of the alanine dipeptide: An application of dynamic importance sampling
    • Jang H, Woolf TB. Multiple pathways in conformational transitions of the alanine dipeptide: an application of dynamic importance sampling. J Comput Chem 2006;27:1136-1141.
    • (2006) J Comput Chem , vol.27 , pp. 1136-1141
    • Jang, H.1    Woolf, T.B.2
  • 34
    • 0031793435 scopus 로고    scopus 로고
    • pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers
    • Gray C, Tamm LK. pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers. Protein Sci 1998;7:2359-2373.
    • (1998) Protein Sci , vol.7 , pp. 2359-2373
    • Gray, C.1    Tamm, L.K.2
  • 35
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie KR, Prestegard JH, Engelman DM. A transmembrane helix dimer: structure and implications. Science 1997;276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 36
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ WP, Engelman DM. The GxxxG motif: a framework for transmembrane helix-helix association. J Mol Biol 2000;296:911-919.
    • (2000) J Mol Biol , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 37
    • 0037076540 scopus 로고    scopus 로고
    • GXXXG and AXXXA: Common alpha-helical interaction motifs in proteins, particularly in extremophiles
    • Kleiger G, Grothe R, Mallick P, Eisenberg D. GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles. Biochemistry 2002;41:5990-5997.
    • (2002) Biochemistry , vol.41 , pp. 5990-5997
    • Kleiger, G.1    Grothe, R.2    Mallick, P.3    Eisenberg, D.4
  • 38
    • 1942504108 scopus 로고    scopus 로고
    • Tools for channels: Moving towards molecular calculations of gating and permeation in ion channel biophysics
    • Woolf TB, Zuckerman DM, Lu N, Jang H. Tools for channels: moving towards molecular calculations of gating and permeation in ion channel biophysics. J Mol Graph Model 2004;22:359-368.
    • (2004) J Mol Graph Model , vol.22 , pp. 359-368
    • Woolf, T.B.1    Zuckerman, D.M.2    Lu, N.3    Jang, H.4
  • 40
    • 0028020035 scopus 로고
    • Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer
    • Woolf TB, Roux B. Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer. Proc Natl Acad Sci USA 1994;91:11631-11635.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11631-11635
    • Woolf, T.B.1    Roux, B.2
  • 41
    • 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 TB, Roux B. Structure, energetics, and dynamics of lipid-protein interactions: a molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins 1996;24:92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 42
    • 0030731888 scopus 로고    scopus 로고
    • Molecular dynamics of individual alpha-helices of bacteriorhodopsin in dimyristol phosphatidylocholine. I. Structure and dynamics
    • Woolf TB. Molecular dynamics of individual alpha-helices of bacteriorhodopsin in dimyristol phosphatidylocholine. I. Structure and dynamics. Biophys J 1997;73:2376-2392.
    • (1997) Biophys J , vol.73 , pp. 2376-2392
    • Woolf, T.B.1
  • 43
    • 0031961813 scopus 로고    scopus 로고
    • Molecular dynamics simulations of individual alpha-helices of bacteriorhodopsin in dimyristoylphosphatidylcholine. II. Interaction energy analysis
    • Woolf TB. Molecular dynamics simulations of individual alpha-helices of bacteriorhodopsin in dimyristoylphosphatidylcholine. II. Interaction energy analysis Biophys J 1998;74:115-131.
    • (1998) Biophys J , vol.74 , pp. 115-131
    • Woolf, T.B.1
  • 44
    • 0141927102 scopus 로고    scopus 로고
    • Molecular dynamics simulation of dark-adapted rhodopsin in an explicit membrane bilayer: Coupling between local retinal and larger scale conformational change
    • Crozier PS, Stevens MJ, Forrest LR, Woolf TB. Molecular dynamics simulation of dark-adapted rhodopsin in an explicit membrane bilayer: coupling between local retinal and larger scale conformational change. J Mol Biol 2003;333:493-514.
    • (2003) J Mol Biol , vol.333 , pp. 493-514
    • Crozier, P.S.1    Stevens, M.J.2    Forrest, L.R.3    Woolf, T.B.4
  • 45
    • 3042730827 scopus 로고    scopus 로고
    • How environment supports a state: Molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation
    • Jang H, Crozier PS, Stevens MJ, Woolf TB. How environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation. Biophys J 2004;87:129-145.
    • (2004) Biophys J , vol.87 , pp. 129-145
    • Jang, H.1    Crozier, P.S.2    Stevens, M.J.3    Woolf, T.B.4
  • 46
    • 33749535555 scopus 로고    scopus 로고
    • Interaction of protegrin-1 with lipid bilayers: Membrane thinning effect
    • Jang H, Ma B, Woolf TB, Nussinov R. Interaction of protegrin-1 with lipid bilayers: membrane thinning effect. Biophys J 2006;91:2848-2859.
    • (2006) Biophys J , vol.91 , pp. 2848-2859
    • Jang, H.1    Ma, B.2    Woolf, T.B.3    Nussinov, R.4
  • 47
    • 34247625467 scopus 로고    scopus 로고
    • Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect
    • Jang H, Ma B, Nussinov R. Conformational study of the protegrin-1 (PG-1) dimer interaction with lipid bilayers and its effect. BMC Struct Biol 2007;7:21.
    • (2007) BMC Struct Biol , vol.7 , pp. 21
    • Jang, H.1    Ma, B.2    Nussinov, R.3
  • 48
    • 34548788549 scopus 로고    scopus 로고
    • Models of (beta)-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • Jang H, Zheng J, Nussinov R. Models of (beta)-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process. Biophys J 2007;93:1938-1949.
    • (2007) Biophys J , vol.93 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 49
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC. Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 1999;28:319-365.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 50
    • 17044450798 scopus 로고    scopus 로고
    • Molecular dynamics simulations of charged and neutral lipid bilayers: Treatment of electrostatic interactions
    • Rog T, Murzyn K, Pasenkiewicz-Gierula M. Molecular dynamics simulations of charged and neutral lipid bilayers: treatment of electrostatic interactions. Acta Biochim Pol 2003;50:789-798.
    • (2003) Acta Biochim Pol , vol.50 , pp. 789-798
    • Rog, T.1    Murzyn, K.2    Pasenkiewicz-Gierula, M.3
  • 51
    • 0033135037 scopus 로고    scopus 로고
    • Impact of Cl- and Na+ ions on simulated structure and dynamics of betaARK1 PH domain
    • Pfeiffer S, Fushman D, Cowburn D. Impact of Cl- and Na+ ions on simulated structure and dynamics of betaARK1 PH domain. Proteins 1999;35:206-217.
    • (1999) Proteins , vol.35 , pp. 206-217
    • Pfeiffer, S.1    Fushman, D.2    Cowburn, D.3
  • 52
    • 0031834850 scopus 로고    scopus 로고
    • Importance of explicit salt ions for protein stability in molecular dynamics simulation
    • Ibragimova GT, Wade RC. Importance of explicit salt ions for protein stability in molecular dynamics simulation. Biophys J 1998;74:2906-2911.
    • (1998) Biophys J , vol.74 , pp. 2906-2911
    • Ibragimova, G.T.1    Wade, R.C.2
  • 53
    • 0029737564 scopus 로고    scopus 로고
    • What is the surface tension of a lipid bilayer membrane?
    • Jahnig F. What is the surface tension of a lipid bilayer membrane?. Biophys J 1996;71:1348-1349.
    • (1996) Biophys J , vol.71 , pp. 1348-1349
    • Jahnig, F.1
  • 54
    • 0029767694 scopus 로고    scopus 로고
    • On simulating lipid bilayers with an applied surface tension: Periodic boundary conditions and undulations
    • Feller SE, Pastor RW. On simulating lipid bilayers with an applied surface tension: periodic boundary conditions and undulations. Biophys J 1996;71:1350-1355.
    • (1996) Biophys J , vol.71 , pp. 1350-1355
    • Feller, S.E.1    Pastor, R.W.2
  • 55
    • 2942750047 scopus 로고    scopus 로고
    • Simulations of a membrane-anchored peptide: Structure, dynamics, and influence on bilayer properties
    • Jensen MO, Mouritsen OG, Peters GH. Simulations of a membrane-anchored peptide: structure, dynamics, and influence on bilayer properties. Biophys J 2004;86:3556-3575.
    • (2004) Biophys J , vol.86 , pp. 3556-3575
    • Jensen, M.O.1    Mouritsen, O.G.2    Peters, G.H.3
  • 56
    • 21244462687 scopus 로고    scopus 로고
    • Experimental validation of molecular dynamics simulations of lipid bilayers: A new approach
    • Benz RW, Castro-Roman F, Tobias DJ, White SH. Experimental validation of molecular dynamics simulations of lipid bilayers: a new approach. Biophys J 2005;88:805-817.
    • (2005) Biophys J , vol.88 , pp. 805-817
    • Benz, R.W.1    Castro-Roman, F.2    Tobias, D.J.3    White, S.H.4
  • 57
    • 0032614136 scopus 로고    scopus 로고
    • Constant surface tension simulations of lipid bilayers: The sensitivity of surface areas and compressibilities
    • Feller SE, Pastor RW. Constant surface tension simulations of lipid bilayers: the sensitivity of surface areas and compressibilities. J Chem Phys 1999;111:1281-1287.
    • (1999) J Chem Phys , vol.111 , pp. 1281-1287
    • Feller, S.E.1    Pastor, R.W.2
  • 58
    • 28444481767 scopus 로고    scopus 로고
    • A molecular dynamics study of the response of lipid bilayers and monolayers to trehalose
    • Skibinsky A, Venable RM, Pastor RW. A molecular dynamics study of the response of lipid bilayers and monolayers to trehalose. Biophys J 2005;89:4111-4121.
    • (2005) Biophys J , vol.89 , pp. 4111-4121
    • Skibinsky, A.1    Venable, R.M.2    Pastor, R.W.3
  • 59
    • 0344236133 scopus 로고    scopus 로고
    • Lipid/protein interactions and the membrane/water interfacial region
    • Domence C, Bond PJ, Deol SS, Sansom MSP. Lipid/protein interactions and the membrane/water interfacial region. J Am Chem Soc 2003;125:14966-14967.
    • (2003) J Am Chem Soc , vol.125 , pp. 14966-14967
    • Domence, C.1    Bond, P.J.2    Deol, S.S.3    Sansom, M.S.P.4
  • 60
    • 10044244661 scopus 로고    scopus 로고
    • Lipid-protein interactions of integral membrane proteins: A comparative simulation study
    • Deol SS, Bond PJ, Domene C, Sansom MS. Lipid-protein interactions of integral membrane proteins: a comparative simulation study. Biophys J 2004;87:3737-3749.
    • (2004) Biophys J , vol.87 , pp. 3737-3749
    • Deol, S.S.1    Bond, P.J.2    Domene, C.3    Sansom, M.S.4
  • 61
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus M, McCammon JA. Molecular dynamics simulations of biomolecules. Nat Struct Biol 2002;9:646-652.
    • (2002) Nat Struct Biol , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.