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Volumn 88, Issue 5, 2005, Pages 3321-3333

Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: Structure and collective motions

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; MUSCARINIC M1 RECEPTOR; MUSCARINIC M2 RECEPTOR; MUSCARINIC M3 RECEPTOR; MUSCARINIC M4 RECEPTOR; NICOTINIC RECEPTOR; RECEPTOR SUBTYPE;

EID: 17844364634     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.052878     Document Type: Article
Times cited : (42)

References (75)
  • 1
    • 0031708266 scopus 로고    scopus 로고
    • Electrostatics and the ion selectivity of ligand-gated ion channels
    • Adcock, C., G. R. Smith, and M. S. P. Sansom. 1998. Electrostatics and the ion selectivity of ligand-gated ion channels. Biophys. J. 75:1211-1222.
    • (1998) Biophys. J. , vol.75 , pp. 1211-1222
    • Adcock, C.1    Smith, G.R.2    Sansom, M.S.P.3
  • 2
    • 0033796251 scopus 로고    scopus 로고
    • The nicotinic acetylcholine receptor: From molecular model to single channel conductance
    • Adcock, C., G. R. Smith, and M. S. P. Sansom. 2000. The nicotinic acetylcholine receptor: from molecular model to single channel conductance. Eur. Biophys. J. 29:29-37.
    • (2000) Eur. Biophys. J. , vol.29 , pp. 29-37
    • Adcock, C.1    Smith, G.R.2    Sansom, M.S.P.3
  • 4
    • 17844406709 scopus 로고    scopus 로고
    • The a7 nicotinic acetylcholine receptor: Molecular modelling, electrostatics, and energetics
    • In press
    • Amiri, S., K. Tai, O. Beckstein, P. C. Biggin, and M. S. P. Sansom. 2005. The a7 nicotinic acetylcholine receptor: molecular modelling, electrostatics, and energetics. Mol. Membr. Biol. In press.
    • (2005) Mol. Membr. Biol.
    • Amiri, S.1    Tai, K.2    Beckstein, O.3    Biggin, P.C.4    Sansom, M.S.P.5
  • 5
    • 2142715470 scopus 로고    scopus 로고
    • Water dynamics and dewetting transitions in the small mechanosensitive channel MscS
    • Anishkin, A., and S. Sukharev. 2004. Water dynamics and dewetting transitions in the small mechanosensitive channel MscS. Biophys. J. 86:2883-2895.
    • (2004) Biophys. J. , vol.86 , pp. 2883-2895
    • Anishkin, A.1    Sukharev, S.2
  • 7
    • 0030623823 scopus 로고    scopus 로고
    • Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential
    • Bahar, I., A. R. Atilgan, and B. Erman. 1997. Direct evaluation of thermal fluctuations in proteins using a single-parameter harmonic potential. Fold. Des. 2:173-181.
    • (1997) Fold. Des. , vol.2 , pp. 173-181
    • Bahar, I.1    Atilgan, A.R.2    Erman, B.3
  • 8
  • 9
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J., and J. M. Thornton. 1988. Helix geometry in proteins. J. Mol. Biol. 201:601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 10
    • 16644370327 scopus 로고    scopus 로고
    • Dynamite: A simple way to gain insight into protein motions
    • Barrett, C. P., B. A. Hall, and M. E. M. Noble. 2004. Dynamite: a simple way to gain insight into protein motions. Acta Cryst. D. 60:2280-2287.
    • (2004) Acta Cryst. D , vol.60 , pp. 2280-2287
    • Barrett, C.P.1    Hall, B.A.2    Noble, M.E.M.3
  • 12
    • 0035961071 scopus 로고    scopus 로고
    • A hydrophobic gating mechanism for nanopores
    • Beckstein, O., P. C. Biggin, and M. S. P. Sansom. 2001. A hydrophobic gating mechanism for nanopores. J. Phys. Chem. B. 105:12902-12905.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12902-12905
    • Beckstein, O.1    Biggin, P.C.2    Sansom, M.S.P.3
  • 13
    • 0038472282 scopus 로고    scopus 로고
    • Liquid-vapor oscillations of water in hydrophobic nanopores
    • Beckstein, O., and M. S. P. Sansom. 2003. Liquid-vapor oscillations of water in hydrophobic nanopores. Proc. Natl. Acad. Sci. USA. 100: 7063-7068.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7063-7068
    • Beckstein, O.1    Sansom, M.S.P.2
  • 14
    • 33748573642 scopus 로고    scopus 로고
    • The influence of geometry, surface character and flexibility on the permeation of ions and water through biological pores
    • Beckstein, O., and M. S. P. Sansom. 2004. The influence of geometry, surface character and flexibility on the permeation of ions and water through biological pores. Phys. Biol. 1:42-52.
    • (2004) Phys. Biol. , vol.1 , pp. 42-52
    • Beckstein, O.1    Sansom, M.S.P.2
  • 15
    • 8844228899 scopus 로고    scopus 로고
    • Not ions alone: Barriers to ion permeation in nanopores and channels
    • Beckstein, O., K. Tai, and M. S. P. Sansom. 2004. Not ions alone: barriers to ion permeation in nanopores and channels. J. Am. Chem. Soc. 126: 14694-14695.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 14694-14695
    • Beckstein, O.1    Tai, K.2    Sansom, M.S.P.3
  • 19
    • 0036343993 scopus 로고    scopus 로고
    • Conformational dynamics of helix S6 from Shaker potassium channel: Simulation studies
    • Bright, J. N., I. H. Shrivastava, F. S. Cordes, and M. S. P. Sansom. 2002. Conformational dynamics of helix S6 from Shaker potassium channel: simulation studies. Biopolymers. 64:303-313.
    • (2002) Biopolymers , vol.64 , pp. 303-313
    • Bright, J.N.1    Shrivastava, I.H.2    Cordes, F.S.3    Sansom, M.S.P.4
  • 20
    • 11844258265 scopus 로고    scopus 로고
    • A speed limit for conformational change of an allosteric membrane protein
    • Chakrapani, S., and A. Auerbach. 2005. A speed limit for conformational change of an allosteric membrane protein. Proc. Natl. Acad. Sci. USA. 102:87-92.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 87-92
    • Chakrapani, S.1    Auerbach, A.2
  • 21
    • 0027057058 scopus 로고
    • The functional architecture of the acetylcholine nicotinic receptor explored by affinity labelling and site-directed mutagenesis
    • Changeux, J. P., J. I. Galzi, A. Devillers-Thiéry, and D. Bertrand. 1992. The functional architecture of the acetylcholine nicotinic receptor explored by affinity labelling and site-directed mutagenesis. Q. Rev. Biophys. 25:395-432.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 395-432
    • Changeux, J.P.1    Galzi, J.I.2    Devillers-Thiéry, A.3    Bertrand, D.4
  • 22
    • 0036430199 scopus 로고    scopus 로고
    • Proline-induced distortions of transmembrane helices
    • Cordes, F. S., J. N. Bright, and M. S. P. Sansom. 2002. Proline-induced distortions of transmembrane helices. J. Mol. Biol. 323:951-960.
    • (2002) J. Mol. Biol. , vol.323 , pp. 951-960
    • Cordes, F.S.1    Bright, J.N.2    Sansom, M.S.P.3
  • 25
    • 2442548865 scopus 로고    scopus 로고
    • Theoretical conformation of the closed and open states of the acetylcholine receptor channel
    • Cony, B. 2004. Theoretical conformation of the closed and open states of the acetylcholine receptor channel. Biochim. Biophys. Acta. 1663:2-5.
    • (2004) Biochim. Biophys. Acta , vol.1663 , pp. 2-5
    • Cony, B.1
  • 26
    • 0037197654 scopus 로고    scopus 로고
    • Structure of the transition state of gating in the acetylcholine receptor channel pore: A F-value analysis
    • Cymes, G. D., C. Grosman, and A. Auerbach. 2002. Structure of the transition state of gating in the acetylcholine receptor channel pore: a F-value analysis. Biochemistry. 41:5548-5555.
    • (2002) Biochemistry , vol.41 , pp. 5548-5555
    • Cymes, G.D.1    Grosman, C.2    Auerbach, A.3
  • 27
    • 33846823909 scopus 로고
    • Particle mesh Ewald - An N.log(N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald-an N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98: 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 28
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J., J. E. Nielsen, J. A. McCammon, and N. A. Baker. 2004. PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic. Acids Res. 32: W665-W667.
    • (2004) Nucleic. Acids Res. , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 29
    • 0032561237 scopus 로고    scopus 로고
    • Pathway to a folding intermediate observed in a microsecond simulation in aqueous solution
    • Duan, Y., and P. A. Kollman. 1998. Pathway to a folding intermediate observed in a microsecond simulation in aqueous solution. Science. 282:740-744.
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 32
    • 0037671392 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the bacterial outer membrane protein FhuA: A comparative study of the ferrichrome-free and bound states
    • Faraldo-Gómez, J. D., G. R. Smith, and M. S. P. Sansom. 2003. Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states. Biophys. J. 85:1-15.
    • (2003) Biophys. J. , vol.85 , pp. 1-15
    • Faraldo-Gómez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 33
    • 0028031541 scopus 로고
    • Neurotransmitter-gated ion channels as unconventional allosteric proteins
    • Galzi, J. L., and J. P. Changeux. 1994. Neurotransmitter-gated ion channels as unconventional allosteric proteins. Curr. Opin. Struct. Biol. 4:554-565.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 554-565
    • Galzi, J.L.1    Changeux, J.P.2
  • 34
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • Grosman, C., M. Zhou, and A. Auerbach. 2000. Mapping the conformational wave of acetylcholine receptor channel gating. Nature. 403:773-776.
    • (2000) Nature , vol.403 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 35
    • 17844380512 scopus 로고    scopus 로고
    • Conformational dynamics of the ligand-binding domain of inward rectifier K channels as revealed by MD simulations
    • In press
    • Haider, S., A. Grottesi, F. M. Ashcroft, and M. S. P. Sansom. 2005. Conformational dynamics of the ligand-binding domain of inward rectifier K channels as revealed by MD simulations. Biophys. J. In press.
    • (2005) Biophys. J.
    • Haider, S.1    Grottesi, A.2    Ashcroft, F.M.3    Sansom, M.S.P.4
  • 36
    • 0242385357 scopus 로고    scopus 로고
    • Asymmetric structural motions of the homomeric a7 nicotinic receptor ligand binding domain revealed by molecular dynamics simulation
    • Henchman, R. H., H. L. Wang, S. M. Sine, P. Taylor, and J. A. McCammon. 2003. Asymmetric structural motions of the homomeric a7 nicotinic receptor ligand binding domain revealed by molecular dynamics simulation. Biophys. J. 85:3007-3018.
    • (2003) Biophys. J. , vol.85 , pp. 3007-3018
    • Henchman, R.H.1    Wang, H.L.2    Sine, S.M.3    Taylor, P.4    McCammon, J.A.5
  • 37
    • 0034500645 scopus 로고    scopus 로고
    • Similarities between principal components of protein dynamics and random diffusion
    • Hess, B. 2000. Similarities between principal components of protein dynamics and random diffusion. Phys. Rev. F. 62:8438-8448.
    • (2000) Phys. Rev. F. , vol.62 , pp. 8438-8448
    • Hess, B.1
  • 41
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern-recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern-recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 42
    • 0036480194 scopus 로고    scopus 로고
    • Emerging structure of the nicotinic acetylcholine receptors
    • Karlin, A. 2002. Emerging structure of the nicotinic acetylcholine receptors. Nat. Rev. Neurosci. 3:102-114.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 102-114
    • Karlin, A.1
  • 43
    • 0029593370 scopus 로고
    • Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins
    • Karlin, A., and M. H. Akabas. 1995. Toward a structural basis for the function of nicotinic acetylcholine receptors and their cousins. Neuron. 15:1231-1244.
    • (1995) Neuron , vol.15 , pp. 1231-1244
    • Karlin, A.1    Akabas, M.H.2
  • 44
    • 4143126482 scopus 로고    scopus 로고
    • A model of the closed form of the nicotinic acetylcholine receptor M2 channel pore
    • Kim, S., A. K. Chamberlain, and J. U. Bowie. 2004. A model of the closed form of the nicotinic acetylcholine receptor M2 channel pore. Biophys. J. 87:792-799.
    • (2004) Biophys. J. , vol.87 , pp. 792-799
    • Kim, S.1    Chamberlain, A.K.2    Bowie, J.U.3
  • 45
    • 0033996292 scopus 로고    scopus 로고
    • Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers and transbilayer bundles
    • Law, R. J., L. R. Forrest, K. M. Ranatunga, P. La Rocca, D. P. Tieleman, and M. S. P. Sansom. 2000. Structure and dynamics of the pore-lining helix of the nicotinic receptor: MD simulations in water, lipid bilayers and transbilayer bundles. Proteins. 39:47-55.
    • (2000) Proteins , vol.39 , pp. 47-55
    • Law, R.J.1    Forrest, L.R.2    Ranatunga, K.M.3    La Rocca, P.4    Tieleman, D.P.5    Sansom, M.S.P.6
  • 46
    • 12244294449 scopus 로고    scopus 로고
    • Pores formed by the nicotinic receptor M2d peptide: A molecular dynamics simulation study
    • Law, R. J., D. P. Tieleman, and M. S. P. Sansom. 2003. Pores formed by the nicotinic receptor M2d peptide: a molecular dynamics simulation study. Biophys. J. 84:14-27.
    • (2003) Biophys. J. , vol.84 , pp. 14-27
    • Law, R.J.1    Tieleman, D.P.2    Sansom, M.S.P.3
  • 47
    • 0026684455 scopus 로고
    • The permeation pathway of neurotransmitter-gated ion channels
    • Lester, H. 1992. The permeation pathway of neurotransmitter-gated ion channels. Annu. Rev. Biophys. Biomol. Struct. 21:267-292.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 267-292
    • Lester, H.1
  • 49
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317.
    • (2001) J. Mol. Model. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 50
    • 3042607959 scopus 로고    scopus 로고
    • The transmembrane domain of the 5-HT3 receptor: Its role in selectivity and gating
    • Lummis, S. C. R. 2004. The transmembrane domain of the 5-HT3 receptor: its role in selectivity and gating. Biochem. Soc. Trans. 32:535-539.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 535-539
    • Lummis, S.C.R.1
  • 51
    • 4644289077 scopus 로고    scopus 로고
    • Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating
    • Mitra, A., T. D. Bailey, and A. Auerbach. 2004. Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating. Structure. 12:1909-1918.
    • (2004) Structure , vol.12 , pp. 1909-1918
    • Mitra, A.1    Bailey, T.D.2    Auerbach, A.3
  • 52
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A., Y. Fujiyoshi, and N. Unwin. 2003. Structure and gating mechanism of the acetylcholine receptor pore. Nature. 423:949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 53
    • 0029150299 scopus 로고
    • Design of molecular function: Channels of communication
    • Montal, M. 1995. Design of molecular function: channels of communication. Annu. Rev. Biophys. Biomol. Struct. 24:31-57.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 31-57
    • Montal, M.1
  • 54
    • 0027403316 scopus 로고
    • Design, synthesis and functional characterisation of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor
    • Montai, M. O., T. Iwamoto, J. M. Tomich, and M. Montal. 1993. Design, synthesis and functional characterisation of a pentameric channel protein that mimics the presumed pore structure of the nicotinic cholinergic receptor. FEBS Lett. 320:261-266.
    • (1993) FEBS Lett. , vol.320 , pp. 261-266
    • Montai, M.O.1    Iwamoto, T.2    Tomich, J.M.3    Montal, M.4
  • 55
    • 0010528163 scopus 로고
    • M2d, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor
    • Oiki, S., W. Danho, V. Madison, and M. Montal. 1988. M2d, a candidate for the structure lining the ionic channel of the nicotinic cholinergic receptor. Proc. Natl. Acad. Sci. USA. 85:8703-8707.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8703-8707
    • Oiki, S.1    Danho, W.2    Madison, V.3    Montal, M.4
  • 56
    • 0032919444 scopus 로고    scopus 로고
    • Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
    • Opella, S. J., F. M. Marassi, J. J. Gesell, A. P. Valente, Y. Kim, M. Oblatt-Montal, and M. Montal. 1999. Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy. Nat. Struct. Biol. 6:374-379.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 374-379
    • Opella, S.J.1    Marassi, F.M.2    Gesell, J.J.3    Valente, A.P.4    Kim, Y.5    Oblatt-Montal, M.6    Montal, M.7
  • 57
    • 0036522962 scopus 로고    scopus 로고
    • Evidence for a centrally located gate in the pore of a serotonin-gated ion channel
    • Panicker, S., H. Cruz, C. Arrabit, and P. A. Slesinger. 2002. Evidence for a centrally located gate in the pore of a serotonin-gated ion channel. J. Neurosci. 22:1629-1639.
    • (2002) J. Neurosci. , vol.22 , pp. 1629-1639
    • Panicker, S.1    Cruz, H.2    Arrabit, C.3    Slesinger, P.A.4
  • 58
    • 33749223814 scopus 로고
    • Reevaluation of the Born model of ion hydration
    • Rashin, A., and B. Honig. 1985. Reevaluation of the Born model of ion hydration. J. Phys. Chem. 89:5588-5593.
    • (1985) J. Phys. Chem. , vol.89 , pp. 5588-5593
    • Rashin, A.1    Honig, B.2
  • 59
    • 1542365497 scopus 로고    scopus 로고
    • Effect of the pore region of a transmembrane ion channel on the physical properties of a simple membrane
    • Saiz, L., S. Bandyopadhyay, and M. L. Klein. 2004. Effect of the pore region of a transmembrane ion channel on the physical properties of a simple membrane. J. Phys. Chem. B. 108:2608-2613.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 2608-2613
    • Saiz, L.1    Bandyopadhyay, S.2    Klein, M.L.3
  • 60
    • 0036286655 scopus 로고    scopus 로고
    • Computer simulation studies of model biological membranes
    • Saiz, L., and M. L. Klein. 2002. Computer simulation studies of model biological membranes. Acc. Chem. Res. 35:482-489.
    • (2002) Acc. Chem. Res. , vol.35 , pp. 482-489
    • Saiz, L.1    Klein, M.L.2
  • 61
    • 0029813087 scopus 로고    scopus 로고
    • The pore domain of the nicotinic acetylcholine receptor: Molecular modelling and electrostatics
    • Sankararamakrishnan, R., C. Adcock, and M. S. P. Sansom. 1996. The pore domain of the nicotinic acetylcholine receptor:- molecular modelling and electrostatics. Biophys. J. 71:1659-1671.
    • (1996) Biophys. J. , vol.71 , pp. 1659-1671
    • Sankararamakrishnan, R.1    Adcock, C.2    Sansom, M.S.P.3
  • 62
    • 0028824169 scopus 로고
    • Modelling packing interactions in parallel helix bundles: Pentameric bundles of nicotinic receptor M2 helices
    • Sankararamakrishnan, R., and M. S. P. Sansom. 1995. Modelling packing interactions in parallel helix bundles:- pentameric bundles of nicotinic receptor M2 helices. Biochim. Biophys. Acta. 1239:122-132.
    • (1995) Biochim. Biophys. Acta , vol.1239 , pp. 122-132
    • Sankararamakrishnan, R.1    Sansom, M.S.P.2
  • 63
    • 0037133320 scopus 로고    scopus 로고
    • Intrinsic flexibility and gating mechanism of the potassium channel KcsA
    • Shen, Y. F., Y. F. Kong, and J. P. Ma. 2002. Intrinsic flexibility and gating mechanism of the potassium channel KcsA. Proc. Natl. Acad. Sci. USA. 99:1949-1953.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1949-1953
    • Shen, Y.F.1    Kong, Y.F.2    Ma, J.P.3
  • 64
    • 0037174385 scopus 로고    scopus 로고
    • All-atom structure prediction and folding simulations of a stable protein
    • Simmerling, C., B. Strockbine, and A. E. Roitberg. 2002. All-atom structure prediction and folding simulations of a stable protein. J. Am. Chem. Soc. 124:11258-11259.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11258-11259
    • Simmerling, C.1    Strockbine, B.2    Roitberg, A.E.3
  • 65
    • 0030404988 scopus 로고    scopus 로고
    • Hole: A program for the analysis of the pore dimensions of ion channel structural models
    • Smart, O. S., J. G. Neduvelil, X. Wang, B. A. Wallace, and M. S. P. Sansom. 1996. Hole: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14:354-360.
    • (1996) J. Mol. Graph. , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.P.5
  • 66
    • 1642419567 scopus 로고    scopus 로고
    • Mechanistic contributions of residues in the M1 transmembrane domain of the nicotinic receptor to channel gating
    • Spitzmaul, G., J. Corradi, and C. Bouzat. 2004. Mechanistic contributions of residues in the M1 transmembrane domain of the nicotinic receptor to channel gating. Mol. Membr. Biol. 21:39-50.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 39-50
    • Spitzmaul, G.1    Corradi, J.2    Bouzat, C.3
  • 67
    • 0034906622 scopus 로고    scopus 로고
    • Analysis of a 10-ns molecular dynamics simulation of mouse acetylcholinesterase
    • Tai, K., T. Shen, U. Börjesson, M. Philippopoulos, and J. A. McCammon. 2001. Analysis of a 10-ns molecular dynamics simulation of mouse acetylcholinesterase. Biophys. J. 81:715-724.
    • (2001) Biophys. J. , vol.81 , pp. 715-724
    • Tai, K.1    Shen, T.2    Börjesson, U.3    Philippopoulos, M.4    McCammon, J.A.5
  • 68
    • 0037140753 scopus 로고    scopus 로고
    • Mechanism of acetylcholinesterase inhibition by fasciculin: A 5-ns molecular dynamics simulation
    • Tai, K., T. Shen, R. H. Henchman, Y. Bourne, P. Marchot, and J. A. McCammon. 2002. Mechanism of acetylcholinesterase inhibition by fasciculin: a 5-ns molecular dynamics simulation. J. Am. Chem. Soc. 124:6153-6161.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6153-6161
    • Tai, K.1    Shen, T.2    Henchman, R.H.3    Bourne, Y.4    Marchot, P.5    McCammon, J.A.6
  • 69
    • 0031972865 scopus 로고    scopus 로고
    • Kinked-helices model of the nicotinic acetylcholine receptor ion channel and its complexes with blockers: Simulation by the Monte Carlo minimization method
    • Tikhonov, D. B., and B. S. Zhorov. 1998. Kinked-helices model of the nicotinic acetylcholine receptor ion channel and its complexes with blockers: simulation by the Monte Carlo minimization method. Biophys. J. 74:242-255.
    • (1998) Biophys. J. , vol.74 , pp. 242-255
    • Tikhonov, D.B.1    Zhorov, B.S.2
  • 70
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9Å resolution
    • Unwin, N. 1993. Nicotinic acetylcholine receptor at 9Å resolution. J. Mol. Biol. 229:1101-1124.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 71
    • 0028921479 scopus 로고
    • Acetylcholine receptor channel imaged in the open state
    • Unwin, N. 1995. Acetylcholine receptor channel imaged in the open state. Nature. 373:37-43.
    • (1995) Nature , vol.373 , pp. 37-43
    • Unwin, N.1
  • 72
    • 0043238084 scopus 로고    scopus 로고
    • Dynamical properties of the MscL of Escherichia coli: A normal mode analysis
    • Valadie, H., J. J. Lacapcre, Y. H. Sanejouand, and C. Etchebest. 2003. Dynamical properties of the MscL of Escherichia coli: A normal mode analysis. J. Mol. Biol. 332:657-674.
    • (2003) J. Mol. Biol. , vol.332 , pp. 657-674
    • Valadie, H.1    Lacapcre, J.J.2    Sanejouand, Y.H.3    Etchebest, C.4
  • 75
    • 13644270375 scopus 로고    scopus 로고
    • Conformational dynamics of the nicotinic acetylcholine receptor channel: A 35-ns molecular dynamics simulation study
    • In press
    • Xu, Y., F. J. Barrantes, X. Luo, K. Chen, J. Shen, and H. Jiang. 2005. Conformational dynamics of the nicotinic acetylcholine receptor channel: a 35-ns molecular dynamics simulation study. J. Am. Chem. Soc. In press.
    • (2005) J. Am. Chem. Soc.
    • Xu, Y.1    Barrantes, F.J.2    Luo, X.3    Chen, K.4    Shen, J.5    Jiang, H.6


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