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Volumn 4, Issue , 2013, Pages

The pore of voltage-gated potassium ion channels is strained when closed

Author keywords

[No Author keywords available]

Indexed keywords

VOLTAGE GATED POTASSIUM CHANNEL;

EID: 84878680599     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms2858     Document Type: Article
Times cited : (48)

References (60)
  • 1
    • 0003443746 scopus 로고    scopus 로고
    • Sinauer Associates, Inc, Sunderland, Massachusetts, USA, 3rd edition
    • Hille, B. Ion Channels of Excitable Membranes (Sinauer Associates, Inc, Sunderland, Massachusetts, USA, 3rd edition, 2001)
    • (2001) Ion Channels of Excitable Membranes
    • Hille, B.1
  • 2
    • 0035499892 scopus 로고    scopus 로고
    • + channel-Fab complex at 2.0 A resolution
    • DOI 10.1038/35102009
    • Zhou, Y., Morais-Cabral, J. H., Kaufman, A. & MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K channel-Fab complex at 2.0 A resolution. Nature 414, 43-48 (2001) (Pubitemid 33041616)
    • (2001) Nature , vol.414 , Issue.6859 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    Mackinnon, R.4
  • 3
    • 23244456428 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1126/science.1116269
    • Long, S. B., Campbell, E. B. & MacKinnon, R. Crystal structure of a mammalian voltage-dependent Shaker family K channel. Science 309, 897-903 (2005) (Pubitemid 41099919)
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 4
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • DOI 10.1038/nature06265, PII NATURE06265
    • Long, S. B., Tao, X., Campbell, E. B. & MacKinnon, R. Atomic structure of a voltage-dependent K channel in a lipid membrane-like environment. Nature 450, 376-382 (2007) (Pubitemid 350126743)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 5
    • 66149157329 scopus 로고    scopus 로고
    • Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K channels
    • Lee, S. -Y., Banerjee, A. & MacKinnon, R. Two separate interfaces between the voltage sensor and pore are required for the function of voltage-dependent K channels. PLoS Biol. 7, e47 (2009)
    • (2009) PLoS Biol , vol.7
    • Lee, S.-Y.1    Banerjee, A.2    MacKinnon, R.3
  • 6
    • 0025801502 scopus 로고
    • Conserved positioning of proline residues in membrane-spanning helices of ion-channel proteins
    • Woolfson, D. N., Mortishire-Smith, R. J. & Williams, D. H. Conserved positioning of proline residues in membrane-spanning helices of ion-channel proteins. Biochem. Biophys. Res. Comm. 175, 733-737 (1991)
    • (1991) Biochem. Biophys. Res. Comm , vol.175 , pp. 733-737
    • Woolfson, D.N.1    Mortishire-Smith, R.J.2    Williams, D.H.3
  • 7
    • 0029838750 scopus 로고    scopus 로고
    • Molecular dynamics simulations of isolated transmembrane helices of potassium channels
    • Kerr, I. D., Son, H. S., Sankararamakrishnan, R. & Sansom, M. S. P. Molecular dynamics simulations of isolated transmembrane helices of potassium channels. Biopolymers 39, 503-515 (1996)
    • (1996) Biopolymers , vol.39 , pp. 503-515
    • Kerr, I.D.1    Son, H.S.2    Sankararamakrishnan, R.3    Sansom, M.S.P.4
  • 8
    • 0034030664 scopus 로고    scopus 로고
    • Structure and dynamics of K channel pore-lining helices: A comparative simulation study
    • Shrivastava, I. H., Capener, C. E., Forrest, L. R. & Sansom, M. S. P. Structure and dynamics of K channel pore-lining helices: a comparative simulation study. Biophys. J. 78, 79-92 (2000) (Pubitemid 30207120)
    • (2000) Biophysical Journal , vol.78 , Issue.1 , pp. 79-92
    • Shrivastava, I.H.1    Capener, C.E.2    Forrest, L.R.3    Sansom, M.S.P.4
  • 9
    • 0035427377 scopus 로고    scopus 로고
    • Proline-induced hinges in transmembrane helices: Possible roles in ion channel gating
    • Tieleman, D. P., Shrivastava, I. H., Ulmschneider, M. R. & Sansom, M. S. P. Proline-induced hinges in transmembrane helices: possible roles in ion channel gating. Proteins 44, 63-72 (2001)
    • (2001) Proteins , vol.44 , pp. 63-72
    • Tieleman, D.P.1    Shrivastava, I.H.2    Ulmschneider, M.R.3    Sansom, M.S.P.4
  • 10
    • 0037448550 scopus 로고    scopus 로고
    • The flexing/twirling helix: Exploring the flexibility about molecular hinges formed by proline and glycine motifs in transmembrane helices
    • Bright, J. N. & Sansom, M. S. P. The flexing/twirling helix: exploring the flexibility about molecular hinges formed by proline and glycine motifs in transmembrane helices. J. Phys. Chem. B 107, 627-636 (2003)
    • (2003) J. Phys. Chem. B , vol.107 , pp. 627-636
    • Bright, J.N.1    Sansom, M.S.P.2
  • 11
    • 67249136876 scopus 로고    scopus 로고
    • Conformational dynamics of the inner pore helix of voltage-gated potassium channels
    • Choe, S. & Grabe, M. Conformational dynamics of the inner pore helix of voltage-gated potassium channels. J. Chem. Phys. 130, 215103 (2009)
    • (2009) J. Chem. Phys , vol.130 , pp. 215103
    • Choe, S.1    Grabe, M.2
  • 12
    • 77951236840 scopus 로고    scopus 로고
    • Cooperative nature of gating transitions in K channels as seen from dynamic importance sampling calculations
    • Denning, E. J. & Woolf, T. B. Cooperative nature of gating transitions in K channels as seen from dynamic importance sampling calculations. Proteins 78, 1105-1119 (2010)
    • (2010) Proteins , vol.78 , pp. 1105-1119
    • Denning, E.J.1    Woolf, T.B.2
  • 13
    • 0030795112 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80357-8
    • Liu, Y., Holmgren, M., Jurman, M. E. & Yellen, G. Gated access to the pore of a voltage-dependent K channel. Neuron 19, 175-184 (1997) (Pubitemid 27333003)
    • (1997) Neuron , vol.19 , Issue.1 , pp. 175-184
    • Liu, Y.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 14
    • 0034688285 scopus 로고    scopus 로고
    • + channel and its structural implications
    • DOI 10.1038/35002099
    • del Camino, D., Holmgren, M., Liu, Y. & Yellen, G. Blocker protection in the pore of a voltage-gated K channel and its structural implications. Nature 403, 321-325 (2000) (Pubitemid 30062389)
    • (2000) Nature , vol.403 , Issue.6767 , pp. 321-325
    • Del Camino, D.1    Holmgren, M.2    Liu, Y.3    Yellen, G.4
  • 15
    • 0346118860 scopus 로고    scopus 로고
    • Gating of shaker-type channels requires the flexibility of s6 caused by prolines
    • DOI 10.1074/jbc.M306097200
    • Labro, A. J., Raes, A. L., Bellens, I., Ottschytsch, N. & Snyders, D. J. Gating of Shaker-type channels requires the flexibility of S6 caused by prolines. J. Biol. Chem. 278, 50724-50731 (2003) (Pubitemid 37548921)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50724-50731
    • Labro, A.J.1    Raes, A.L.2    Bellens, I.3    Ottschytsch, N.4    Snyders, D.J.5
  • 16
    • 0036016539 scopus 로고    scopus 로고
    • Scanning the intracellular S6 activation gate in the Shaker K channel
    • Hackos, D. H., Chang, T.-H. & Swartz, K. J. Scanning the intracellular S6 activation gate in the Shaker K channel. J. Gen. Physiol. 119, 521-532 (2002)
    • (2002) J. Gen. Physiol , vol.119 , pp. 521-532
    • Hackos, D.H.1    Chang, T.-H.2    Swartz, K.J.3
  • 17
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • DOI 10.1126/science.1116270
    • Long, S. B., Campbell, E. B. & MacKinnon, R. Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908 (2005) (Pubitemid 41099920)
    • (2005) Science , vol.309 , Issue.5736 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 18
    • 77957924708 scopus 로고    scopus 로고
    • Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP
    • Butterwick, J. A. & MacKinnon, R. Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP. J. Mol. Biol. 403, 591-606 (2010)
    • (2010) J. Mol. Biol , vol.403 , pp. 591-606
    • Butterwick, J.A.1    MacKinnon, R.2
  • 19
    • 0036846783 scopus 로고    scopus 로고
    • + channels
    • DOI 10.1085/jgp.20028696
    • Lu, Z., Klem, A. M. & Ramu, Y. Coupling between voltage sensors and activation gate in voltage-gated K channels. J. Gen. Physiol. 120, 663-676 (2002) (Pubitemid 35332586)
    • (2002) Journal of General Physiology , vol.120 , Issue.5 , pp. 663-676
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 20
    • 59649096789 scopus 로고    scopus 로고
    • Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by non-interacting residues
    • Labro, A. J. et al. Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by non-interacting residues. J. Gen. Physiol. 132, 667-680 (2008)
    • (2008) J. Gen. Physiol , vol.132 , pp. 667-680
    • Labro, A.J.1
  • 21
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • DOI 10.1038/nature03650
    • Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K. & Okamura, Y. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435, 1239-1243 (2005) (Pubitemid 40943089)
    • (2005) Nature , vol.435 , Issue.7046 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 22
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I. S., Moran, M. M., Chong, J. A. & Clapham, D. E. A voltage-gated proton-selective channel lacking the pore domain. Nature 440, 1213-1216 (2006)
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 23
    • 0030175867 scopus 로고    scopus 로고
    • Voltage-sensing residues in the S2 and S4 segments of the K channel
    • Seoh, S., Sigg, D., Papazian, D. & Bezanilla, F. Voltage-sensing residues in the S2 and S4 segments of the K channel. Neuron 16, 1159-1167 (1996)
    • (1996) Neuron , vol.16 , pp. 1159-1167
    • Seoh, S.1    Sigg, D.2    Papazian, D.3    Bezanilla, F.4
  • 24
    • 0030175348 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80143-9
    • Aggarwal, S. K. & MacKinnon, R. Contribution of the S4 segment to gating charge in the Shaker K channel. Neuron 16, 1169-1177 (1996) (Pubitemid 26227238)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 25
    • 0028140472 scopus 로고
    • Shaker potassium channel gating III: Evaluation of kinetic models for activation
    • Zagotta, W. N., Hoshi, T. & Aldrich, R. W. Shaker potassium channel gating. III: evaluation of kinetic models for activation. J. Gen. Physiol. 103, 321-362 (1994) (Pubitemid 24068562)
    • (1994) Journal of General Physiology , vol.103 , Issue.2 , pp. 321-362
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 26
    • 23844459909 scopus 로고    scopus 로고
    • Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement
    • DOI 10.1038/nature03888
    • Chanda, B., Asamoah, O. K., Blunck, R., Roux, B. & Bezanilla, F. Gating charge displacement in voltage-gated ion channels involves limited transmembrane movement. Nature 436, 852-856 (2005) (Pubitemid 41160644)
    • (2005) Nature , vol.436 , Issue.7052 , pp. 852-856
    • Chanda, B.1    Asamoah, O.K.2    Blunck, R.3    Roux, B.4    Bezanilla, F.5
  • 29
    • 77950544751 scopus 로고    scopus 로고
    • Principles of conduction and hydrophobic gating in K channels
    • Jensen, M. O. et al. Principles of conduction and hydrophobic gating in K channels. Proc. Natl Acad. Sci. USA 107, 5833-5838 (2010)
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 5833-5838
    • Jensen, M.O.1
  • 30
    • 8844228899 scopus 로고    scopus 로고
    • Not ions alone: Barriers to ion permeation in nanopores and channels
    • DOI 10.1021/ja045271e
    • Beckstein, O., Tai, K. & Sansom, M. S. P. Not ions alone: barriers to ion permeation in nanopores and channels. J. Am. Chem. Soc. 126, 14694-14695 (2004) (Pubitemid 39532132)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.45 , pp. 14694-14695
    • Beckstein, O.1    Tai, K.2    Sansom, M.S.P.3
  • 31
    • 0344406673 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(03)00157-0
    • Soler-Llavina, G. J., Holmgren, M. & Swartz, K. J. Defining the conductance of the closed state in a voltage-gated K channel. Neuron 38, 61-67 (2003) (Pubitemid 36423353)
    • (2003) Neuron , vol.38 , Issue.1 , pp. 61-67
    • Soler-Llavina, G.J.1    Holmgren, M.2    Swartz, K.J.3
  • 32
    • 49349111148 scopus 로고    scopus 로고
    • Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers
    • Tao, X. & MacKinnon, R. Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers. J. Mol. Biol. 382, 24-33 (2008)
    • (2008) J. Mol. Biol , vol.382 , pp. 24-33
    • Tao, X.1    MacKinnon, R.2
  • 33
    • 47249112246 scopus 로고    scopus 로고
    • A kv channel with an altered activation gate sequence displays both 'fast' and 'slow' activation kinetics
    • Labro, A. J., Grottesi, A., Sansom, M. S. P., Raes, A. L. & Snyders, D. J. A Kv channel with an altered activation gate sequence displays both 'fast' and 'slow' activation kinetics. Am. J. Physiol. 294, C1476-C1484 (2008)
    • (2008) Am. J. Physiol , vol.294
    • Labro, A.J.1    Grottesi, A.2    Sansom, M.S.P.3    Raes, A.L.4    Snyders, D.J.5
  • 34
    • 77951547997 scopus 로고    scopus 로고
    • An intersubunit interaction between S4-S5 linker and S6 is responsible for the slow off-gating component in Shaker K channels
    • Batulan, Z., Haddad, G. A. & Blunck, R. An intersubunit interaction between S4-S5 linker and S6 is responsible for the slow off-gating component in Shaker K channels. J. Biol. Chem. 285, 14005-14019 (2010)
    • (2010) J. Biol. Chem , vol.285 , pp. 14005-14019
    • Batulan, Z.1    Haddad, G.A.2    Blunck, R.3
  • 35
    • 84891944267 scopus 로고    scopus 로고
    • Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation
    • Chowdhury, S. & Chanda, B. Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation. J. Gen. Physiol. 103, 321-362 (2011)
    • (2011) J. Gen. Physiol , vol.103 , pp. 321-362
    • Chowdhury, S.1    Chanda, B.2
  • 36
    • 0037131520 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0092-8674(02)01013-9
    • Yifrach, O. & MacKinnon, R. Energetics of pore opening in a voltage-gated K channel. Cell 111, 231-239 (2002) (Pubitemid 35292443)
    • (2002) Cell , vol.111 , Issue.2 , pp. 231-239
    • Yifrach, O.1    MacKinnon, R.2
  • 37
    • 79956125732 scopus 로고    scopus 로고
    • Mode shift of the voltage sensors in Shaker K channels is caused by energetic coupling to the pore domain
    • Haddad, G. A. & Blunck, R. Mode shift of the voltage sensors in Shaker K channels is caused by energetic coupling to the pore domain. J. Gen. Physiol. 137, 455-472 (2011)
    • (2011) J. Gen. Physiol , vol.137 , pp. 455-472
    • Haddad, G.A.1    Blunck, R.2
  • 38
    • 84867766690 scopus 로고    scopus 로고
    • Dual effect of phosphatidyl (4,5)-bisphosphate PIP2 on Shaker K channels
    • Abderemane-Ali, F. et al. Dual effect of phosphatidyl (4,5)-bisphosphate PIP2 on Shaker K channels. J. Biol. Chem. 287, 36158-36167 (2012)
    • (2012) J. Biol. Chem , vol.287 , pp. 36158-36167
    • Abderemane-Ali, F.1
  • 39
    • 0031870974 scopus 로고    scopus 로고
    • + channels. The effect of temperature on ionic and gating currents
    • DOI 10.1085/jgp.112.2.223
    • Rodrguez, B. M., Sigg, D. & Bezanilla, F. Voltage gating of Shaker K channels. The effect of temperature on ionic and gating currents. J. Gen. Physiol. 112, 223-242 (1998) (Pubitemid 28369162)
    • (1998) Journal of General Physiology , vol.112 , Issue.2 , pp. 223-242
    • Rodriguez, B.M.1    Sigg, D.2    Bezanilla, F.3
  • 40
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., Scheuer, T., Zheng, N. & Catterall, W. A. The crystal structure of a voltage-gated sodium channel. Nature 475, 353-358 (2011)
    • (2011) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 41
    • 78649455219 scopus 로고    scopus 로고
    • The contribution of individual subunits to the coupling of the voltage sensor to pore opening in Shaker K channels: Effect of ILT mutations in heterotetramers
    • Gagnon, D. G. & Bezanilla, F. The contribution of individual subunits to the coupling of the voltage sensor to pore opening in Shaker K channels: effect of ILT mutations in heterotetramers. J. Gen. Physiol. 136, 555-568 (2010)
    • (2010) J. Gen. Physiol , vol.136 , pp. 555-568
    • Gagnon, D.G.1    Bezanilla, F.2
  • 43
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz, K. J. Sensing voltage across lipid membranes. Nature 456, 891-897 (2008)
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 44
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: Structure, function, and pathophysiology
    • Catterall, W. A. Ion channel voltage sensors: structure, function, and pathophysiology. Neuron 67, 915-928 (2010)
    • (2010) Neuron , vol.67 , pp. 915-928
    • Catterall, W.A.1
  • 46
    • 83355177269 scopus 로고    scopus 로고
    • In search of a consensus model of the resting state of a voltage-sensing domain
    • Vargas, E., Bezanilla, F. & Roux, B. In search of a consensus model of the resting state of a voltage-sensing domain. Neuron 72, 713-720 (2011)
    • (2011) Neuron , vol.72 , pp. 713-720
    • Vargas, E.1    Bezanilla, F.2    Roux, B.3
  • 47
    • 81755185839 scopus 로고    scopus 로고
    • Gating charge interactions with the S1 segment during activation of a Na channel voltage sensor
    • DeCaen, P. G., Yarov-Yarovoy, V., Scheuer, T. & Catterall, W. A. Gating charge interactions with the S1 segment during activation of a Na channel voltage sensor. Proc. Natl Acad. Sci. USA 108, 18825-18830 (2011)
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 18825-18830
    • Decaen, P.G.1    Yarov-Yarovoy, V.2    Scheuer, T.3    Catterall, W.A.4
  • 49
    • 84859651420 scopus 로고    scopus 로고
    • Mechanism of voltage gating in potassium channels
    • Jensen, M. O. et al. Mechanism of voltage gating in potassium channels. Science 336, 229-233 (2012)
    • (2012) Science , vol.336 , pp. 229-233
    • Jensen, M.O.1
  • 52
    • 1842422868 scopus 로고    scopus 로고
    • + channels: A molecular switch for electrical signaling
    • DOI 10.1016/S0896-6273(04)00116-3, PII S0896627304001163
    • Zhao, Y., Yarov-Yarovoy, V., Scheuer, T. & Catterall, W. A. A gating hinge in Na channels; a molecular switch for electrical signaling. Neuron 41, 859-865 (2004) (Pubitemid 38429730)
    • (2004) Neuron , vol.41 , Issue.6 , pp. 859-865
    • Zhao, Y.1    Yarov-Yarovoy, V.2    Scheuer, T.3    Catterall, W.A.4
  • 53
    • 41449119304 scopus 로고    scopus 로고
    • Coarse-grained md simulations of membrane protein-bilayer self-assembly
    • DOI 10.1016/j.str.2008.01.014, PII S0969212608000683
    • Scott, K. A. et al. Coarse-grained MD simulations of membrane protein-bilayer self-assembly. Structure 16, 621-630 (2008) (Pubitemid 351458703)
    • (2008) Structure , vol.16 , Issue.4 , pp. 621-630
    • Scott, K.A.1    Bond, P.J.2    Ivetac, A.3    Chetwynd, A.P.4    Khalid, S.5    Sansom, M.S.P.6
  • 54
    • 79954524314 scopus 로고    scopus 로고
    • From coarse grained to atomistic: A serial multiscale approach to membrane protein simulations
    • Stansfeld, P. J. & Sansom, M. S. P. From coarse grained to atomistic: a serial multiscale approach to membrane protein simulations. J. Chem. Theo. Comp. 7, 1157-1166 (2011)
    • (2011) J. Chem. Theo. Comp , vol.7 , pp. 1157-1166
    • Stansfeld, P.J.1    Sansom, M.S.P.2
  • 56
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method
    • Kumar, S., Rosenberg, J. M., Bouzida, D., Swendsen, R. H. & Kollman, P. A. The weighted histogram analysis method for free-energy calculations on biomolecules. I. The method. J. Comp. Chem. 13, 1011-1021 (1992)
    • (1992) J. Comp. Chem , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 57
    • 79958185452 scopus 로고    scopus 로고
    • MDAnalysis: A toolkit for the analysis of molecular dynamics simulations
    • Michaud-Agrawal, N., Denning, E. J., Woolf, T. B. & Beckstein, O. MDAnalysis: a toolkit for the analysis of molecular dynamics simulations. J. Comp. Chem. 32, 2319-2327 (2011)
    • (2011) J. Comp. Chem , vol.32 , pp. 2319-2327
    • Michaud-Agrawal, N.1    Denning, E.J.2    Woolf, T.B.3    Beckstein, O.4
  • 58
    • 0035498860 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1038/35102067
    • Bernèche, S. & Roux, B. Energetics of ion conduction through the K channel. Nature 414, 73-77 (2001) (Pubitemid 33041625)
    • (2001) Nature , vol.414 , Issue.6859 , pp. 73-77
    • Berneche, S.1    Roux, B.2
  • 59
    • 53249150686 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer
    • Bond, P. J., Wee, C. L. & Sansom, M. S. P. Coarse-grained molecular dynamics simulations of the energetics of helix insertion into a lipid bilayer. Biochemistry 47, 11321-11331 (2008)
    • (2008) Biochemistry , vol.47 , pp. 11321-11331
    • Bond, P.J.1    Wee, C.L.2    Sansom, M.S.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.