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Volumn 119, Issue 33, 2015, Pages 10390-10398

Melittin Aggregation in Aqueous Solutions: Insight from Molecular Dynamics Simulations

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; AGGREGATES; IONIC STRENGTH; MOLECULAR DYNAMICS; MONOMERS; OLIGOMERS; SOLUTIONS;

EID: 84939788897     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/acs.jpcb.5b03254     Document Type: Article
Times cited : (35)

References (48)
  • 1
    • 0015527253 scopus 로고
    • Bee Wasp Venoms
    • Habermann, E. Bee Wasp Venoms Science 1972, 177, 314-322 10.1126/science.177.4046.314
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 2
    • 0027056421 scopus 로고
    • Thermodynamics of Melittin Tetramerization Determined by Circular-Dichroism and Implications for Protein Folding
    • Wilcox, W.; Eisenberg, D. Thermodynamics of Melittin Tetramerization Determined by Circular-Dichroism and Implications for Protein Folding Protein Sci. 1992, 1, 641-653 10.1002/pro.5560010510
    • (1992) Protein Sci. , vol.1 , pp. 641-653
    • Wilcox, W.1    Eisenberg, D.2
  • 3
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores
    • Yang, L.; Harroun, T. A.; Weiss, T. M.; Ding, L.; Huang, H. W. Barrel-Stave Model or Toroidal Model? A Case Study on Melittin Pores Biophys. J. 2001, 81, 1475-1485 10.1016/S0006-3495(01)75802-X
    • (2001) Biophys. J. , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 4
    • 0019332396 scopus 로고
    • High-Resolution 1H-NMR Studies of Self-Aggregation of Melittin in Aqueous Solution
    • Brown, L. R.; Lauterwein, J.; Wüthrich, K. High-Resolution 1H-NMR Studies of Self-Aggregation of Melittin in Aqueous Solution Biochim. Biophys. Acta, Protein Struct. 1980, 622, 231-244 10.1016/0005-2795(80)90034-3
    • (1980) Biochim. Biophys. Acta, Protein Struct. , vol.622 , pp. 231-244
    • Brown, L.R.1    Lauterwein, J.2    Wüthrich, K.3
  • 5
    • 0019332428 scopus 로고
    • High-Resolution 1H-NMR Studies of Monomeric Melittin in Aqueous Solution
    • Lauterwein, J.; Brown, L. R.; Wüthrich, K. High-Resolution 1H-NMR Studies of Monomeric Melittin in Aqueous Solution Biochim. Biophys. Acta, Protein Struct. 1980, 622, 219-230 10.1016/0005-2795(80)90033-1
    • (1980) Biochim. Biophys. Acta, Protein Struct. , vol.622 , pp. 219-230
    • Lauterwein, J.1    Brown, L.R.2    Wüthrich, K.3
  • 6
    • 0032532218 scopus 로고    scopus 로고
    • The Structure of the Melittin Tetramer at Different Temperatures - An NOE-Based Calculation with Chemical Shift Refinement
    • Iwadate, M.; Asakura, T.; Williamson, M. P. The Structure of the Melittin Tetramer at Different Temperatures-an NOE-Based Calculation with Chemical Shift Refinement Eur. J. Biochem. 1998, 257, 479-487 10.1046/j.1432-1327.1998.2570479.x
    • (1998) Eur. J. Biochem. , vol.257 , pp. 479-487
    • Iwadate, M.1    Asakura, T.2    Williamson, M.P.3
  • 7
    • 84866347612 scopus 로고    scopus 로고
    • Nmr Studies on the Monomer-Tetramer Transition of Melittin in an Aqueous Solution at High and Low Temperatures
    • Miura, Y. Nmr Studies on the Monomer-Tetramer Transition of Melittin in an Aqueous Solution at High and Low Temperatures Eur. Biophys. J. 2012, 41, 629-636 10.1007/s00249-012-0831-7
    • (2012) Eur. Biophys. J. , vol.41 , pp. 629-636
    • Miura, Y.1
  • 8
    • 0028804445 scopus 로고
    • Modulation of Melittin-Induced Lysis by Surface-Charge Density of Membranes
    • Monette, M.; Lafleur, M. Modulation of Melittin-Induced Lysis by Surface-Charge Density of Membranes Biophys. J. 1995, 68, 187-195 10.1016/S0006-3495(95)80174-8
    • (1995) Biophys. J. , vol.68 , pp. 187-195
    • Monette, M.1    Lafleur, M.2
  • 9
    • 0020479123 scopus 로고
    • The Structure of Melittin. II. Interpretation of the Structure
    • Terwilliger, T. C.; Eisenberg, D. The Structure of Melittin. II. Interpretation of the Structure J. Biol. Chem. 1982, 257, 6016-6022
    • (1982) J. Biol. Chem. , vol.257 , pp. 6016-6022
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 10
    • 0020479083 scopus 로고
    • The Structure of Melittin. I. Structure Determination and Partial Refinement
    • Terwilliger, T. C.; Eisenberg, D. The Structure of Melittin. I. Structure Determination and Partial Refinement J. Biol. Chem. 1982, 257, 6010-6015
    • (1982) J. Biol. Chem. , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 11
    • 0018487558 scopus 로고
    • The Self-Association of Melittin and Its Binding to Lipids: An Intrinsic Fluorescence Polarization Study
    • Faucon, J. F.; Dufourcq, J.; Lussan, C. The Self-Association of Melittin and Its Binding to Lipids: An Intrinsic Fluorescence Polarization Study FEBS Lett. 1979, 102, 187-190 10.1016/0014-5793(79)80956-4
    • (1979) FEBS Lett. , vol.102 , pp. 187-190
    • Faucon, J.F.1    Dufourcq, J.2    Lussan, C.3
  • 12
    • 0018483723 scopus 로고
    • Conformational Change and Self Association of Monomeric Melittin
    • Talbot, J. C.; Dufourcq, J.; de Bony, J.; Faucon, J. F.; Lussan, C. Conformational Change and Self Association of Monomeric Melittin FEBS Lett. 1979, 102, 191-193 10.1016/0014-5793(79)80957-6
    • (1979) FEBS Lett. , vol.102 , pp. 191-193
    • Talbot, J.C.1    Dufourcq, J.2    De Bony, J.3    Faucon, J.F.4    Lussan, C.5
  • 13
    • 0022798958 scopus 로고
    • The Structure of Melittin in Membranes
    • Vogel, H.; Jahnig, F. The Structure of Melittin in Membranes Biophys. J. 1986, 50, 573-582 10.1016/S0006-3495(86)83497-X
    • (1986) Biophys. J. , vol.50 , pp. 573-582
    • Vogel, H.1    Jahnig, F.2
  • 14
    • 25444458922 scopus 로고    scopus 로고
    • Ultrafast Hydration Dynamics in Melittin Folding and Aggregation: Helix Formation and Tetramer Self-Assembly
    • Qiu, W. H.; Zhang, L. Y.; Kao, Y. T.; Lu, W. Y.; Li, T. P.; Kim, J.; Sollenberger, G. M.; Wang, L. J.; Zhong, D. P. Ultrafast Hydration Dynamics in Melittin Folding and Aggregation: Helix Formation and Tetramer Self-Assembly J. Phys. Chem. B 2005, 109, 16901-16910 10.1021/jp0511754
    • (2005) J. Phys. Chem. B , vol.109 , pp. 16901-16910
    • Qiu, W.H.1    Zhang, L.Y.2    Kao, Y.T.3    Lu, W.Y.4    Li, T.P.5    Kim, J.6    Sollenberger, G.M.7    Wang, L.J.8    Zhong, D.P.9
  • 15
    • 69149100640 scopus 로고    scopus 로고
    • Solvation in Protein (Un)Folding of Melittin Tetramer-Monomer Transition
    • Othon, C. M.; Kwon, O. H.; Lin, M. M.; Zewail, A. H. Solvation in Protein (Un)Folding of Melittin Tetramer-Monomer Transition Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 12593-12598 10.1073/pnas.0905967106
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 12593-12598
    • Othon, C.M.1    Kwon, O.H.2    Lin, M.M.3    Zewail, A.H.4
  • 17
    • 11244272784 scopus 로고    scopus 로고
    • Dissection of Antibacterial and Toxic Activity of Melittin - A Leucine Zipper Motif Plays a Crucial Role in Determining Its Hemolytic Activity but Not Antibacterial Activity
    • Asthana, N.; Yadav, S. P.; Ghosh, J. K. Dissection of Antibacterial and Toxic Activity of Melittin-a Leucine Zipper Motif Plays a Crucial Role in Determining Its Hemolytic Activity but Not Antibacterial Activity J. Biol. Chem. 2004, 279, 55042-55050 10.1074/jbc.M408881200
    • (2004) J. Biol. Chem. , vol.279 , pp. 55042-55050
    • Asthana, N.1    Yadav, S.P.2    Ghosh, J.K.3
  • 19
    • 84880996730 scopus 로고    scopus 로고
    • Melittin: A Lytic Peptide with Anticancer Properties
    • Gajski, G.; Garaj-Vrhovac, V. Melittin: A Lytic Peptide with Anticancer Properties Environ. Toxicol. Pharmacol. 2013, 36, 697-705 10.1016/j.etap.2013.06.009
    • (2013) Environ. Toxicol. Pharmacol. , vol.36 , pp. 697-705
    • Gajski, G.1    Garaj-Vrhovac, V.2
  • 20
    • 0025870831 scopus 로고
    • Aggregation State of Melittin in Lipid Vesicle Membranes
    • John, E.; Jahnig, F. Aggregation State of Melittin in Lipid Vesicle Membranes Biophys. J. 1991, 60, 319-328 10.1016/S0006-3495(91)82056-2
    • (1991) Biophys. J. , vol.60 , pp. 319-328
    • John, E.1    Jahnig, F.2
  • 21
    • 0024471945 scopus 로고
    • Characterization of Selectively C-13-Labeled Synthetic Melittin and Melittin Analogs in Isotropic Solvents by Circular-Dichroism, Fluorescence, and NMR-Spectroscopy
    • Weaver, A. J.; Kemple, M. D.; Prendergast, F. G. Characterization of Selectively C-13-Labeled Synthetic Melittin and Melittin Analogs in Isotropic Solvents by Circular-Dichroism, Fluorescence, and NMR-Spectroscopy Biochemistry 1989, 28, 8614-8623 10.1021/bi00447a052
    • (1989) Biochemistry , vol.28 , pp. 8614-8623
    • Weaver, A.J.1    Kemple, M.D.2    Prendergast, F.G.3
  • 22
    • 0020482260 scopus 로고
    • Effect of the State of Association of Melittin and Phospholipids on Their Reciprocal Binding
    • Talbot, J. C.; Lalanne, J.; Faucon, J. F.; Dufourcq, J. Effect of the State of Association of Melittin and Phospholipids on Their Reciprocal Binding Biochim. Biophys. Acta, Biomembr. 1982, 689, 106-112 10.1016/0005-2736(82)90194-8
    • (1982) Biochim. Biophys. Acta, Biomembr. , vol.689 , pp. 106-112
    • Talbot, J.C.1    Lalanne, J.2    Faucon, J.F.3    Dufourcq, J.4
  • 23
    • 0038762371 scopus 로고
    • Does Dimeric Melittin Occur in Aqueous-Solutions
    • Schubert, D.; Pappert, G.; Boss, K. Does Dimeric Melittin Occur in Aqueous-Solutions Biophys. J. 1985, 48, 327-329 10.1016/S0006-3495(85)83786-3
    • (1985) Biophys. J. , vol.48 , pp. 327-329
    • Schubert, D.1    Pappert, G.2    Boss, K.3
  • 24
    • 0031972614 scopus 로고    scopus 로고
    • Hydrogen Bonding in Helical Polypeptides from Molecular Dynamics Simulations and Amide Hydrogen Exchange Analysis: Alamethicin and Melittin in Methanol
    • Sessions, R. B.; Gibbs, N.; Dempsey, C. E. Hydrogen Bonding in Helical Polypeptides from Molecular Dynamics Simulations and Amide Hydrogen Exchange Analysis: Alamethicin and Melittin in Methanol Biophys. J. 1998, 74, 138-152 10.1016/S0006-3495(98)77775-6
    • (1998) Biophys. J. , vol.74 , pp. 138-152
    • Sessions, R.B.1    Gibbs, N.2    Dempsey, C.E.3
  • 25
    • 0033033560 scopus 로고    scopus 로고
    • Hydrophobic Hydration of Amphipathic Peptides
    • Cheng, Y. K.; Sheu, W. S.; Rossky, P. J. Hydrophobic Hydration of Amphipathic Peptides Biophys. J. 1999, 76, 1734-1743 10.1016/S0006-3495(99)77335-2
    • (1999) Biophys. J. , vol.76 , pp. 1734-1743
    • Cheng, Y.K.1    Sheu, W.S.2    Rossky, P.J.3
  • 26
    • 24344448662 scopus 로고    scopus 로고
    • Observation of a Dewetting Transition in the Collapse of the Melittin Tetramer
    • Liu, P.; Huang, X. H.; Zhou, R. H.; Berne, B. J. Observation of a Dewetting Transition in the Collapse of the Melittin Tetramer Nature 2005, 437, 159-162 10.1038/nature03926
    • (2005) Nature , vol.437 , pp. 159-162
    • Liu, P.1    Huang, X.H.2    Zhou, R.H.3    Berne, B.J.4
  • 27
    • 84873383442 scopus 로고    scopus 로고
    • Inclusion of Lateral Pressure/Curvature Stress Effects in Implicit Membrane Models
    • Zhan, H.; Lazaridis, T. Inclusion of Lateral Pressure/Curvature Stress Effects in Implicit Membrane Models Biophys. J. 2013, 104, 643-654 10.1016/j.bpj.2012.12.022
    • (2013) Biophys. J. , vol.104 , pp. 643-654
    • Zhan, H.1    Lazaridis, T.2
  • 28
    • 84877086411 scopus 로고    scopus 로고
    • Conformational States of Melittin at a Bilayer Interface
    • Andersson, M.; Ulmschneider, J. P.; Ulmschneider, M. B.; White, S. H. Conformational States of Melittin at a Bilayer Interface Biophys. J. 2013, 104, L12-L14 10.1016/j.bpj.2013.02.006
    • (2013) Biophys. J. , vol.104 , pp. 12-L14
    • Andersson, M.1    Ulmschneider, J.P.2    Ulmschneider, M.B.3    White, S.H.4
  • 29
    • 84865318587 scopus 로고    scopus 로고
    • Binding and Reorientation of Melittin in a POPC Bilayer: Computer Simulations
    • Irudayam, S. J.; Berkowitz, M. L. Binding and Reorientation of Melittin in a POPC Bilayer: Computer Simulations Biochim. Biophys. Acta, Biomembr. 2012, 1818, 2975-2981 10.1016/j.bbamem.2012.07.026
    • (2012) Biochim. Biophys. Acta, Biomembr. , vol.1818 , pp. 2975-2981
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 30
    • 79959997001 scopus 로고    scopus 로고
    • Influence of the Arrangement and Secondary Structure of Melittin Peptides on the Formation and Stability of Toroidal Pores
    • Irudayam, S. J.; Berkowitz, M. L. Influence of the Arrangement and Secondary Structure of Melittin Peptides on the Formation and Stability of Toroidal Pores Biochim. Biophys. Acta, Biomembr. 2011, 1808, 2258-2266 10.1016/j.bbamem.2011.04.021
    • (2011) Biochim. Biophys. Acta, Biomembr. , vol.1808 , pp. 2258-2266
    • Irudayam, S.J.1    Berkowitz, M.L.2
  • 31
    • 77953724763 scopus 로고    scopus 로고
    • Antimicrobial Peptides in Toroidal and Cylindrical Pores
    • Mihajlovic, M.; Lazaridis, T. Antimicrobial Peptides in Toroidal and Cylindrical Pores Biochim. Biophys. Acta, Biomembr. 2010, 1798, 1485-1493 10.1016/j.bbamem.2010.04.004
    • (2010) Biochim. Biophys. Acta, Biomembr. , vol.1798 , pp. 1485-1493
    • Mihajlovic, M.1    Lazaridis, T.2
  • 32
    • 74949104869 scopus 로고    scopus 로고
    • Cause and Effect of Melittin-Induced Pore Formation: A Computational Approach
    • Manna, M.; Mukhopadhyay, C. Cause and Effect of Melittin-Induced Pore Formation: A Computational Approach Langmuir 2009, 25, 12235-12242 10.1021/la902660q
    • (2009) Langmuir , vol.25 , pp. 12235-12242
    • Manna, M.1    Mukhopadhyay, C.2
  • 33
    • 0011613265 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation of Melittin in a Dimyristoylphosphatidylcholine Bilayer Membrane
    • Bernèche, S.; Nina, M.; Roux, B. Molecular Dynamics Simulation of Melittin in a Dimyristoylphosphatidylcholine Bilayer Membrane Biophys. J. 1998, 75, 1603-1618 10.1016/S0006-3495(98)77604-0
    • (1998) Biophys. J. , vol.75 , pp. 1603-1618
    • Bernèche, S.1    Nina, M.2    Roux, B.3
  • 34
    • 0036229927 scopus 로고    scopus 로고
    • Simulations of Membranes and Other Interfacial Systems Using P2(1) and Pc Periodic Boundary Conditions
    • Dolan, E. A.; Venable, R. M.; Pastor, R. W.; Brooks, B. R. Simulations of Membranes and Other Interfacial Systems Using P2(1) and Pc Periodic Boundary Conditions Biophys. J. 2002, 82, 2317-2325 10.1016/S0006-3495(02)75577-X
    • (2002) Biophys. J. , vol.82 , pp. 2317-2325
    • Dolan, E.A.1    Venable, R.M.2    Pastor, R.W.3    Brooks, B.R.4
  • 35
    • 0038675609 scopus 로고    scopus 로고
    • Effective Energy Function for Proteins in Lipid Membranes
    • Lazaridis, T. Effective Energy Function for Proteins in Lipid Membranes Proteins: Struct., Funct., Genet. 2003, 52, 176-192 10.1002/prot.10410
    • (2003) Proteins: Struct., Funct., Genet. , vol.52 , pp. 176-192
    • Lazaridis, T.1
  • 37
    • 0034091671 scopus 로고    scopus 로고
    • Protein-Induced Membrane Disorder: A Molecular Dynamics Study of Melittin in a Dipalmitoylphosphatidylcholine Bilayer
    • Bachar, M.; Becker, O. M. Protein-Induced Membrane Disorder: A Molecular Dynamics Study of Melittin in a Dipalmitoylphosphatidylcholine Bilayer Biophys. J. 2000, 78, 1359-1375 10.1016/S0006-3495(00)76690-2
    • (2000) Biophys. J. , vol.78 , pp. 1359-1375
    • Bachar, M.1    Becker, O.M.2
  • 38
    • 70350238527 scopus 로고    scopus 로고
    • Membrane Poration by Antimicrobial Peptides Combining Atomistic and Coarse-Grained Descriptions
    • Rzepiela, A. J.; Sengupta, D.; Goga, N.; Marrink, S. J. Membrane Poration by Antimicrobial Peptides Combining Atomistic and Coarse-Grained Descriptions Faraday Discuss. 2010, 144, 431-443 10.1039/B901615E
    • (2010) Faraday Discuss. , vol.144 , pp. 431-443
    • Rzepiela, A.J.1    Sengupta, D.2    Goga, N.3    Marrink, S.J.4
  • 39
    • 84889648332 scopus 로고    scopus 로고
    • Free-Energy Landscape of Protein Oligomerization from Atomistic Simulations
    • Barducci, A.; Bonomi, M.; Prakash, M. K.; Parrinello, M. Free-Energy Landscape of Protein Oligomerization from Atomistic Simulations Proc. Natl. Acad. Sci. U. S. A. 2013, 110, E4708-E4713 10.1073/pnas.1320077110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 4708-E4713
    • Barducci, A.1    Bonomi, M.2    Prakash, M.K.3    Parrinello, M.4
  • 40
    • 0034763782 scopus 로고    scopus 로고
    • Solid-State NMR Structure Determination of Melittin in a Lipid Environment
    • Lam, Y. H.; Wassall, S. R.; Morton, C. J.; Smith, R.; Separovic, F. Solid-State NMR Structure Determination of Melittin in a Lipid Environment Biophys. J. 2001, 81, 2752-2761 10.1016/S0006-3495(01)75918-8
    • (2001) Biophys. J. , vol.81 , pp. 2752-2761
    • Lam, Y.H.1    Wassall, S.R.2    Morton, C.J.3    Smith, R.4    Separovic, F.5
  • 41
    • 0018110023 scopus 로고
    • Variations in Circular-Dichroism and Proton-NMR Relaxation Properties of Melittin Upon Interaction with Phospholipids
    • Strom, R.; Crifo, C.; Viti, V.; Guidoni, L.; Podo, F. Variations in Circular-Dichroism and Proton-NMR Relaxation Properties of Melittin Upon Interaction with Phospholipids FEBS Lett. 1978, 96, 45-50 10.1016/0014-5793(78)81059-X
    • (1978) FEBS Lett. , vol.96 , pp. 45-50
    • Strom, R.1    Crifo, C.2    Viti, V.3    Guidoni, L.4    Podo, F.5
  • 42
    • 0019852408 scopus 로고
    • The Sting - Melittin Forms Channels in Lipid Bilayers
    • Tosteson, M. T.; Tosteson, D. C. The Sting-Melittin Forms Channels in Lipid Bilayers Biophys. J. 1981, 36, 109-116 10.1016/S0006-3495(81)84719-4
    • (1981) Biophys. J. , vol.36 , pp. 109-116
    • Tosteson, M.T.1    Tosteson, D.C.2
  • 43
    • 0031235787 scopus 로고    scopus 로고
    • Dielectric Properties of Aqueous Nacl Solutions at Microwave Frequencies
    • Nörtemann, K.; Hilland, J.; Kaatze, U. Dielectric Properties of Aqueous Nacl Solutions at Microwave Frequencies J. Phys. Chem. A 1997, 101, 6864-6869 10.1021/jp971623a
    • (1997) J. Phys. Chem. A , vol.101 , pp. 6864-6869
    • Nörtemann, K.1    Hilland, J.2    Kaatze, U.3
  • 44
    • 5244283949 scopus 로고
    • Mutual Coagulation of Colloidal Dispersions
    • Hogg, R.; Healy, T. W.; Fuerstenau, D. W. Mutual Coagulation of Colloidal Dispersions Trans. Faraday Soc. 1966, 62, 1638-1651 10.1039/tf9666201638
    • (1966) Trans. Faraday Soc. , vol.62 , pp. 1638-1651
    • Hogg, R.1    Healy, T.W.2    Fuerstenau, D.W.3
  • 45
    • 65249093640 scopus 로고    scopus 로고
    • Thermodynamics of Melittin Binding to Lipid Bilayers. Aggregation and Pore Formation
    • Klocek, G.; Schulthess, T.; Shai, Y.; Seelig, J. Thermodynamics of Melittin Binding to Lipid Bilayers. Aggregation and Pore Formation Biochemistry 2009, 48, 2586-2596 10.1021/bi802127h
    • (2009) Biochemistry , vol.48 , pp. 2586-2596
    • Klocek, G.1    Schulthess, T.2    Shai, Y.3    Seelig, J.4
  • 47
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual Molecular Dynamics
    • Humphrey, W.; Dalke, A.; Schulten, K. VMD: Visual Molecular Dynamics J. Mol. Graphics 1996, 14, 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 48
    • 26444452027 scopus 로고    scopus 로고
    • Protein Secondary Structure Assignment Revisited: A Detailed Analysis of Different Assignment Methods
    • Martin, J.; Letellier, G.; Marin, A.; Taly, J. F.; de Brevern, A. G.; Gibrat, J. F. Protein Secondary Structure Assignment Revisited: A Detailed Analysis of Different Assignment Methods BMC Struct. Biol. 2005, 5, 17 10.1186/1472-6807-5-17
    • (2005) BMC Struct. Biol. , vol.5 , pp. 17
    • Martin, J.1    Letellier, G.2    Marin, A.3    Taly, J.F.4    De Brevern, A.G.5    Gibrat, J.F.6


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