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Typus
KomplettPlagiat
Bearbeiter
Klgn
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 38, Zeilen: 1-12
Quelle: Anézo 2003
Seite(n): 61, Zeilen: 61
[In 1992 and 1993, several research groups reported simulation studies of single component membranes consisting, for instance, of dipalmitoylphosphatidylcholine (DPPC), dilauroylphosphatidylethanolamine (DLPE), or palmitoyloleoylphosphatidylcholine (POPC) molecules, demonstrating that the MD] technique applied to patches of a few phospholipids in water has enormous potential and can give detailed insights into lipid motions and interactions.

During the past ten years, computer hardware has become faster and cheaper, software problems have found innovative solutions, so that impressive improvements in the size and complexity of the simulated systems as well as in calculation time have been achieved. These improvements enable one nowadays to simulate mixed lipid systems (mixing for instance two type of phospholipids [30] or introducing a certain amount of cholesterol [31]), to include small molecules like drugs into the bilayer [32,33], or to insert peptides or even membrane proteins to study their interactions with the lipid components [34,35]. These new applications have been performed with more or less success and the simulation of lipid-protein systems in particular still remains a very challenging area.


30. de Vries, A. H.; Mark, A. E.; Marrink, S. J. J. Phys. Chem. B 2003.

31. Robinson, A. J.; Richards, W. G.; Thomas, P. J.; Hann, M. M. Biophys. J. 1995, 68, 164.

32. Huang, P.; Bertaccini, E.; Loew, G. H. 1995, 12, 725. [sic]

33. Alper, H. E.; Stouch, T. R. 1995, 99, 5724. [sic]

34. Chiu, S. W.; Subramaniam, S.; Jakobson, E. Biophys. J. 1999, 76, 1929.

35. Tieleman, D. P.; Berendsen, H. J. C.; Sansom, M. S. P. Biophys. J. 1999, 76, 1757.

In 1992 and 1993, several research groups reported simulation studies of single component membranes consisting, for instance, of dipalmitoylphosphatidylcholine (DPPC), dilauroylphosphatidylethanolamine (DLPE), or palmitoyloleoylphosphatidylcholine (POPC) molecules, demonstrating that the MD technique applied to patches of a few phospholipids in water has enormous potential and can give detailed insights into lipid motions and interactions.

During the past ten years, computer hardware has become faster and cheaper, software problems have found innovative solutions, so that impressive improvements in the size and complexity of the simulated systems as well as in calculation time have been achieved. These improvements enable one nowadays to simulate mixed lipid systems (mixing for instance two type of phospholipids [57] or introducing a certain amount of cholesterol [58–64]), to include small molecules like drugs into the bilayer [65–73], or to insert peptides or even membrane proteins to study their interactions with the lipid components [61,74–85]. These new applications have been performed with more or less success and the simulation of lipid- protein systems in particular still remains a very challenging area, which can only benefit in the next years from the increase in simulation time scale and system size.


[57] A. H. de Vries, A. E. Mark, and S. J. Marrink. J. Phys. Chem. B, 2003. In press.

[58] A. J. Robinson, W. G. Richards, P. J. Thomas, and M. M. Hann. Biophys. J., 68:164–170, 1995.

[59] K. Tu, M. L. Klein, and D. J. Tobias. Biophys. J., 75:2147–2156, 1998.

[60] A. M. Smondyrev and M. L. Berkowitz. Biophys. J., 77:2075–2089, 1999.

[61] M. Pasenkiewicz-Gierula, K. Murzyn, T. Róg, and C. Czaplewski. Acta Biochim. Pol., 47:601–611, 2000.

[62] M. Pasenkiewicz-Gierula T. Róg, K. Kitamura, and A. Kusumi. Biophys. J., 78:1376– 1389, 2000.

[63] A. Léonard, C. Escrive, M. Laguerre, E. Pebay-Peyroula,W. Néri, T. Pott, J. Katsaras, and E. J. Dufourc. Langmuir, 17:2019–2030, 2001.

[64] A. M. Smondyrev and M. L. Berkowitz. Biophys. J., 80:1649–1658, 2001.

[65] H. E. Alper and T. R. Stouch. J. Phys. Chem., 99:5724–5731, 1995.

[66] P. Huang, E. Bertaccini, and G. H. Loew. J. Biomol. Struct. Dyn., 12:725–754, 1995.

[67] J. J. López Cascales, M. L. Huertas, and J. García de la Torre. Biophys. Chem., 69:1–8, 1997.

[68] M. Aiello, O. Moran, M. Pisciotta, and F. Gambale. Eur. Biophys. J., 27:211–218, 1998.

[69] K. Tu, M. Tarek, M. L. Klein, and D. Scharf. Biophys. J., 75:2123–2134, 1998.

[70] L. Koubi, M. Tarek, M. L. Klein, and D. Scharf. Biophys. J., 78:800–811, 2000.

[71] L. Koubi, M. Tarek, S. Bandyopadhyay, M. L. Klein, and D. Scharf. Biophys. J., 81:3339–3345, 2001.

[72] J. A. Söderhäll and A. Laaksonen. J. Phys. Chem. B, 105:9308–9315, 2001.

[73] A. Grossfield and T. B. Woolf. Langmuir, 18:198–210, 2002.

[74] D. P. Tieleman and H. J. C. Berendsen. Biophys. J., 74:2786–2801, 1998.

[75] D. P. Tieleman, H. J. C. Berendsen, and M. S. P. Sansom. Biophys. J., 76:1757–1769, 1999.

[76] S.-W. Chiu, S. Subramaniam, and E. Jakobsson. Biophys. J., 76:1929–1938, 1999.

[77] S.-W. Chiu, S. Subramaniam, and E. Jakobsson. Biophys. J., 76:1939–1950, 1999.

[78] Y. Z. Tang, W. Z. Chen, C. X. Wang, and Y. Y. Shi. Eur. Biophys. J., 28:478–488, 1999.

[79] M. Nina, S. Bernecke, and B. Roux. Eur. Biophys. J., 29:439–454, 2000.

[80] R. J. Law, L. R. Forrest, K. M. Ranatunga, P. La Rocca, D. P. Tieleman, and M. S. P. Sansom. Proteins: Struct. Func. Genet., 39:47–55, 2000.

[81] L. R. Forrest, A. Kukol, I. T. Arkin, D. P. Tieleman, and M. S. P. Samson. Biophys. J., 78:55–69, 2000.

[82] D. P. Tieleman and M. S. P. Sansom. Int. J. Quant. Chem., 83:166–179, 2001.

[83] J. Baudry, E. Tajkhorshid, F. Molnar, J. Phillips, and K. Schulten. J. Phys. Chem. B, 105:905–918, 2001.

[84] D. E. Elmore and D. A. Dougherty. Biophys. J., 81:1345–1359, 2001.

[85] C. M. Shepherd, H. J. Vogel, and D. J. Tieleman. Biochim. [sic] J., 370:233–243, 2003.

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