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Erratum: “Coherent phonon excitation and linear thermal expansion in structural dynamics and ultrafast electron diffraction of laser-heated metals” [J. Chem. Phys. 128, 164702 (2008)]

The trigger sequence in the GCN4 leucine zipper: alpha-helical propensity and multistate dynamics of folding and dimerization

J. Chem. Phys. 129, 175103 (2008); doi:10.1063/1.3006421

Published 7 November 2008

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Prem P. Chapagain, Yanxin Liu, and Bernard S. Gerstman
Department of Physics, Florida International University, University Park, Miami, Florida 33199, USA
We investigate the importance of the trigger sequence in the folding and dimerization of the GCN4 leucine zipper. We examine the role of the enhanced propensity of the amino acids in the trigger sequence to form an alpha-helix. Using computer simulations, we calculate heat capacities, free energy profiles, and the probability for successful dimerization as a function of the strength of the alpha-helical propensity of the trigger sequence. Our results elucidate the experimentally observed importance of the trigger sequence for dimerization and why it is not necessary for the trigger to have a specific “consensus” sequence of amino acids. We also find that a stronger trigger sequence not only increases the probability for dimerization but also changes the dimerization dynamics by introducing multiple intermediate states. ©2008 American Institute of Physics
History: Received 19 August 2008; accepted 3 October 2008; published 7 November 2008
Permalink: http://link.aip.org/link/?JCPSA6/129/175103/1
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KEYWORDS and PACS

Keywords
PACS
  • 87.15.Cc
    Folding of biomolecules: thermodynamics, statistical mechanics, models and pathways
  • 87.14.E-
    Proteins
  • 87.19.Pp
    Biothermics and thermal processes in biology (higher organisms)
  • 87.10.-e
    General theory and mathematical aspects (biological/medical physics)
  • YEAR: 2008

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ISSN:
0021-9606 (print)   1089-7690 (online)
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REFERENCES (53)

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  1. S. Jones and J. M. Thornton, Proc. Natl. Acad. Sci. U.S.A. 93, 13 (1996).
  2. E. D. Levy, J. B. Pereira-Leal, C. Chothia, and S. A. Teichmann, PLOS Comput. Biol. 2, e155 (2006).
  3. E. K. O'Shea, J. D. Klemm, P. S. Kim, and T. Alber, Science 254, 539 (1991).
  4. D. A. Parry, R. D. Fraser, and J. M. Squire, J. Struct. Biol. 163, 258 (2008).
  5. T. Alber, Curr. Opin. Genet. Dev. 2, 205 (1992).
  6. J. A. Zitzewitz, B. Ibarra-Molero, D. R. Fishel, K. L. Terry, and C. R. Matthews, J. Mol. Biol. 296, 1105 (2000).
  7. W. L. DeLano and A. T. Brunger, Proteins 20, 105 (1994).
  8. M. Nilges and A. T. Brunger, Proteins 15, 133 (1993).
  9. D. Mohanty, B. N. Dominy, A. Kolinski, C. L. Brooks III, and J. Skolnick, Proteins 35, 447 (1999)
  10. D. Mohanty, A. Kolinski, and J. Skolnick, Biophys. J. 77, 54 (1999).
  11. X. Zeng, H. Zhu, H. A. Lashuel, and J. C. Hu, Protein Sci. 6, 2218 (1997).
  12. O. D. Monera, N. E. Zhou, P. Lavigne, C. M. Kay, and R. S. Hodges, J. Biol. Chem. 271, 3995 (1996).
  13. A. A. Gorfe, P. Ferrara, A. Caflisch, D. N. Marti, H. R. Bosshard, and I. Jelesarov, Proteins 46, 41 (2002).
  14. M. E. Holtzer, G. L. Bretthorst, D. A. d'Avignon, R. H. Angeletti, L. Mints, and A. Holtzer, Biophys. J. 80, 939 (2001).
  15. T. Cellmer, D. Bratko, J. M. Prausnitz, and H. Blanch, J. Chem. Phys. 122, 174908 (2005)
  16. Biotechnol. Bioeng. 89, 78 (2005).
  17. T. Wang, W. L. Lau, W. F. DeGrado, and F. Gai, Biophys. J. 89, 4180 (2005).
  18. M. Gruber and A. N. Lupas, Trends Biochem. Sci. 28, 679 (2003).
  19. M. Gruber, J. Soding, and A. N. Lupas, J. Struct. Biol. 155, 140 (2006).
  20. M. Vieth, A. Kolinski, C. L. Brooks III, and J. Skolnick, J. Mol. Biol. 237, 361 (1994).
  21. M. Vieth, A. Kolinski, C. L. Brooks III, and J. Skolnick, J. Mol. Biol. 251, 448 (1995).
  22. H. R. Bosshard, E. Durr, T. Hitz, and I. Jelesarov, Biochemistry 40, 3544 (2001).
  23. P. B. Harbury, T. Zhang, P. S. Kim, and T. Alber, Science 262, 1401 (1993).
  24. A. Maucuer, J. H. Camonis, and A. Sobel, Proc. Natl. Acad. Sci. U.S.A. 92, 3100 (1995).
  25. A. Hach, T. Hon, and L. Zhang, J. Biol. Chem. 275, 248 (2000).
  26. A. Hillar, D. E. Culham, Y. I. Vernikovska, J. M. Wood, and J. M. Boggs, Biochemistry 44, 10170 (2005).
  27. L. B. Moran, J. P. Schneider, A. Kentsis, G. A. Reddy, and T. R. Sosnick, Proc. Natl. Acad. Sci. U.S.A. 96, 10699 (1999).
  28. P. Lavigne, F. D. Sonnichsen, C. M. Kay, and R. S. Hodges, Science 271, 1136 (1996).
  29. W. K. Meisner and T. R. Sosnick, Proc. Natl. Acad. Sci. U.S.A. 101, 13478 (2004).
  30. R. A. Kammerer, T. Schulthess, R. Landwehr, A. Lustig, J. Engel, U. Aebi, and M. O. Steinmetz, Proc. Natl. Acad. Sci. U.S.A. 95, 13419 (1998).
  31. M. O. Steinmetz, A. Stock, T. Schulthess, R. Landwehr, A. Lustig, J. Faix, G. Gerisch, U. Aebi, and R. A. Kammerer, EMBO J. 17, 1883 (1998).
  32. M. O. Steinmetz, I. Jelesarov, W. M. Matousek, S. Honnappa, W. Jahnke, J. H. Missimer, S. Frank, A. T. Alexandrescu, and R. A. Kammerer, Proc. Natl. Acad. Sci. U.S.A. 104, 7062 (2007).
  33. D. L. Lee, P. Lavigne, and R. S. Hodges, J. Mol. Biol. 306, 539 (2001).
  34. D. L. Lee, S. Ivaninskii, P. Burkhard, and R. S. Hodges, Protein Sci. 12, 1395 (2003).
  35. A. I. Dragan and P. L. Privalov, J. Mol. Biol. 321, 891 (2002).
  36. R. M. Hoffman and B. D. Sykes, Proteins 73, 338 (2008).
  37. J. H. Missimer, M. O. Steinmetz, W. Jahnke, F. K. Winkler, W. F. van Gunsteren, and X. Daura, Chem. Biodivers. 2, 1086 (2005).
  38. Y. C. Kim and G. Hummer, J. Mol. Biol. 375, 1416 (2008).
  39. Y. Liu, P. P. Chapagain, J. L. Parra, and B. S. Gerstman, J. Chem. Phys. 128, 045106 (2008).
  40. J. Skolnick and A. Kolinski, J. Mol. Biol. 221, 499 (1991).
  41. P. P. Chapagain, J. L. Parra, B. S. Gerstman, and Y. Liu, J. Chem. Phys. 127, 075103 (2007).
  42. B. S. Gerstman and P. P. Chapagain, J. Chem. Phys. 123, 054901 (2005).
  43. A. N. Lupas and M. Gruber, Adv. Protein Chem. 70, 37 (2005).
  44. W. M. Matousek, B. Ciani, C. A. Fitch, B. Garcia-Moreno, R. A. Kammerer, and A. T. Alexandrescu, J. Mol. Biol. 374, 206 (2007).
  45. R. A. Kammerer, V. A. Jaravine, S. Frank, T. Schulthess, R. Landwehr, A. Lustig, C. Garcia-Echeverria, A. T. Alexandrescu, J. Engel, and M. O. Steinmetz, J. Biol. Chem. 276, 13685 (2001).
  46. E. J. Spek, A. H. Bui, M. Lu, and N. R. Kallenbach, Protein Sci. 7, 2431 (1998).
  47. S. A. Potekhin, V. N. Medvedkin, I. A. Kashparov, and S. Venyaminov, Protein Eng. 7, 1097 (1994).
  48. M. Portwich, S. Keller, H. M. Strauss, C. C. Mahrenholz, I. Kretzschmar, A. Kramer, and R. Volkmer, Angew. Chem., Int. Ed. Engl. 46, 1654 (2007).
  49. P. P. Chapagain and B. S. Gerstman, Biopolymers 81, 167 (2006).
  50. J. C. Hu, N. E. Newell, B. Tidor, and R. T. Sauer, Protein Sci. 2, 1072 (1993).
  51. R. A. Kammerer, T. Schulthess, R. Landwehr, A. Lustig, D. Fischer, and J. Engel, J. Biol. Chem. 273, 10602 (1998).
  52. A. M. Ferrenberg and R. H. Swendsen, Phys. Rev. Lett. 63, 1195 (1989).
  53. N. D. Socci and J. N. Onuchic, J. Chem. Phys. 103, 4732 (1995).
  54. Y. Bai, T. R. Sosnick, L. Mayne, and S. W. Englander, Science 269, 192 (1995).
  55. A. G. Turjanski, J. S. Gutkind, R. B. Best, and G. Hummer, PLOS Comput. Biol. 4, e1000060 (2008).

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