Scaling and self-organized criticality in proteins: Lysozyme c

Physical Review E - Statistical, Nonlinear, and Soft Matter Physics

Volumn 80, Issue 5, 2009, Pages

  Phillips, J C ^a  

^a RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL TREND; CLASSICAL FORCE FIELDS; DEFENSINS; EXPERIMENTAL STUDIES; FULLY COMPATIBLE; HYDROPHOBICITY SCALE; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN-PROTEIN INTERACTIONS; REAL-SPACE; SELF-ORGANIZED CRITICALITY; SUBSTRATE BINDING;

BIOINFORMATICS; CRITICALITY (NUCLEAR FISSION); ENZYMES; HYDROPHOBICITY; ORGANIC SOLVENTS; PROGRAMMABLE LOGIC CONTROLLERS; SIMULATORS; WATER ANALYSIS;

PROTEINS;

EID: 71449100768     PISSN: 15393755     EISSN: 15502376     Source Type: Journal    
DOI: 10.1103/PhysRevE.80.051916     Document Type: Article

References (26)

1. P. Bak, C. Tang, and K. Wiesenfeld, Phys. Rev. Lett. 59, 381 (1987). 10.1103/PhysRevLett.59.381
2. M. A. Moret and G. F. Zebende, Phys. Rev. E 75, 011920 (2007). 10.1103/PhysRevE.75.011920
3. J. C. Phillips, Proc. Natl. Acad. Sci. U.S.A. 106, 3107 (2009) 10.1073/pnas.0811262106
4. J. C. Phillips, Proc. Natl. Acad. Sci. U.S.A. 106, 3113 (2009). 10.1073/pnas.0811308105
5. P. Jolles, Lysozymes: Model Enzymes in Biochemistry and Biology (Birkhauser Verlag, Basel, 1996).
6. D. Ringe and G. A. Petsko, Science 320, 1428 (2008). 10.1126/science. 1159747
7. T. Park, D. K. Struck, J. F. Deaton, and R. Young, Proc. Natl. Acad. Sci. U.S.A. 103, 19713 (2006). 10.1073/pnas.0600943103
8. J. Kyte and R. F. Doolittle, J. Mol. Biol. 157, 105 (1982). 10.1016/0022-2836(82)90515-0
9. G. D. Rose, A. R. Geselowitz, G. J. Lesser, R. H. Lee, and M. H. Zehfus, Science 229, 834 (1985). 10.1126/science.4023714
10. P. A. Alexander, Y. He, Y. Chen, J. Orban, and P. N. Bryan, Proc. Natl. Acad. Sci. U.S.A. 104, 11963 (2007). 10.1073/pnas.0700922104
11. A. E. Kister and J. C. Phillips, Proc. Natl. Acad. Sci. U.S.A. 105, 9233 (2008). 10.1073/pnas.0803264105
12. T. Durek, V. Y. Torbeev, and S. B. H. Kent, Proc. Natl. Acad. Sci. U.S.A. 104, 4846 (2007). 10.1073/pnas.0610630104
13. F. Merzel and J. C. Smith, Proc. Natl. Acad. Sci. U.S.A. 99, 5378 (2002). 10.1073/pnas.082335099
14. E. M. Prager and P. Jolles, Lysozymes: Model Enzymes in Biochemistry and Biology (Birkhauser Verlag, Basel, 1996).
15. T. Imoto, Lysozymes: Model Enzymes in Biochemistry and Biology (Birkhauser Verlag, Basel, 1996).
16. C. N. Pace and J. M. Scholtz, Biophys. J. 75, 422 (1998). 10.1016/S0006-3495(98)77529-0
17. D. K. Griffin, BMC Genomics 9, 168 (2008). 10.1186/1471-2164-9-168
18. M. Stuart-Audette, Y. Blouquit, M. Faraggi, C. Sicardi-Roselli, C. Houee-Levin, and P. Jolles, Eur. J. Biochem. 270, 3565 (2003). 10.1046/j.1432-1033.2003.03741.x
19. S. Chakravarty, D. G. Georgiev, P. Boolchand, and M. Micoulaut, J. Phys.: Condens. Matter 17, L1 (2005). 10.1088/0953-8984/17/1/L01
20. R. E. W. Hancock, Lancet 349, 418 (1997). 10.1016/S0140-6736(97)80051-7
21. T. S. Ryge and P. R. Hansen, J. Pept. Sci. 11, 727 (2005). 10.1002/psc.705
22. S. Hayward, A. Kitao, and H. J. C. Berendsen, Proteins 27, 425 (1997). 10.1002/(SICI)1097-0134(199703)27:3<425::AID-PROT10>3.0.CO;2-N
23. N. Hori, G. Chikenji, R. S. Berry, and S. Takada, Proc. Natl. Acad. Sci. U.S.A. 106, 73 (2008). 10.1073/pnas.0811560106
24. J. C. Phillips, e-print arXiv:0808.2312.
25. J. C. Phillips, e-print arXiv:0802.3641.
26. A. Widmer-Cooper, H. Perry, P. Harrowell, and D. R. Reichman, Nat. Phys. 4, 711 (2008). 10.1038/nphys1025