On the inverse temperature transition and development of an entropic elastomeric force of the elastin mimetic peptide [LGGVG] 3,7

Journal of Chemical Physics

Volumn 136, Issue 8, 2012, Pages

  Huang, Jiaxin ^a   Sun, Cheng ^a   Mitchell, Odingo ^a   Ng, Nicole ^a   Wang, Zhao Na ^a   Boutis, Gregory S ^a  

^a CITY UNIVERSITY OF NEW YORK   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELASTIN PEPTIDES; FREQUENCY MODES; HIGH-FREQUENCY MODE; INVERSE TEMPERATURE TRANSITIONS; LOW-FREQUENCY MODES; MODEL PEPTIDES; MOLECULAR DYNAMICS SIMULATIONS; SIDE-CHAINS; STRAINED CONDITION; THERMAL AND MECHANICAL PROPERTIES; THERMAL BEHAVIORS; WATER MOLECULE;

ELASTICITY; ELONGATION; ENTROPY; GLYCOPROTEINS; HYDROGEN BONDS; MOLECULAR DYNAMICS; PEPTIDES;

BIOMIMETICS;

ELASTIN; ELASTOMER; HYDROGEN; PEPTIDE; WATER;

ARTICLE; BIOMIMETICS; CHEMISTRY; ENTROPY; HYDROGEN BOND; MOLECULAR DYNAMICS; PROTEIN CONFORMATION;

BIOMIMETICS; ELASTIN; ELASTOMERS; ENTROPY; HYDROGEN; HYDROGEN BONDING; MOLECULAR DYNAMICS SIMULATION; PEPTIDES; PROTEIN CONFORMATION; WATER;

EID: 84857878938     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3685454     Document Type: Article

References (41)

1. C. A. Hoeve and P. J. Flory, J. Am. Chem. Soc. 80, 6523 (1958). 10.1021/ja01557a016
2. D. W. Urry and T. M. Parker, J. Muscle Res. Cell. Motil. 23, 543 (2002). 10.1023/A:1023422925910 (Pubitemid 36583671)
3. D. W. Urry, J. Protein. Chem. 7, 1 (1987). 10.1007/BF01025411
4. D. W. Urry, R. G. Shaw, and K. U. Prasad, Biochem. Biophys. Res. Commun. 130, 50 (1985). 10.1016/0006-291X(85)90380-8 (Pubitemid 15248998)
5. D. W. Urry, T. L. Trapane, and K. U. Prasad, Biopolymers 24, 2345 (1985). 10.1002/bip.360241212
6. D. W. Urry, T. L. Trapane, and K. U. Prasad, Biochemistry 24, 5182 (1985). 10.1021/bi00340a034 (Pubitemid 15242624)
7. B. Li, D. O. Alonso, and V. Dagett, J. Mol. Biol. 305, 581 (2001). 10.1006/jmbi.2000.4306 (Pubitemid 33032863)
8. H. Meirovitch, J. Miao, and J. Klein-Seetharamanmx-Seetharaman, J. Mol. Biol. 344, 797 (2004). 10.1016/j.jmb.2004.09.061 (Pubitemid 39469221)
9. E. Schreiner, C. Nicolini, B. Ludolph, R. Ravindra, N. Otte, A. Kohlmeyer, R. Rousseau, R. Winter, and D. Marx, Phys. Rev. Lett. 92, 148101 (2004). 10.1103/PhysRevLett.92.148101
10. R. Glaves, M. Baer, E. Schreiner, R. Stoll, and D. Marx, Chem. Phys. Chem. 22, 2759 (2008). 10.1002/cphc.200800474
11. J. R. McDaniel, D. J. Callahan, and A. Chilkoti, Adv. Drug Delivery Rev. 62, 1456 (2010). 10.1016/j.addr.2010.05.004
12. L. D. Muiznieks, A. S. Weiss, and F. W. Keeley, Biochem. Cell. Biol. 88, 239 (2001). 10.1139/O09-161
13. D. W. Urry, L. W. Mitchell, T. Ohnishi, and M. M. Long, J. Mol. Biol. 96, 101 (1975). 10.1016/0022-2836(75)90184-9
14. C. M. Venkatachalam and D. W. Urry, Macromolecules 14, 1225 (1981). 10.1021/ma50006a017
15. X. L. Yao and M. Hong, J. Am. Chem. Soc. 126, 4199 (2003). 10.1021/ja036686n
16. X. L. Yao, V. P. Conticello, and M. Hong, Magn. Reson. Chem. 42, 267 (2004). 10.1002/mrc.1330 (Pubitemid 38178096)
17. A. Perry, M. P. Stypa, B. K. Tenn, and K. K. Kumashiro, Biophys. J. 82, 1086 (2002). 10.1016/S0006-3495(02)75468-4
18. A. M. Tamburro and L. Debelle, Int. J. Biochem. Cell. Biol. 31, 261 (1999). 10.1016/S1357-2725(98)00098-3 (Pubitemid 29094776)
19. M. A. Lillie and J. M. Gosline, Int. J. Biol. Macromol. 30, 119 (2002). 10.1016/S0141-8130(02)00008-9 (Pubitemid 34242691)
20. M. Martino, A. Coviello, and A. M. Tamburro, Int. J. Biol. Macromol. 27, 59 (2000). 10.1016/S0141-8130(99)00118-X (Pubitemid 30110489)
21. F. Leli, A. M. Tamburro, V. Villani, P. Grimaldi, and V. Guantieri, Biopolymers 32, 159 (1992).
22. K. Ohgo, W. P. Niemczura, J. Ashida, M. Okonogi, T. Asakura, and K. K. Kumashiro, Biomacromolecules 7, 3306 (2006). 10.1021/bm0607168 (Pubitemid 46111783)
23. B. Li, D. O. V. Alonso, B. J. Bennion, and V. Daggett, J. Am. Chem. Soc. 123, 11991 (2001). 10.1021/ja010363e (Pubitemid 33135030)
24. B. Hess, C. Kutnzer, D. V. D. Spoel, and E. Lindahl, J. Chem. Theory Comput. 4, 435 (2008). 10.1021/ct700301q
25. W. L. Jorgensen and J. Tirado-Rives, J. Am. Chem. Soc. 110, 1657 (1988). 10.1021/ja00214a001
26. H. J. C. Berendsen, J. P. M. Postma, A. DiNola, and J. R. Haak, J. Chem. Phys. 81, 3684 (1984). 10.1063/1.448118
27. O. Teleman, B. Jonsson, and S. Engstrom, Mol. Phys. 60, 193 (1987). 10.1080/00268978700100141
28. K. J. Zimmerman, Comput. Chem. 12, 310 (1991). 10.1002/jcc.540120305
29. I. Andricioaei and M. Karplus, J. Chem. Phys. 115, 6289 (2001). 10.1063/1.1401821 (Pubitemid 33046603)
30. R. Rousseau, E. Schreiner, A. Kohlmeyer, and D. Marx, Biophys. J. 86, 1393 (2004). 10.1016/S0006-3495(04)74210-1
31. C. Sun, O. Mitchell, J. Huang, and G. Boutis, J. Phys. Chem. B 47, 13935 (2011). 10.1021/jp207607r
32. X. Ma, C. Sun, J. Huang, and G. Boutis, J. Phys. Chem. B 116, 555 (2012). 10.1021/jp208966k
33. G. Boutis, C. Renner, T. Isahkarov, T. Islam, L. Kannangara, P. Kaur, E. Mananga, A. Ntekim, Y. Rumala, and D. Wei, Biopolymers 87, 352 (2007). 10.1002/bip.20838
34. S. A. Harris and C. A. Laughton, J. Phys. Condens. Matter 19, 076103 (2007). 10.1088/0953-8984/19/7/076103 (Pubitemid 46485363)
35. P. J. Flory, Statistical Mechanics of Chain Molecules (Wiley, New York, 1969).
36. Z. R. Wasserman and F. R. Salemme, Biopolymers 29, 1613 (1990). 10.1002/bip.360291211
37. W. Lei, H. H. Tan, C. Jagadish, Q. J. Ren, J. Lu, and Z. H. Chen, App. Phys. Lett. 92, 223108 (2010). 10.1063/1.3522889
38. M. Siakavellas, A. G. Kontos, and E. Anastassakis, J. Appl. Phys. 84, 517 (1998). 10.1063/1.368055
39. J. Groenen, A. Mlayah, R. Carles, A. Ponchet, A. Le Corre, and S. Salaun, Appl. Phys. Lett. 69, 943 (1996). 10.1063/1.116951
40. J. Numata, M. Wan, and E. W. Knapp, Genome. Inform. Ser. 18, 192 (2007). 10.1142/9781860949920-0019
41. A. Valiaev, D. W. Lim, S. Schmidler, R. L. Clark, A. Chilkoti, and S. Zauscher, J. Am. Chem. Soc. 130, 10939 (2008). 10.1021/ja800502h