Power-law dependence of the melting temperature of ubiquitin on the volume fraction of macromolecular crowders

Journal of Chemical Physics

Volumn 134, Issue 9, 2011, Pages

  Waegele, Matthias M ^a   Gai, Feng ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MACROMOLECULAR CROWDING; MELTING TEMPERATURES; POLYPEPTIDE CHAIN; POWER-LAW DEPENDENCES; THEORETICAL TREATMENTS; UBIQUITIN;

GLUCOSE; MACROMOLECULES; METAL MELTING; PHASE TRANSITIONS; TITRATION;

MELTING POINT;

UBIQUITIN;

ARTICLE; CHEMISTRY; INFRARED SPECTROSCOPY; MACROMOLECULE; PROTEIN FOLDING; THERMODYNAMICS; TRANSITION TEMPERATURE;

MACROMOLECULAR SUBSTANCES; PROTEIN FOLDING; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; TRANSITION TEMPERATURE; UBIQUITIN;

EID: 79952526173     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3556671     Document Type: Article

References (60)

1. H.-X. Zhou, G. Rivas, and A. P. Minton, Annu. Rev. Biophys. 37, 375 (2008). 10.1146/annurev.biophys.37.032807.125817
2. J. A. Dix and A. S. Verkman, Annu. Rev. Biophys. 37, 247 (2008). 10.1146/annurev.biophys.37.032807.125824
3. K. Richter, M. Nessling, and P. Lichter, Biochim. Biophys. Acta 1738, 2100 (2008). 10.1016/j.bbamcr.2008.07.017
4. B. van den Berg, R. Wain, C. M. Dobson, and R. J. Ellis, EMBO J. 18, 6927 (2000). 10.1093/emboj/18.24.6927
5. Y. X. Qu and D. W. Bolen, Biophys. Chem. 101, 155 (2002). 10.1016/S0301-4622(02)00148-5 (Pubitemid 35462044)
6. K. Sasahara, P. McPhie, and A. P. Minton, J. Mol. Biol. 326, 1227 (2003). 10.1016/S0022-2836(02)01443-2 (Pubitemid 36263394)
7. N. Tokuriki, M. Kinjo, S. Negi, M. Hoshino, M. Y. Goto, I. Urabe, and T. Yomo, Protein Sci. 13, 125 (2004). 10.1110/ps.03288104 (Pubitemid 38021147)
8. X. J. Ai, Z. Zhou, Y. W. Bai, and W.-Y. Choy, J. Am. Chem. Soc. 128, 3916 (2006). 10.1021/ja057832n
9. G. Ping, G. Yang, and J.-M. Yuan, Polymer 47, 2564 (2006). 10.1016/j.polymer.2005.12.085
10. L. Stagg, S.-Q. Zhang, M. S. Cheung, and P. Wittung-Stafshede, Proc. Natl. Acad. Sci. USA 104, 18976 (2007). 10.1073/pnas.0705127104
11. A. Roberts and S. E. Jackson, Biophys. Chem. 128, 140 (2007). 10.1016/j.bpc.2007.03.011 (Pubitemid 46844853)
12. J. M. Yuan, C.-L. Chyan, H.-X. Zhou, T. Y. Chung, H. Peng, G. Ping, and G. Yang, Protein Sci. 17, 2156 (2008). 10.1110/ps.037325.108
13. L. M. Charlton, C. O. Barnes, C. G. Li, J. Orans, G. B. Young, and G. J. Pielak, J. Am. Chem. Soc. 130, 6826 (2008). 10.1021/ja8005995 (Pubitemid 351748420)
14. J. Batra, K. Xu, and H.-X. Zhou, Proteins 77, 133 (2009). 10.1002/prot.22425
15. J. Batra, K. Xu, S. Qin, and H.-X. Zhou, Biophys. J. 97, 906 (2009). 10.1016/j.bpj.2009.05.032
16. Y. Phillip, E. Sherman, G. Haran, and G. Schreiber, Biophys. J. 97, 875 (2009). 10.1016/j.bpj.2009.05.026
17. S. Mukherjee, M. M. Waegele, P. Chowdhury, L. Guo, and F. Gai, J. Mol. Biol. 393, 227 (2009). 10.1016/j.jmb.2009.08.016
18. D. Homouz, L. Stagg, P. Wittung-Stafshede, and M. S. Cheung, Biophys. J. 96, 671 (2009). 10.1016/j.bpj.2008.10.014
19. J. Hong and L. M. Gierasch, J. Am. Chem. Soc. 132, 10445 (2010). 10.1021/ja103166y
20. A. Miklos, C. Li, N. G. Sharaf, and G. J. Pielak, Biochemistry 49, 6984 (2010). 10.1021/bi100727y
21. A. Christiansen, Q. Wang, A. Samiotakis, M. S. Cheung, and P. Wittung-Stafshede, Biochemistry 49, 6519 (2010). 10.1021/bi100578x
22. A. R. Kinjo and S. Takada, Phys. Rev. E 66, 031911 (2002). 10.1103/PhysRevE.66.031911 (Pubitemid 40606415)
23. M. S. Cheung, D. Klimov, and D. Thirumalai, Proc. Natl. Acad. Sci. USA 102, 4753 (2005). 10.1073/pnas.0409630102 (Pubitemid 40471526)
24. D. D. Minh, C. E. Chang, J. Trylska, V. Tozzini, and J. A. McCammon, J. Am. Chem. Soc. 128, 6006 (2006). 10.1021/ja060483s
25. G. Wieczorek and P. Zielenkiewicz, Biophys. J. 95, 5030 (2008). 10.1529/biophysj.108.136291
26. D. Pincus and D. Thirumalai, J. Phys. Chem. B 113, 359 (2009). 10.1021/jp807755b
27. S. Qin and H. X. Zhou, Biophys. J. 97, 12 (2009). 10.1016/j.bpj.2009.03. 066
28. D. Tsao and N. V. Dokholyan, Phys. Chem. Chem. Phys. 12, 3491 (2010). 10.1039/b924236h
29. J. Mittal and R. B. Best, Biophys. J. 98, 315 (2010). 10.1016/j.bpj.2009.10.009
30. A. P. Minton, Biopolymers 20, 2093 (1981). 10.1002/bip.1981.360201006
31. H.-Y. Zhou and C. K. Hall, Biopolymers 38, 273 (1996). 10.1002/(SICI)1097-0282(199602)38:2273::AID-BIP113.3.CO;2-7
32. A. P. Minton, Biophys. J. 78, 101 (2000). 10.1016/S0006-3495(00)76576-3
33. H.-X. Zhou, Proteins 72, 1109 (2008). 10.1002/prot.22111
34. M. B. Gee and P. E. Smith, J. Chem. Phys. 131, 165101 (2009). 10.1063/1.3253299
35. S. Qin and H.-X. Zhou, Phys. Rev. E 81, 031919 (2010). 10.1103/PhysRevE.81.031919
36. A. H. Elcock, Curr. Opin. Struct. Biol. 20, 196 (2010). 10.1016/j.sbi.2010.01.008
37. P.-G. De Gennes, Scaling Concepts in Polymer Physics (Cornell University Press, Ithaca, NY, 1979).
38. T. Sakaue and E. Raphal, Macromolecules 39, 2621 (2006). 10.1021/ma0514424
39. N. Rathore, T. A. Knotts IV, and J. J. de Pablo, Biophys. J. 90, 1767 (2006). 10.1529/biophysj.105.071076
40. J. Mittal and R. B. Best, Proc. Natl. Acad. Sci. USA 105, 20233 (2008). 10.1073/pnas.0807742105
41. F. Takagi, N. Koga, and S. Takada, Proc. Natl. Acad. Sci. USA 100, 11367 (2003). 10.1073/pnas.1831920100 (Pubitemid 37205941)
42. W. Wang, W.-X. Xu, Y. Levy, E. Trizac, and P. G. Wolynes, Proc. Natl. Acad. Sci. USA 106, 5517 (2009). 10.1073/pnas.0809649106
43. M. R. Shaw and D. Thirumalai, Phys. Rev. A 44, R4797 (1991). 10.1103/PhysRevA.44.R4797
44. T. Biben and J. P. Hansen, Phys. Rev. Lett. 66, 2215 (1991). 10.1103/PhysRevLett.66.2215
45. S. Vijay-Kumar, C. E. Bugg, and W. J. Cook, J. Mol. Biol. 194, 531 (1987). 10.1016/0022-2836(87)90679-6
46. S. Khorasanizadeh, I. D. Peters, T. R. Butt, and H. Roder, Biochemistry 32, 7054 (1993). 10.1021/bi00078a034
47. P. L. Wintrode, G. I. Makhatadze, and P. L. Privalov, Proteins 18, 246 (1994). 10.1002/prot.340180305
48. B. A. Krantz and T. R. Sosnick, Biochemsitry 39, 11696 (2000). 10.1021/bi000792+
49. S. C. Colley, I. P. Clark, S. R. Griffiths-Jones, M. W. George, and M. S. Searle, Chem. Commun. 16, 1493 (2000). 10.1039/b003768k
50. H. S. Chung, M. Khalil, A. W. Smith, Z. Ganim, and A. Tokmakoff, Proc. Natl. Acad. Sci. USA 102, 612 (2005). 10.1073/pnas.0408646102 (Pubitemid 40282713)
51. H. S. Chung and A. Tokmakoff, Proteins 72, 474 (2008). 10.1002/prot.22043 (Pubitemid 351809181)
52. Y. Xu, R. Oyola, and F. Gai, J. Am. Chem. Soc. 125, 15388 (2003). 10.1021/ja037053b (Pubitemid 37532180)
53. E. R. Henry and J. Hofrichter, Methods Enzymol. 210, 129 (1992). 10.1016/0076-6879(92)10010-B
54. S. T. R. Walsh, R. P. Cheng, W. W. Wright, D. O. V. Alonso, V. Daggett, J. M. Vanderkooi, and W. F. DeGrado, Protein Sci. 12, 520 (2003). 10.1110/ps.0223003 (Pubitemid 36244922)
55. S. Mukherjee, P. Chowdhury, and F. Gai, J. Phys. Chem. B 111, 4596 (2007). 10.1021/jp0689060 (Pubitemid 46787657)
56. B. Efron, Can. J. Stat., 9, 139 (1981). 10.2307/3314608
57. J. K. Armstrong, R. B. Wenby, H. J. Meiselman, and T. C. Fisher, Biophys. J. 87, 4259 (2004). 10.1529/biophysj.104.047746 (Pubitemid 39602928)
58. A. G. Ogston and B. N. Preston, Biochem. J. 183, 1 (1979).
59. J. R. Wenner and V. A. Bloomfield, Biophys. J. 77, 3234 (1999). 10.1016/S0006-3495(99)77154-7
60. Z. Liu, W. Weng, R. M. Bookchin, V. L. Lew, and F. A. Ferrone, Biophys. J. 94, 3629 (2008). 10.1529/biophysj.107.117465