Effects of tethering a multistate folding protein to a surface

Journal of Chemical Physics

Volumn 134, Issue 18, 2011, Pages

  Wei, Shuai ^a   Knotts, Thomas A ^a  

^a Department of Electrical and Computer Engineering   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PHYSICAL CHEMISTRY;

EXPERIMENTAL TECHNIQUES; FOLDED STATE; FOLDING MECHANISM; MOLECULAR CONFIGURATIONS; MOLECULAR SIMULATIONS; PROTEIN ARRAYS; RATIONAL DESIGN; STABLE STATE;

PROTEINS;

LYSOZYME;

ARTICLE; BACTERIOPHAGE T4; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE PROPERTY;

BACTERIOPHAGE T4; MODELS, MOLECULAR; MURAMIDASE; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE PROPERTIES;

EID: 80052304943     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3589863     Document Type: Article

References (66)

1. P. Jonkheijm, D. Weinrich, H. Schroeder, C. M. Niemeyer, and H. Waldmann, Angew. Chem., Int. Ed. 47, 9618 (2008). 10.1002/anie.200801711
2. U. Bilitewski, Anal. Chim. Acta 568, 232 (2006). 10.1016/j.aca.2005.12.073
3. H. Zhu and M. Snyder, Curr. Opin. Chem. Biol. 7, 55 (2003). 10.1016/S1367-5931(02)00005-4
4. M. Uttamchandani and S. Q. Yao, Curr. Pharm. Des. 14, 2428 (2008). 10.2174/138161208785777450
5. M. Cretich, F. Damina, G. Pirria, and M. Chiari, Biomol. Eng. 23, 77 (2006). 10.1016/j.bioeng.2006.02.001
6. N. Adam, The Physics and Chemistry of Surfaces (Oxford University Press, London, 1941).
7. D. Cheesman and J. Davies, Adv. Protein Chem. 9, 439 (1954). 10.1016/S0065-3233(08)60211-9
8. A. Rothen, Adv. Protein Chem. 3, 123 (1947). 10.1016/S0065-3233(08)60078-9
9. A. P. L. Brun, S. A. Holt, D. S. Shah, C. F. Majkrzak, and J. H. Lakey, Eur. Biophys. J. 37, 639 (2008). 10.1007/s00249-008-0291-2
10. K. K. Chittur, Biomaterials 19, 357 (1998). 10.1016/S0142-9612(97)00223-8
11. F. Evers, C. Reichhart, R. Steitz, M. Tolan, and C. Czeslik, Phys. Chem. Chem. Phys. 12, 4375 (2010). 10.1039/b925134k
12. S. Aoyagi and M. D. Kudo, Biosens. Bioelectron. 20, 1626 (2005). 10.1016/j.bios.2004.06.040
13. S. Aoyagi, Surf. Interface Anal. 41, 136 (2009). 10.1002/sia.2989
14. R. Chatterjee, Appl. Surf. Sci. 231, 437 (2004). 10.1016/j.apsusc.2004.03.164
15. B. Hagenhoff, Biosens. Bioelectron. 10, 885 (1995). 10.1016/0956-5663(95)99226-B
16. Y.-P. Kim, M.-Y. Hong, H. K. Shon, D. W. Moon, H.-S. Kim, and T. G. Lee, Appl. Surf. Sci. 252, 6801 (2006). 10.1016/j.apsusc.2006.02.203
17. J.-W. Park, H. Min, Y.-P. Kim, H. K. Shon, J. Kim, D. W. Moon, and T. G. Lee, Surf. Interface Anal. 41, 694 (2009). 10.1002/sia.3049
18. F. Liu, M. Dubey, H. Takahashi, D. G. Castner, and D. W. Grainger, Anal. Chem. 82, 2947 (2010). 10.1021/ac902964q
19. H. Wang, D. G. Castner, B. D. Ratner, and S. Jiang, Langmuir 20, 1877 (2004). 10.1021/la035376f
20. M. Agashe, V. Raut, S. J. Stuart, and R. A. Latour, Langmuir 21, 1103 (2005). 10.1021/la0478346
21. K. Battle, E. A. Salter, R. W. Edmunds, and A. Wierzbicki, J. Cryst. Growth 312, 1257 (2010). 10.1016/j.jcrysgro.2009.12.038
22. J. C. Hower, Y. He, M. T. Bernards, and S. Jiang, J. Chem. Phys. 125, 214704 (2006). 10.1063/1.2397681
23. R. A. Latour, Biointerphases 3, FC2 (2008). 10.1116/1.2965132
24. L. Li, S. Chen, J. Zheng, B. D. Ratner, and S. Jiang, J. Phys. Chem. B 109, 2934 (2005). 10.1021/jp0473321
25. G. Raffaini and F. Ganazzoli, Langmuir 19, 3403 (2003). 10.1021/la026853h
26. G. Raffaini and F. Ganazzoli, Langmuir 26, 5679 (2010). 10.1021/la903769c
27. V. P. Raut, M. A. Agashe, S. J. Stuart, and R. A. Latour, Langmuir 22, 2402 (2006). 10.1021/la053501c
28. Y. Sun, W. J. Welsh, and R. A. Latour, Langmuir 21, 5616 (2005). 10.1021/la046932o
29. F. Wang, S. J. Stuart, and R. A. Latour, BioInterphases 3, 9 (2008). 10.1116/1.2840054
30. Y. Xie, J. Zhou, and S. Jiang, J. Chem. Phys. 132, 065101 (2010). 10.1063/1.3305244
31. L. Zhang and Y. Sun, Biochem. Eng. J. 48, 408 (2010). 10.1016/j.bej.2009.12.003
32. G. Collier, N. A. Vellore, R. A. Latour, and S. J. Stuart, BioInterphases 4, 57 (2009). 10.1116/1.3266417
33. N. A. Vellore, J. A. Yancey, G. Collier, R. A. Latour, and S. J. Stuart, Langmuir 26, 7396 (2010). 10.1021/la904415d
34. T. A. Knotts IV, N. Rathore, and J. J. de Pablo, Proteins 61, 385 (2005). 10.1002/prot.20581
35. M. Friedel, A. Baumketner, and J. Shea, Proc. Natl. Acad. Sci. U.S.A. 103, 8396 (2006). 10.1073/pnas.0601210103
36. M. Friedel, A. Baumketner, and J.-E. Shea, J. Chem. Phys. 126, 095101 (2007). 10.1063/1.2464114
37. T. A. Knotts IV, N. Rathore, and J. J. de Pablo, Biophys. J. 94, 4473 (2008). 10.1529/biophysj.107.123158
38. Z. Zhuang, A. I. Jewett, P. Soto, and J.-E. Shea, Phys. Biol. 6, 015004 (2009). 10.1088/1478-3975/6/1/015004
39. S. Wei and T. A. Knotts IV, J. Chem. Phys. 133, 115102 (2010). 10.1063/1.3479039
40. H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat, H. Weissig, I. N. Shindyalov, and P. E. Bourne, Nucleic Acids Res. 22, 235 (2000). 10.1093/nar/28.1.235
41. A. L. Cuff, I. Sillitoe, T. Lewis, O. C. Redfern, R. Garratt, J. Thornton, and C. A. Orengo, Nucleic Acids Res. 37, D310 (2009). 10.1093/nar/gkn877
42. C. Orengo, A. Michie, D. Jones, M. Swindells, and J. Thornton, Structure (London) 5, 1093 (1997). 10.1016/S0969-2126(97)00260-8
43. D. Frishman and P. Argos, Proteins 23, 566 (1995). 10.1002/prot.340230412
44. W. Humphrey, A. Dalke, and K. Schulten, J. Mol. Graphics 14, 33 (1996). 10.1016/0263-7855(96)00018-5
45. C. Tanford, K. C. Aune, and A. Ikai, J. Mol. Biol. 73, 185 (1973). 10.1016/0022-2836(73)90322-7
46. K. Kuwajima, Y. Hiraoka, M. Ikeguchi, and S. Sugai, Biochemistry 24, 874 (1985). 10.1021/bi00325a010
47. A. Chaffotte, Y. Guillou, and M. Goldberg, Biochemistry 31, 9694 (1992). 10.1021/bi00155a024
48. S. Radford, C. Dobson, and P. Evans, Nature (London) 358, 302 (1992). 10.1038/358302a0
49. T. Kiefhaber, Proc. Natl. Acad. Sci. U.S.A. 92, 9029 (1995). 10.1073/pnas.92.1.9
50. M. Parker, J. Spence, and A. Clarke, J. Mol. Biol. 253, 771 (1995). 10.1006/jmbi.1995.0590
51. G. Wildegger and T. Kiefhaber, J. Mol. Biol. 270, 294 (1997). 10.1006/jmbi.1997.1030
52. A. Miranker, C. Robinson, S. Randord, R. Aplin, and C. Dobson, Science 262, 896 (1993). 10.1126/science.8235611
53. J. Karanicolas and C. L. Brooks III, J. Mol. Biol. 334, 309 (2003). 10.1016/j.jmb.2003.09.047
54. J. Karanicolas and C. L. Brooks III, Proc. Natl. Acad. Sci. U.S.A. 100, 3954 (2003). 10.1073/pnas.0731771100
55. J. Karanicolas and C. L. Brooks III, Proc. Natl. Acad. Sci. U.S.A. 101, 3432 (2004). 10.1073/pnas.0304825101
56. R. D. Hills, Jr. and C. L. Brooks III, Int. J. Mol. Sci. 10, 889 (2009). 10.3390/ijms10030889
57. T. J. Schmitt, J. E. Clark, and T. A. Knotts IV, J. Chem. Phys. 131, 235101 (2009). 10.1063/1.3270167
58. See http://mmtsb.org/ for Go Model Builder.
59. Y. Sugita and Y. Okamoto, Chem. Phys. Lett. 314, 141 (1999). 10.1016/S0009-2614(99)01123-9
60. Y. Sugita, A. Kitao, and Y. Okamoto, J. Chem. Phys. 113, 6042 (2000). 10.1063/1.1308516
61. S. Nosé, J. Chem. Phys. 81, 511 (1984). 10.1063/1.447334
62. W. G. Hoover, Phys. Rev. A 31, 1695 (1985). 10.1103/PhysRevA.31.1695
63. S. Nosé, J. Phys.: Condens. Matter 2, SA115 (1990). 10.1111/j.1525-1594.1990.tb02955.x
64. S. Kumar, D. Bouzida, R. H. Swendsen, P. A. Kollman, and J. M. Rosenberg, J. Comput. Chem. 13, 1011 (1992). 10.1002/jcc.540130812
65. P. Peluso, D. S. Wilson, D. Do, H. Tran, M. Venkatasubbaiah, D. Quincy, B. Heidecker, K. Poindexter, N. Tolani, M. Phelan, K. Witte, L. S. Jung, P. Wagner, and S. Nock, Anal. Biochem. 312, 113 (2003). 10.1016/S0003-2697(02)00442-6
66. R. Wacker, H. Schroder, and C. Niemeyer, Anal. Biochem. 330, 281 (2004). 10.1016/j.ab.2004.03.017