Molecular orientation distributions in protein films. 1. Cytochrome c adsorbed to substrates of variable surface chemistry

Journal of the American Chemical Society

Volumn 119, Issue 3, 1997, Pages 560-570

  Wood, Laurie L ^a   Cheng, Shih Song ^a   Edmiston, Paul L ^a   Saavedra, S Scott ^a  

^a University of Arizona ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C;

ARTICLE; ENZYME IMMOBILIZATION; ENZYME STRUCTURE; MOLECULAR DYNAMICS; SURFACE PROPERTY; THERMODYNAMICS;

EID: 1842365512     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja962366a     Document Type: Article

References (44)

1. Taylor, R. F. Protein Immobilization. Fundamentals and Applications; Marcel Dekker: New York, 1991.
2. Ahlers, M.; Müller, W.; Reichert, A.; Ringsdorf, H.; Venzmer, J. Angew. Chem., Int. Ed. Engl. 1990, 29, 1269-1285.
3. Swalen, J. D.; Allara, D. L.; Andrade, J. D.; Chandross, E. A.; Garoff, S.; Israelchvili, J.; McCarthy, T. J.; Murray, R.; Pease, R. F.; Rabolt, J. F.; Wynne, K. J.; Yu, H. Langmuir 1987, 3, 932-950.
4. Lin, J. N.; Andrade, J. D.; Chang, I.-N. J. Immunol. Methods 1989, 125, 67-77.
5. Blankenburg, R.; Meller, P.; Ringsdorf, H.; Salesse, C. Biochemistry 1989, 28, 8214-8221.
6. Darst, S. A.; Ahlers, M.; Meller, P. H.; Kubalek, E. W.; Blankenburg, R.; Ribi, H. O.; H. Ringsdorf; Kornberg, R. D. Biophys. J. 1991, 59, 387-396.
7. See for example: (a) Herron, J. N.; Müller, W.; Paudler, M.; Riegler, H.; Ringsdorf, H.; Suci, P. A. Langmuir 1992, 8, 1413-1416. (b) Fischer, B.; Heyn, S. P.; Egger, M.; Gaub, H. E. Langmuir 1993, 9, 136-140.
8. See for example: (a) Herron, J. N.; Müller, W.; Paudler, M.; Riegler, H.; Ringsdorf, H.; Suci, P. A. Langmuir 1992, 8, 1413-1416. (b) Fischer, B.; Heyn, S. P.; Egger, M.; Gaub, H. E. Langmuir 1993, 9, 136-140.
9. Spinke, J.; Liley, M.; Guder, H.-J.; Angermaier, L.; Knoll, W. Langmuir 1993, 9, 1821-1825.
10. Müller, W.; Ringsdorf, H.; Rump, E.; Wildburg, G.; Zhang, X.; Angermaier, L.; Knoll, W.; Liley, M.; Spinke, J. Science 1993, 262, 1706-1708.
11. See for example: (a) Koyama, K.; Yamaguchi, N.; Miyasaka, T. Science 1994, 265, 762-765.
12. (b) Mrksich, M.; Grunwell, J. R.; Whitesides, G. M. J. Am. Chem. Soc. 1995, 117, 12009-12010.
13. (a) Duschl, C.; Liley, M.; Corradin, G.; Vogel, H. Biophys. J. 1994, 67, 1229-1237.
14. (b) Thompson, N. L.; Poglitsch, C. L.; Timbs, M. M.; Pisarschick, M. L. Acc. Chem. Res. 1993, 26, 6567-573.
15. Chang, I.-N.; Herron, J. N. Langmuir 1995, 11, 2083-2089.
16. Song, S.; Clark, R. A.; Bowden, E. F.; Tarlov, M. J. J. Phys. Chem. 1993, 97, 6564-6572.
17. Prokop, L. A.; Strongin, R. M.; Smith, A. B., III; Blasie, J. K.; Peticolas, L. J.; Bean, J. C. Biophys. J. 1995, 70, 2131-2143.
18. Shnek, D. R.; Pack, D. W.; Sasaki, D. Y.; Arnold, F. H. Langmuir 1994, 10, 2382-2388.
19. (a) Stayton, P. S.; Ollinger, J. M.; Jiang, M.; Bohn, P. W.; Sligar, S. G. J. Am. Chem. Soc. 1992, 114, 9298-9299.
20. (b) Hong, H.-G.; Jiang, M.; Sligar, S. G.; Bohn, P. W. Langmuir 1994, 10, 153-158.
21. (a) Amador, S. M.; Pachence, J. M.; Fischetti, R.; McCauley, J. P., Jr.; Smith, A. B., III; Blasie, J. K. Langmuir 1993, 9, 812-817.
22. (b) Chupa, J. A.; McCauley, J. P., Jr.; Strongin, R. M.; Smith, A. B., III; Blasie, J. K.; Peticolas, L. J.; Bean, J. C. Biophys. J. 1994, 67, 336-348.
23. (a) Walker, D. S.; Hellinga, H. W; Saavedra, S. S.; Reichert, W. M. J. Phys. Chem. 1993, 97, 10217-10222.
24. (b) Lee, J. E; Saavedra, S. S. in Proteins at Interfaces II; Horbett, T. A., Brash, J. L., Eds.; ACS Symposium Series 602; American Chemical Society: Washington DC, 1995; pp 269-279.
25. (c) Lee, J. E; Saavedra, S. S. Langmuir 1996, 12, 4025-4032.
26. Fraaije, J. G. E. M.; Kleijn, J. M.; van der Graaf, M.; Dijt, J. C. Biophys. J. 1990, 57, 965-975.
27. (a) Bos, M. A.; Kleijn, J. M. Biophys. J. 1995, 68, 2573-2579.
28. (b) Bos, M. A.; Kleijn, J. M. Biophys. J. 1995, 68, 2566-2572.
29. Timbs, M. M.; Thompson, N. L. Biophys. J. 1990, 58, 413-428.
30. Edmiston, P. L.; Wood, L. L.; Lee, J. E.; Saavedra, S. S. J. Phys. Chem. 1996, 100, 775-784.
31. Edmiston, P. L.; Lee, J. E.; Cheng, S.-S.; Saavedra, S. S. J. Am. Chem. Soc. 1997, 119, 560.
32. Walker, D. S.; Reichert, W. M.; Berry, C. J. Appl. Spectrosc. 1992, 46, 1437-1441.
33. SAMSA Fluorescein (A-685). Technical bulletin; available from Molecular Probes, Eugene, OR.
34. Riddles, P. W.; Blakeley, R. P.; Zerner, B. Methods Enzymol. 1983, 91, 49-60.
35. Vanderkooi, J. M.; Adar, F.; Erecinska, M. Eur. J. Biochem. 1976, 64, 381-387.
36. Bhatia, S. K.; Shriver-Lake, L. C.; Prior, K. J.; Georger, J. H.; Calvert, J. M.; Bredehorst, R.; Ligler, F. S. Anal. Biochem. 1989, 178, 408-413.
37. Brayer, G. D.; Murphy, M. E. Cytochrome c: A Multidisciplinary Approach; Scott, R. A., Mauk, A. G., Eds.; University Science Books: Sausalito, CA, 1996; Chapter 3 and references therein.
38. Moench, S. J.; Satterlee, J. D. J. Biol. Chem. 1989, 264, 9923-9931.
39. σ.
40. See for example: Chen, M; Cassidy, R. M. J. Chromatogr. 1992, 602, 227-234.
41. The tendency of proteins to undergo conformational changes upon adsorption to an interface is well recognized, but poorly understood from a fundamental perspective. See: (a) Andrade, J. D.; Hlady, V. Adv. Polym. Sci. 1986, 79, 1-63. (b) Haynes, C. A.; Norde, W. Colloids Surf. B: Biointerfaces 1994, 2, 517-566. (c) Brash, J. L.; Horbett, T. A. In Proteins at Interfaces II; Horbett, T. A., Brash, J. L., Eds.; ACS Symposium Series 602; American Chemical Society: Washington, DC, 1995; pp 1-23 and references therein.
42. The tendency of proteins to undergo conformational changes upon adsorption to an interface is well recognized, but poorly understood from a fundamental perspective. See: (a) Andrade, J. D.; Hlady, V. Adv. Polym. Sci. 1986, 79, 1-63. (b) Haynes, C. A.; Norde, W. Colloids Surf. B: Biointerfaces 1994, 2, 517-566. (c) Brash, J. L.; Horbett, T. A. In Proteins at Interfaces II; Horbett, T. A., Brash, J. L., Eds.; ACS Symposium Series 602; American Chemical Society: Washington, DC, 1995; pp 1-23 and references therein.
43. The tendency of proteins to undergo conformational changes upon adsorption to an interface is well recognized, but poorly understood from a fundamental perspective. See: (a) Andrade, J. D.; Hlady, V. Adv. Polym. Sci. 1986, 79, 1-63. (b) Haynes, C. A.; Norde, W. Colloids Surf. B: Biointerfaces 1994, 2, 517-566. (c) Brash, J. L.; Horbett, T. A. In Proteins at Interfaces II; Horbett, T. A., Brash, J. L., Eds.; ACS Symposium Series 602; American Chemical Society: Washington, DC, 1995; pp 1-23 and references therein.
44. Tobias, D. J.; Mar, W.; Blasie, J. K.; Klein, M. L. Biophys. J., in press.