Arginine methylation in a β-hairpin peptide: Implications for Arg-π interactions, ΔCp°, and the cold denatured state

Journal of the American Chemical Society

Volumn 128, Issue 39, 2006, Pages 12735-12742

  Hughes, Robert M ^a   Waters, Marcey L ^a  

^a University of North Carolina at Chapel Hill   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE METHYLATION; DENATURED STATES; GUANIDINIUM MOIETIES; HYDROPHOBIC INTERACTIONS;

ENTHALPY; METHANE; POSITIVE IONS; SPECIFIC HEAT; STRUCTURE (COMPOSITION); THERMODYNAMICS;

AMINO ACIDS;

ARGININE; CATION; GUANIDINE; INDOLE DERIVATIVE; TRYPTOPHAN;

ARTICLE; BETA SHEET; COLD; ENTHALPY; ENTROPY; FORCE; HYDROPHOBICITY; METHYLATION; MOLECULAR INTERACTION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SURFACE PROPERTY; TEMPERATURE DEPENDENCE; THERMODYNAMICS;

AMINO ACID SEQUENCE; ARGININE; COLD; ELECTROSTATICS; LYSINE; METHYLATION; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; TRYPTOPHAN;

EID: 33749535702     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja061656g     Document Type: Article

References (52)

1. (a) McBride, A. E.; Silver, P. A. Cell 2001, 106, 5-8.
2. (b) Lee, D. Y.; Teyssier, C.; Strahl, B. D.; Stallcup, M. R. Endocr. Rev. 2005, 26, 147-170.
3. (c) Bedford, M. T.; Richard. S. Mol. Cell 2005, 18, 263-272.
4. Cosgrove, M. S.; Boeke, J. D.; Wolberger, C. Nat. Struct. Mol. Biol. 2004, 11, 1037-1043.
5. Cote, J.; Richard, S. J. Biol. Chem. 2005, 280, 28476-28483.
6. Flanagan, J. F., IV; Mi, L.-Z.; Chruszcz, M.; Cymborowski, M.; Clines, K. L.; Kim, Y.; Minor, W.; Rastinejad, F.; Khorasanizadeh, S. Nature 2005, 438, 1181-1185.
7. de Vos, A. M.; Ultsch, M.; Kossiakoff, A. A. Science 1992, 255, 306-312.
8. (a) Burley, S. K.; Petsko, G. A. FEBS Lett. 1986, 203, 139-143.
9. (b) Flocco, M. M.; Mowbray, S. L. J. Mol. Biol. 1994, 235, 709-717.
10. (c) Mitchell, J. B. O.; Nandi, C. L.; McDonald, I. K.; Thornton, J. M.; Price, S. L. J. Mol. Biol. 1994, 239, 315-331.
11. (d) Gallivan, J. P.; Dougherty, D. A. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 9459-9464.
12. (a) Broccheiri, L.; Karlin, S. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 9297-9301.
13. (b) Karlin, S.; Zuker, M.; Brocchieri, L. J. Mol. Biol. 1994, 239, 227-248.
14. (a) Wei, Y.; Horng, J.; Vendel, A. C.; Raleigh, D. P.; Lumb, K. J. Biochemistry 2003, 42, 7044-7049.
15. (b) Luque, L. E.; Grape, K. P.; Junker, M. Biochemistry 2002, 41, 13663-13671.
16. (c) St. Charles, R.; Padmanabhan, K.; Arni, R. V.; Padmanabhan, K. P.; Tulinsky, A. Protein Sci. 2000, 9, 265-272.
17. (a) Cumpstey, I.; Sundin, A.; Leffler, H.; Nilsson, U. J. Angew. Chem., Int. Ed. 2005, 44, 5110-5112.
18. (b) Woods, A. S. J. Proteome Res. 2004, 3, 478-484.
19. (c) Pellequer, J.; Zhao, B.; Kao, H.; Bell, C. W.; Li, K.; Li, Q. X.; Karu, A. E.; Roberts, V. A. J. Mol. Biol. 2000, 302, 691-699.
20. Crowley, R. B.; Golovin, A. Proteins: Struct., Funct. Bioinf. 2005, 59, 231 -239.
21. (a) Kumaki, Y.; Nitta, K.; Hikichi, K.; Matsumoto, T.; Matsushima, N. J. Biochemistry 2004, 136, 29-37.
22. (b) Wintjens, R.; Lievin, J.; Rooman, M.; Buisine, E. J. Mol. Biol. 2000, 302, 395-410.
23. Shi, Z. S.; Olson, C. A.; Kallenbach, N. R. J. Am. Chem. Soc. 2002, 124, 3284-3291.
24. Tatko, C. D.; Waters, M. L. Protein Sci. 2003, 12, 2443-245Z
25. (a) Ngola, S. M.; Kearney, P. C.; Mecozzi, S.; Russell, K.; Dougherty, D. A. J. Am. Chem. Soc. 1999, 121, 1192-1201.
26. (b) Rensing, S.; Arendt, M.; Springer, A.; Grawe, T.; Schrader, T. J. Org. Chem. 2001, 66, 5814-5821.
27. (c) Thompson, S. E.; Smithrud, D. B. J. Am. Chem. Soc. 2002, 124, 442-449.
28. (d) Nishihara, M.; Perret, F.; Takeuchi, T.; Futaki, S.; Lazar, A. N.; Coleman, A. W.; Sakai, N.; Matile, S. Org. Biomol. Chem. 2005, 3, 1659-1669.
29. Tatko, C. D.; Waters, M. L. J. Am. Chem. Soc. 2004, 126, 2028-2034.
30. Hughes, R. M.; Waters, M. L. J. Am. Chem. Soc. 2005, 127, 6518-6519.
31. Maynard, A. J.; Sharman, G. J.; Searle, M. S. J. Am. Chem. Soc. 1998, 120, 1996-2007.
32. Griffith-Jones, S. R.; Maynard, A. J.; Searle, M. S. J. Mol. Biol. 1999, 292, 1051-1069.
33. Dyer, R. B.; Maness, S. J.; Franzen, S.; Fesinmeyer, R. M.; Olsen, K. A.; Andersen, N. H. Biochemistry 2005, 44, 10406-10415.
34. Prabhu, N. V.; Sharp, K. A. Annu. Rev. Phys. Chem. 2005, 56, 521-48.
35. Atkins, P. W. Phvsical Chemistry, 6th ed.; Oxford University Press: Oxford. U.K., 1998; Chapter 2.
36. (a) Shoemaker, D. P.; Garland, C. W.; Nibler, J. W. Experiments in Physical Chemistry, 4th ed.; McGraw-Hill: New York, 1981; pp 727-730.
37. (b) Moore, D. S. The Basic Principles of Statistics; W. H. Freeman and Co.: New York, 1995; pp 630-633.
38. (c) Foster, J. E.; Holmes, S. F.; Erie, D. A. Cell 2001, 106, 243-252.
39. For example, on the central carbon of the guanidinium group, the charge decreases from = +1.16 for Arg to +0.54 for DMAs and +0.76 for DMAa, as determined from the Merz-Kollman atomic charges. See Supporting Information.
40. (a) Lachner, M.; Jenuwein, T. Curr. Opin. Cell. Biol. 2002, 14, 286-298.
41. (b) Lindroth, A. M.; Shultis, D.; Jasencakova, Z.; Fuchs, J.; Johnson, L.; Schubert, D.; Patnaik, D; Pradhan, S.; Goodrich, J.; Schubert, I.; Jenuwein, T.; Khorasanizadeh, S.; Jacobsen, S. E. Embo J. 2004, 23, 4286-4296.
42. (c) Fischle, W.; Wang, Y. M.; Jacobs, S. A.; Kim, Y. C.; Allis, C. D.; Khorasanizadeh, S. Genes Dev. 2003, 17, 1870-1881.
43. (d) Jacobs, S. A.; Khorasanizadeh, S. Science 2002, 295, 2080-2083.
44. p° obtained for WKMe3 with eq 1 differ slightly from those reported in ref 14 because the data here come from the average of four runs rather than the average of two runs in ref 14. Nonetheless, the difference in fraction folded in any one data point in the thermal denaturation from different data sets was less than 1%.
45. Jenuwein, T.; Allis, C. D. Science 2001, 293, 1074-1080.
46. Wintjens, R.; Lievin, J.; Rooman, M.; Buisine, B. J. Mol. Biol. 2000, 302, 395-410.
47. (a) Lukong, K. E.; Richard, S. Nat. Struct. Mol. Biol. 2004, 11, 914-915.
48. (b) Boisvert, F. M.; Cole, J.; Boulanger, M.; Cleroux, P.; Bachand, F.; Autexier, C.; Richard, S. J. Cell Biol. 2002, 159, 957-969.
49. (c) McBride, A. E.; Cook, J. T.; Stemmler, E. A.; Rutledge, K. L.; McGrath, K. A.; Rubens, J. A. J. Biol. Chem. 2005, 280, 30888-30898.
50. Kaiser, E.; Colescott, R. L.; Bossinger, C. D.; Cook, P. I. Anal. Biochem. 1970, 34, 595-598.
51. Wüthrich, K. NMR of Proteins and Nucleic Acids: John Wiley and Sons: New York, 1986.
52. Origin 7.5; OriginLab Corp.: Northampton, MA, 2005.