Disruption of coiled coil formation by methionine oxidation

Bioorganic and Medicinal Chemistry Letters

Volumn 6, Issue 3, 1996, Pages 229-232

  García Echeverría, Carlos ^a  

^a CIBA GEIGY LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE; OXIDATION; PROTEIN ANALYSIS; PROTEIN STRUCTURE;

EID: 0030062258     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0960-894X(96)00009-1     Document Type: Article

References (16)

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2. (b) Cohen, C.; Parry, D.A.D. Science 1994, 263, 488-489.
3. (c) Pathak, D.; Sigler, P.B. Current Biology 1992, 2, 116-123.
4. (d) Abel, T.; Maniatis, T. Nature 1989, 341, 24-25.
5. (a) Slate, C.A.; Weninger, S.C.; Church, F.C.; Erickson, B.W. Int. J. Peptide Protein Res. 1995, 45, 290-298.
6. (b) Graddis, T.J.; Myszka, D.G.; Chaiken, I.M. Biochemistry 1993, 32, 12664-12671.
7. (c) O'Shea, E.K.; Lumb, K.J.; Kim, P.S. Current Biology 1993, 3, 658-667.
8. (d) Moser, R. Protein Eng. 1992, 5, 323-331.
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11. (b) Landschulz, W.H.; Johnson, P.F.; McKnight, S.L. Science 1988, 240, 1759-1764.
12. García-Echeverria, C. Lett. Pept. Sci. 1994, 1, 255-262.
13. 2 was reported by Su, J.Y.; Hodges, R.S.; Kay, C.M. Biochemistry 1994, 33, 15501-15510. Kay and co-workers found that a minimum of three heptad repeats was required to form a stable two-stranded α-helical coiled-coil.
14. This work expands the "switchable residue" concept of Dado and Gellman: (a) Dado, G.P.; Gellman, S.H. J. Am. Chem. Soc. 1993, 115, 12609-12610. Gellman used methionine residues to control the secondary structure preference, α-helix versus ß-strand, of an 18-mer peptide. For a discussion on the conformational properties of methionine, see:
15. (b) Gellman, S.H., Biochemistry 1991, 30, 6633-6635.
16. Atherton, E.; Sheppard, R.C. In The Peptides; Gross, E.; Meinhofer, J., Eds.; Academic Press: New York, 1987; Vol. 9, pp 1-38.