A fluorescent zinc probe based on metal-induced peptide folding

Journal of the American Chemical Society

Volumn 118, Issue 27, 1996, Pages 6514-6515

  Godwin, Hilary Arnold ^a   Berg, Jeremy M ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; FLUORESCENCE; PROTEIN FOLDING;

EID: 0029975181     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja961184d     Document Type: Article

References (16)

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3. Tsien, R. Y. In Methods in Cell Biology; Taylor, D. L., Wang, Y,-L., Eds.; Academic Press, Inc.: New York, 1989; Vol. 30, pp 127-156.
4. Bright, G. R.; Fisher, G. W.; Rogowska, J.; Taylor, D. L. In Methods in Cell Biology, Taylor, D. L., Wang, Y.-L., Eds., Academic Press, Inc.; New York, 1989; Vol. 30, pp 157-192.
5. Adams, S. R.; Harootunian, A. T.; Buechler, Y. J.; Taylor, S. S.; Tsien, R. Y. Nature 1991, 349, 694-697.
6. Zalewski, P. D.; Forbes, I. J.; Seamark, R. F.; Borlinghaus, R.; Betts, W. H.; Lincoln, S. F.; Ward, A. D. Chem. Biol. 1994, 1, 153-161.
7. Krizek, B. A.; Merkle, D. L.; Berg, J. M. Inorg. Chem. 1993, 32, 937-940.
8. Krizek, B. A.; Berg, J. M. Inorg. Chem. 1992, 31, 2984-2986.
9. Kim, C. A.; Berg. J. M. Nature 1993, 362, 267-270.
10. Eis, P. S.; Lakowicz, J. R. Biochemistry 1993, 32, 7981-7993.
11. An analog in which the acceptor was texas red (TR) was also synthesized (CP-TR-F). Texas red (absorption maximum 600 nm in CP-TR-F) has a smaller spectral overlap with fluorescein than does lissamine (absorption maximum 578 nm in CP-L-F). Less intramolecular energy transfer was observed for CP-TR-F than for CP-L-F. As a result, CP-L-F shows larger changes in fluorescence in response to zinc binding.
12. 14LyS → Cys).
13. ElectroSpray mass spectrometry of CP-L-F was performed by PeptidoGenic Research & Co., 5031 Preston Ave., Livermore, CA 94550, using a Sciex API I ElectroSpray Mass Spectrometer.
14. These spectra are obtained by exciting into the fluorescein absorption (430 nm) of CP-L-F (3-5 μM in 100 mM HEPES, 50 mM NaCI, pH 7.1 buffer) and examining the fluorescence emission as a function of wavelength. All peptide manipulations were performed under an atmosphere of 95% nitrogen-5% hydrogen to avoid peptide oxidation and quenching of the fluorescence by molecular oxygen.
15. Michael, S. F.; Kilfoil, V. J.; Schmidt, M. H.; Amann, B. T.; Berg, J. M. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 4796-4800.
16. -12 M. The samples were equilibrated for 15 min at 37 °C at each point.