Isotope-edited infrared spectroscopy of helical peptides [11]

Journal of the American Chemical Society

Volumn 121, Issue 50, 1999, Pages 11914-11915

  Decatur, Sean M ^a   Antonic, Jelena ^a  

^a MOUNT HOLYOKE COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; CARBON 13; POLYPEPTIDE;

CIRCULAR DICHROISM; INFRARED SPECTROSCOPY; ISOTOPE LABELING; LETTER; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE ANALYSIS; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

EID: 0033596301     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja991279q     Document Type: Letter

References (34)

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18. 2O, the amide proton in the peptide moiety is exchanged for a deuterium, and the resulting amide I′ mode is shifted to lower frequency. See: Diem, M. Introduction to Modern Vibrational Spectroscopy; Wiley: New York, 1993.
19. Assuming that the amide I′ mode is pure carbonyl stretch undergoing simple harmonic motion, this shift can be estimated using the equation v = (1/2π)(√k/μ), where μ is the reduced mass of the carbonyl group.
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24. Sequence based on peptides studied in the following: (a) Armstrong, K. M.; Fairman, R.; Baldwin, R. L. J. Mol. Biol. 1993, 230, 284-291. (b) Armstrong, K. M.; Baldwin, R. L. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 11337-113340. The secondary structures of these peptides were determined by measurement of far-UV circular dichroism spectra; the spectra and % helicity are in agreement with data reported by Armstrong and Baldwin. In our experiments, the amide I′ bands of peptide L2 retain the same relative shape when the concentration is varied in the range 1-10 mM, suggesting that no significant peptide-peptide interactions are occurring.
25. Sequence based on peptides studied in the following: (a) Armstrong, K. M.; Fairman, R.; Baldwin, R. L. J. Mol. Biol. 1993, 230, 284-291. (b) Armstrong, K. M.; Baldwin, R. L. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 11337-113340. The secondary structures of these peptides were determined by measurement of far-UV circular dichroism spectra; the spectra and % helicity are in agreement with data reported by Armstrong and Baldwin. In our experiments, the amide I′ bands of peptide L2 retain the same relative shape when the concentration is varied in the range 1-10 mM, suggesting that no significant peptide-peptide interactions are occurring.
26. 13C-alanine was purchased from Cambridge Isotopes. Peptides were purified by reverse-phase HPLC; purity was confirmed by analytical reverse-phase HPLC and electrospray mass spectrometry. Residual trifluoracteic acid (TFA) from synthesis was removed by lyophilization.
27. 2 plates and a 50-μm Teflon spacer.
28. 10 rather than an a helix. See: (a) Muck, S. M.; Martinez, G. V.; Fiori, W. R.; Todd, A. P.; Millhauser, G. L. Nature 1992, 159, 653-655. (b) Millhauser, G. L. Biochemistry 1995, 34, 3873-3877. (c) Millhauser, G. L.; Stenland, C. J.; Hanson, P.; Bolin, K. A.; van de Ven, F. J. M. J. Mol. Biol. 1997, 267, 963-974.
29. 10 rather than an a helix. See: (a) Muck, S. M.; Martinez, G. V.; Fiori, W. R.; Todd, A. P.; Millhauser, G. L. Nature 1992, 159, 653-655. (b) Millhauser, G. L. Biochemistry 1995, 34, 3873-3877. (c) Millhauser, G. L.; Stenland, C. J.; Hanson, P.; Bolin, K. A.; van de Ven, F. J. M. J. Mol. Biol. 1997, 267, 963-974.
30. 10 rather than an a helix. See: (a) Muck, S. M.; Martinez, G. V.; Fiori, W. R.; Todd, A. P.; Millhauser, G. L. Nature 1992, 159, 653-655. (b) Millhauser, G. L. Biochemistry 1995, 34, 3873-3877. (c) Millhauser, G. L.; Stenland, C. J.; Hanson, P.; Bolin, K. A.; van de Ven, F. J. M. J. Mol. Biol. 1997, 267, 963-974.
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33. Calculations were made using the programs Helix2 and Caphelix, Rohl, C. A.; Chakrabatty, A.; Baldwin, R. L. Protein Sci. 1996, 5, 2623-2637.
34. 10 helical residues at the C-terminus in the L4 peptide on the basis of the data presented here. However, vibrational circular dichroism of these labeled peptides may shed more light onto this question. See: Yoder, G.; Polese, A.; Silva, R. A. G. D.; Formaggio, F.; Crisma, M.; Broxterman, Q. B.; Kamphius, J.; Toniolo, C.; Keiderling, T. A. J. Am. Chem. Soc. 1997, 119, 10278-10285.