Analysis of peptide secondary structures by photoactivatable amino acid analogues

Angewandte Chemie - International Edition

Volumn 51, Issue 50, 2012, Pages 12602-12605

  Kölbel, Knut ^a   Ihling, Christian H ^a   Sinz, Andrea ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

analytical methods; circular dichroism; mass spectrometry; photoaffinity labeling; secondary structure

Indexed keywords

ANALYTICAL METHOD; HIGH RESOLUTION MASS SPECTROMETRY; INTRAMOLECULAR INTERACTIONS; PEPTIDE SECONDARY STRUCTURES; PHOTOACTIVATABLE; PHOTOAFFINITY LABELING; PHOTOCHEMICAL CROSS-LINKING; SECONDARY STRUCTURES; TRANSIENT INTERACTIONS;

AMINO ACIDS; DICHROISM; MASS SPECTROMETRY;

PEPTIDES;

AMINO ACID; PEPTIDE;

AFFINITY LABELING; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; ELECTROSPRAY MASS SPECTROMETRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; PROTEIN SECONDARY STRUCTURE; ULTRAVIOLET RADIATION;

AFFINITY LABELS; AMINO ACID SEQUENCE; AMINO ACIDS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; ULTRAVIOLET RAYS;

EID: 84870607864     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201205308     Document Type: Article

References (23)

1. L. B. Shih, H. Bayley, Anal. Biochem. 1985, 144, 132.
2. H. Bayley, in Chemistry of Diazirines, Vol. 2 (Ed.:, M. T. H. Liu,), CRC, Boca Raton, 1987
3. L. Dubinsky, B. P. Krom, M. M. Meijler, Bioorg. Med. Chem. 2012, 20, 554.
4. M. Suchanek, A. Radzikowska, C. Thiele, Nat. Methods 2005, 2, 261.
5. A. L. MacKinnon, J. L. Garrison, R. S. Hegde, J. Taunton, J. Am. Chem. Soc. 2007, 129, 14560
6. T. Durek, J. Zhang, C. He, S. B. Kent, Org. Lett. 2007, 9, 5497
7. M. Vila-Perelló, M. R. Pratt, F. Tulin, T. W. Muir, J. Am. Chem. Soc. 2007, 129, 8068.
8. A. Sinz, Mass Spectrom. Rev. 2006, 25, 663
9. A. Sinz, Anal. Bioanal. Chem. 2010, 397, 3433.
10. J. Brunner, H. Senn, F. M. Richards, J. Biol. Chem. 1980, 255, 3 313.
11. M. S. Platz, H. Huang, F. Ford, J. Toscano, Pure Appl. Chem. 1997, 69, 803
12. J. Wang, G. Burdzinski, J. Kubicki, M. S. Platz, R. A. Moss, X. Fu, P. Piotrowiak, M. Myahkostupov, J. Am. Chem. Soc. 2006, 128, 16446
13. Y. Zhang, G. Burdzinski, J. Kubicki, M. S. Platz, J. Am. Chem. Soc. 2008, 130, 16134.
14. A. M. Mansoor, I. D. R. Stevens, Tetrahedron Lett. 1966, 16, 17 33.
15. M. Platz, A. S. Admasu, S. Kwiatkowski, P. J. Crocker, N. Imai, D. S. Watt, Bioconjugate Chem. 1991, 2, 337
16. P. J. Weber, A. G. Beck-Sickinger, J. Pept. Res. 1997, 49, 375.
17. A. J. Maynard, G. J. Sharman, M. S. Searle, J. Am. Chem. Soc. 1998, 120, 1996.
18. B. Jayaram, K. Bhushan, S. R. Shenoy, P. Narang, S. Bose, P. Agrawal, D. Sahu, V. Pandey, Nucleic Acids Res. 2006, 34, 6195.
19. Likewise, ions corresponding to cross-linked peptides [1-6]∼[17-25] and [1-6]∼[16-25] were also identified. In the figures, a nomenclature based on, B. Schilling, R. H. Row, B. W. Gibson, X. Guo, M. M. Young, J. Am. Soc. Mass Spectrom. 2003, 14, 834 is applied: the longer peptide is designated as α, the shorter as β. Cross-links themselves are denoted by a ≈.
20. K. Koelbel, C. H. Ihling, U. Kuhn, I. Neundorf, S. Otto, J. Stichel, D. Robaa, A. G. Beck-Sickinger, A. Sinz, E. Wahle, Biochemistry 2012, 51, 5463.
21. B. Fierz, H. Satzger, C. Root, P. Gilch, W. Zinth, T. Kiefhaber, Proc. Natl. Acad. Sci. USA 2007, 104, 216 3.
22. S. Schaks, D. Maucher, C. H. Ihling, A. Sinz, in Biomacromolecular Mass Spectrometry, Vol. 2, Nova Science Publishers, Hauppauge, New York, 2012, p. 249.
23. M. Götze, J. Pettelkau, S. Schaks, K. Bosse, C. H. Ihling, F. Krauth, R. Fritzsche, U. Kühn, A. Sinz, J. Am. Soc. Mass Spectrom. 2012, 23, 7 6.