Solid-Phase Cross-Linking (SPCL): A new tool for protein structure studies

Proteomics

Volumn 11, Issue 7, 2011, Pages 1277-1286

  Paramelle, David ^a   Enjalbal, Christine ^a   Amblard, Muriel ^a   Forest, Eric ^b   Heymann, Michaël ^c   Cantel, Sonia ^a   Geourjon, Christophe ^c   Martinez, Jean ^a   Subra, Gilles ^a  

^a UNIVERSITÉ DE MONTPELLIER   (France)

^b CEA GRENOBLE   (France)

^c UNIVERSITÉ LYON 1   (France)

Author keywords

Cross linkers; MALDI TOF MS; Peptide labelling; Protein structure; Solid phase synthesis; Technology

Indexed keywords

CROSS LINKING REAGENT; PEPTIDE FRAGMENT;

ARTICLE; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; SOLID PHASE CROSS LINKING;

EID: 79953049446     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000029     Document Type: Article

References (23)

1. Back, J. W., De Jong, L., Muijsers, A. O., De Koster, C. G., Chemical cross-linking and mass spectrometry for protein structural modeling. J. Mol. Biol. 2003, 331, 303-313.
2. Sinz, A., Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions. Mass Spectrom. Rev. 2006, 25, 663-682.
3. Jacobsen, R. B., Sale, K. L., Ayson, M. J., Novak, P. et al., Structure and dynamics of dark-state bovine rhodopsin revealed by chemical cross-linking and high-resolution mass spectrometry. Protein Sci. 2006, 15, 1303-1317.
4. Ihling, C., Schmidt, A., Kalkhof, S., Schulz, D. M. et al., Isotope-labeled cross-linkers and fourier transform ion cyclotron resonance mass spectrometry for structural analysis of a protein/peptide complex. J. Am. Soc. Mass Spectrom. 2006, 17, 1100-1113.
5. Collins, C. J., Schilling, B., Young, M., Dollinger, G., Guy, R. K., Isotopically labeled crosslinking reagents: resolution of mass degeneracy in the identification of crosslinked peptides. Bioorg. Med. Chem. Lett. 2003, 13, 4023-4026.
6. Lascoux, D., Paramelle, D., Subra, G., Heymann, M. et al., Discrimination and selective enhancement of signals in the MALDI mass spectrum of a protein by combining a matrix-based label for lysine residues with a neutral matrix. Angew. Chem. Int. Ed. 2007, 46, 5594-5597.
7. Paramelle, D., Cantel, S., Enjalbal, C., Amblard, M. et al., A new generation of cross-linkers for selective detection by MALDI MS. Proteomics 2009, 9, 5384-5388.
8. Trester-Zedlitz, M., Kamada, K., Burley, S. K., Fenyo, D. et al., A modular cross-linking approach for exploring protein interactions. J. Am. Chem. Soc. 2003, 125, 2416-2425.
9. Alley, S. C., Ishmael, F. T., Jones, A. D., Benkovic, S. J., Mapping protein-protein interactions in the bacteriophage T4 DNA polymerase holoenzyme using a novel trifunctional photo-cross-linking and affinity reagent. J. Am. Chem. Soc. 2000, 122, 6126-6127.
10. Sinz, A., Isotope-labeled photoaffinity reagents and mass spectrometry to identify protein-ligand interactions. Angew. Chem. Int. Ed. 2007, 46, 660-662.
11. Cornishbowden, A., IUPAC-IUB Joint-Commission-on-Biochemical-Nomenclature (Jcbn) - nomenclature and symbolism for amino-acids and peptides - Recommendations 1983. Biochem. J. 1984, 219, 345-373.
12. Coantic, S., Subra, G., Martinez, J., Microwave-assisted solid phase peptide synthesis on high loaded resins. Int. J. Pept. Res. Therapeut. 2008, 14, 143-147.
13. Amblard, M., Fehrentz, J. A., Martinez, J., Subra, G., Methods and protocols of modern solid phase peptide synthesis. Mol. Biotechnol. 2006, 33, 239-254.
14. Hancock, W. S., Battersby, J. E., New micro-test for detection of incomplete coupling reactions in solid-phase peptide-synthesis using 2, 4, 6-trinitrobenzene-sulphonic acid. Anal. Biochem. 1976, 71, 260-264.
15. Basso, A., Braiuca, P., De Martin, L., Ebert, C. et al., Nonswelling macroporous synbeads for improved efficiency of solid-phase biotransformations. Chem. - A Eur. J. 2004, 10, 1007-1013.
16. Basso, A., Braiuca, P., Ebert, C., Gardossi, L., Linda, P., Properties and applications of supports for enzyme-mediated transformations in solid phase synthesis. J. Chem. Technol. Biotechnol. 2006, 81, 1626-1640.
17. Bushnell, G. W., Louie, G. V., Brayer, G. D., High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 1990, 214, 585-595.
18. Heymann, M., Paramelle, D., Subra, G., Forest, E. et al., MSX-3D: a tool to validate 3D protein models using mass spectrometry. Bioinformatics 2008, 24, 2782-2783.
19. Guo, X., Bandyopadhyay, P., Schilling, B., Young, M. M. et al., Partial acetylation of lysine residues improves intraprotein cross-linking. Anal. Chem. 2008, 80, 951-960.
20. Schilling, B., Row, R. H., Gibson, B. W., Guo, X., Young, M. M., MS2Assign, automated assignment and nomenclature of tandem mass spectra of chemically crosslinked peptides. J. Am. Soc. Mass Spectrom. 2003, 14, 834-850.
21. Pearson, K. M., Pannell, L. K., Fales, H. M., Intramolecular cross-linking experiments on cytochrome c and ribonuclease A using an isotope multiplet method. Rapid Commun. Mass Spectrom. 2002, 16, 149-159.
22. Muller, D. R., Schindler, P., Towbin, H., Wirth, U. et al., Isotope tagged cross linking reagents. A new tool in mass spectrometric protein interaction analysis. Anal. Chem. 2001, 73, 1927-1934.
23. Kalkhof, S., Ihling, C., Mechtler, K., Sinz, A., Chemical cross-linking and high-performance Fourier transform ion cyclotron resonance mass spectrometry for protein interaction analysis: application to a calmodulin/target peptide complex. Anal. Chem. 2005, 77, 495-503.