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Deterding LJ, Tomer KB, Spatola AF. Tandem mass spectrometry for the structural determination of backbone-modified peptides. J Am Soc Mass Spectrom. 1990;1(2):174-82doi: 10.1016/1044-0305(90)85054-P.
Deterding, L. J., Tomer, K. B., & Spatola, A. F. (1990). Tandem mass spectrometry for the structural determination of backbone-modified peptides. Journal of the American Society for Mass Spectrometry, 1(2), 174-82. https://doi.org/10.1016/1044-0305(90)85054-P
Deterding, L J, et al. "Tandem mass spectrometry for the structural determination of backbone-modified peptides." Journal of the American Society for Mass Spectrometry vol. 1,2 (1990): 174-82. doi: https://doi.org/10.1016/1044-0305(90)85054-P
Deterding LJ, Tomer KB, Spatola AF. Tandem mass spectrometry for the structural determination of backbone-modified peptides. J Am Soc Mass Spectrom. 1990 Apr;1(2):174-82. doi: 10.1016/1044-0305(90)85054-P. PMID: 24248746.
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J Am Soc Mass Spectrom. 1990 Apr;1(2):174-82. doi: 10.1016/1044-0305(90)85054-P.

Tandem mass spectrometry for the structural determination of backbone-modified peptides.

Journal of the American Society for Mass Spectrometry

L J Deterding, K B Tomer, A F Spatola

Affiliations

  1. Laboratory of Moiecular Biophysics, National Institute of Environmental Health Sciences, P.O. Box 12233, 27709, Research Triangle Park, NC.

PMID: 24248746 DOI: 10.1016/1044-0305(90)85054-P

Abstract

A variety of backbone-modified peptides were desorbed by fast atom bombardment and collisionally activated. These peptide modifications involve the replacement of a normal [CONH] peptide linkage with such groups as thiomethylene ether (CH2S), thioamide (CSNH), methyleneamine (CH2NH), and thiomethylene sulfoxide (CH2SO) moieties. Modified linear peptides decompose to give fragmentations characteristic of the modifications as well as typical peptide bond fragments. The presence of a replacement group in cyclic peptides can induce new fragmentations. The presence of other functional groups, such as an exocyclic N-terminal residue, however, can dominate the observed fragmentations. Upon collisional activation, unmodified linear peptides fragment to give N-terminal ions as the most abundant daughter ions. In comparison, ψ[CH2NH] and ψ[CH2S ] modified linear peptides decompose to give prominent C-terminal sequence ions. The ψ[CH2SO] modified linear peptides, however, fragment into both N- and C-terminal ions of high relative abundance. Depending on the modification, daughter ions or internal fragment ions are observed that are characteristic of the amide bond replacement. Useful structural information can therefore be obtained.

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