Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/74158
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Type: Journal article
Title: Backbone fragmentations of [M-H]⁻ anions from peptides. Reinvestigation of the mechanism of the beta prime cleavage
Other Titles: Backbone fragmentations of [M-H](-) anions from peptides. Reinvestigation of the mechanism of the beta prime cleavage
Author: Wang, T.
Tran, T.
Calabrese, A.
Bowie, J.
Citation: Rapid Communications in Mass Spectrometry, 2012; 26(16):1832-1840
Publisher: John Wiley & Sons Ltd
Issue Date: 2012
ISSN: 0951-4198
1097-0231
Statement of
Responsibility: 
Tianfang Wang, T. T. Nha Tran, Antonio N. Calabrese, John H. Bowie
Abstract: RATIONALE: An experimental study has shown that the structure of a β' ion proposed earlier is incorrect. Backbone cleavage β' anions have structures R(NH(-)) from systems [[RNHCH(X)CONHCH(Y)CO(2)H (or C-terminal CONH(2))-H](-) (where R is the rest of the peptide molecule and X and Y represent the α side chains of the individual amino acid residues). METHODS: Ab initio calculations were carried out at the CAM-B3LYP/6-311++g(d,p) level of theory. CONCLUSIONS: The calculations suggest that RNH(-) ions are formed by S(N)i cyclisation processes involving either (i) the C-terminal CO(2)(-) or C-terminal [CONH](-) as appropriate, or (ii) an enolate ion [-NHC(-)(Y)-] cyclising at the backbone CH of the -CH(X)- group. Concomitant C-N bond cleavage then liberates an RNH(-) ion, processes which can occur along the peptide backbone.
Keywords: Anions; Peptides; Spectrometry, Mass, Electrospray Ionization; Amino Acid Sequence; Models, Molecular; Molecular Sequence Data
Rights: Copyright © 2012 John Wiley & Sons, Ltd.
RMID: 0020120676
DOI: 10.1002/rcm.6297
Appears in Collections:Chemistry publications

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