Conformational effect on the fragmentations of peptide derivatives in field desorption mass spectrometry
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference9 articles.
1. Field desorption mass spectrometry of peptides
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1. Insight into β-hairpin stability: a structural and thermodynamic study of diastereomeric β-hairpin mimeticsElectronic supplementary information (ESI) available: temperature and concentration-dependent chemical shifts and melting curves of the investigated molecules in different solvents and details of the X-ray analysis. See http://www.rsc.org/suppdata/nj/b1/b111241d/;New Journal of Chemistry;2002-06-06
2. Fragmentation of an alkali metal-attached peptide probed by collision-induced dissociation Fourier transform mass spectrometry and computational methodology;Journal of Mass Spectrometry;1999-09
3. Fast atom bombardment mass spectrometric study of benzyloxycarbonyl-protected tetrapeptides containing proline;Organic Mass Spectrometry;1994-04
4. Fragmentations of flurbiprofen-L-arginine diastereomers in negative ion fast atom bombardment mass spectrometry;Biological Mass Spectrometry;1993-12
5. Dependence of benzyl alcohol loss onC-terminal amino acid in tandem mass spectrometry ofN-protected tripeptides;Organic Mass Spectrometry;1993-10
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