Fluorescent Modification Of N-Terminal Amino Group In Peptides For Complete Sequence Analysis Using Psd Method In Maldi-Tof-Ms

Authors: Nakagawa M.; Nakanishi H.

Source: Protein and Peptide Letters, Volume 11, Number 1, February 2004 , pp. 71-77(7)

Publisher: Bentham Science Publishers

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Abstract:

In the sequence analyses of peptides from nucleoprotein in influenza virus, it was very difficult to obtain the sufficient numbers of fragment ions using the post-source decay (PSD) method in MALDITOF- MS. Fluorescent modification of the N-terminal amino group in the target peptides was introduced for the PSD measurement. The fluorescently-labelled peptides gave sufficient fragment ions in the PSD spectrum, which leads to the complete sequence analysis of peptide.

Keywords: maldi-tof-ms; psd method; peptide sequence; fluorescently modification; nucleoprotein in influenza virus

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866043478464

Affiliations: 1: Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 6, 1-1, Higashi, Tsukuba, Ibaraki, 305-8566, Japan

Publication date: 2004-02-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.