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Efficient Primary Structure Elucidation of Disulfide-bridged Peptides

The combination of Edman sequence analysis and electrospray tandem mass spectrometry provides accurate and detailed structural data of highlyknotted spider toxins

Purpose

The primary structure determination of disulfide bridged peptides is greatly facilitated using a combination of the Procise cLC 492 sequencing system and the QSTAR Pulsar hybrid quadrupole time-of-flight mass spectrometer. These two techniques provide complementary data for an unambiguous characterization of peptides and proteins, while simultaneously extending the range of applications.

Overview

N-terminal amino acid sequence analysis by Edman degradation has been the workhorse for the de novo sequence determination of peptides and proteins for many years, especially since the introduction of an automated sequenator in 1967 by Per Edman himself. Modern sequencing systems based on the Edman chemistry provide high sensitivity and enable fully automated analyses. Due to the unambiguous sequence data generated, Edman sequencing is still the reference technology for complete de novo protein sequencing. As a further key technology, mass spectrometry has entered the field of bioanalysis within the last decade, enabling rapid protein identification either by peptide mass mapping or by determination of partial amino acid sequences. Besides that, the impressive resolving power and mass accuracy of modern mass spectrometric instrumentation offers a great potential for elucidation of structural details. The combination of Edman sequencing and tandem mass spectrometry is an efficient approach to the primary structure elucidation of complex, highly disulfide-bridged spider toxins.

Key Features

Total de novo sequencing approach

Fully automated amino acid sequence determination using th
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