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Werner Ens

Researcher at University of Manitoba

Publications -  132
Citations -  7644

Werner Ens is an academic researcher from University of Manitoba. The author has contributed to research in topics: Mass spectrometry & Ion. The author has an hindex of 47, co-authored 132 publications receiving 7456 citations. Previous affiliations of Werner Ens include University of Münster & Uppsala University.

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Charting the Proteomes of Organisms with Unsequenced Genomes by MALDI-Quadrupole Time-of-Flight Mass Spectrometry and BLAST Homology Searching

TL;DR: A "MS BLAST" homology searching protocol was developed to overcome specific limitations imposed by mass spectrometric data, such as the limited accuracy of de novo sequence predictions.
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Rapid ‘de novo’ peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time‐of‐flight mass spectrometer

TL;DR: A combination of the nanoelectrospray ion source, isotopic end labeling of peptides and a quadrupole/ time-of-flight instrument allows facile read-out of the sequences of tryptic peptides.
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A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: design and performance

TL;DR: A matrix-assisted laser desorption/ionization source has been coupled to a tandem quadrupole/time-of-flight (QqTOF) mass spectrometer by means of a collisional damping interface and Ion production at pressures near 1 Torr is found to give reduced metastable fragmentation, particularly for higher mass molecular ions.
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An Improved Model for Prediction of Retention Times of Tryptic Peptides in Ion Pair Reversed-phase HPLC Its Application to Protein Peptide Mapping by Off-Line HPLC-MALDI MS

TL;DR: The proposed model is based on the measurement of the retention times of 346 tryptic peptides in the 560- to 4,000-Da mass range, derived from a mixture of 17 protein digests, and can be used for accurate prediction of retention times fortryptic peptide on reversed-phase columns of different sizes with a linear water-ACN gradient and with TFA as the ion-pairing modifier.
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MALDI quadrupole time-of-flight mass spectrometry: a powerful tool for proteomic research.

TL;DR: The high mass resolution and the high mass accuracy of this instrument in both MS and MS/MS modes allow identification of a protein either by peptide mass fingerprinting of the protein digest or from tandem mass spectra acquired by collision-induced dissociation of individual peptide precursors.