Titlebook: Gel-Free Proteomics; Methods and Protocol Kris Gevaert,Joël Vandekerckhove Book 2011 Springer Science+Business Media, LLC 2011 LPI hexalene

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书目名称Gel-Free Proteomics影响因子(影响力)




书目名称Gel-Free Proteomics影响因子(影响力)学科排名




书目名称Gel-Free Proteomics网络公开度




书目名称Gel-Free Proteomics网络公开度学科排名




书目名称Gel-Free Proteomics被引频次




书目名称Gel-Free Proteomics被引频次学科排名




书目名称Gel-Free Proteomics年度引用




书目名称Gel-Free Proteomics年度引用学科排名




书目名称Gel-Free Proteomics读者反馈




书目名称Gel-Free Proteomics读者反馈学科排名

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Einleitung und Gang der Untersuchung,abeled peptide with a 4 Da mass shift from the .O-labeled sample. Peptide .O labeling is ideally suited for generating a labeled “universal” reference sample used for obtaining accurate and reproducible quantitative measurements across large number of samples in quantitative discovery proteomics.

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Betriebliche Führungskräfte-Entwicklungd-based protein immobilization (LPI) is the core technology in a new approach that enables immobilization and digestion of native membrane proteins inside a flow cell format. The presented method is described in the context of comparing the method to traditional approaches where the sample amount that is digested and analyzed is the same.

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Trypsin-Catalyzed Oxygen-18 Labeling for Quantitative Proteomics,abeled peptide with a 4 Da mass shift from the .O-labeled sample. Peptide .O labeling is ideally suited for generating a labeled “universal” reference sample used for obtaining accurate and reproducible quantitative measurements across large number of samples in quantitative discovery proteomics.

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,Membrane Protein Digestion – Comparison of LPI HexaLane with Traditional Techniques,d-based protein immobilization (LPI) is the core technology in a new approach that enables immobilization and digestion of native membrane proteins inside a flow cell format. The presented method is described in the context of comparing the method to traditional approaches where the sample amount that is digested and analyzed is the same.

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Betriebliche Gesundheitspolitiky facilitate “high-throughput” phosphoproteomics research. Here, we describe the setup of a simple, robust, and automated online TiO.-based nanoscale chromatographic approach to selectively enrich and separate phosphorylated peptides from proteolytic digests of moderate and high complexity.