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Directed proteomics of DNA-binding proteins | 29225
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

+44 1223 790975

Directed proteomics of DNA-binding proteins


5th International Conference on Proteomics & Bioinformatics

September 01-03, 2015 Valencia, Spain

Linda Nagore

University of Texas at San Antonio, USA

Posters-Accepted Abstracts: J Proteomics Bioinform

Abstract :

The common difficulty with any enrichment technique is developing a method that can be widely applicable and yet still extract a small subset of the proteome. We discuss a high-throughput MALDI-MS method that uses DNA to enrich for transcriptions factors while simultaneously removing interfering sample components. This was accomplished by using a polyvinylpyrrolidone coated MALDI plate which has the unique advantage of enrichment, desalting, digestion and characterization on a single platform. Protein as well as DNA can be analyzed directly from the support. This approach positively identified five transcription factors from nuclear extract using the hTERT promoter using MS/MS of a discrete set of tryptic peptides. On-target enrichment coupled to MALDI-TOF-MS has shown to be fast, sensitive and highly reproducible with low redundancy and can be applied to any protein that binds DNA including those with low affinities.

Biography :

Email: linda.nagore@gmail.com

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