Controlling nonspecific trypsin cleavages in LC-MS/MS-based shotgun proteomics using optimized experimental conditions
Author:
Affiliation:
1. Minhang Hospital and Institutes of Biomedical Sciences
2. Fudan University
3. Shanghai
4. P. R. China
5. Department of Chemistry
6. Department of Systems Biology for Medicine and School of Basic Medical Sciences
Abstract
The highlight of this study is the efficient control of nonspecific trypsin cleavages in shotgun proteomics and N-glycoproteomics using optimized experimental conditions, which greatly increased the specificity of trypsin.
Publisher
Royal Society of Chemistry (RSC)
Subject
Electrochemistry,Spectroscopy,Environmental Chemistry,Biochemistry,Analytical Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2015/AN/C5AN01505G
Reference27 articles.
1. Trypsin Cleaves Exclusively C-terminal to Arginine and Lysine Residues
2. The Implications of Proteolytic Background for Shotgun Proteomics
3. In-depth Characterization of the Cerebrospinal Fluid (CSF) Proteome Displayed Through the CSF Proteome Resource (CSF-PR)
4. Efficient and Specific Trypsin Digestion of Microgram to Nanogram Quantities of Proteins in Organic−Aqueous Solvent Systems
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