1. IMPROVED APPROACH FOR THE LABELING OF ARGININE, GLUTAMIC, AND ASPARTIC ACID SIDE CHAINS IN PROTEINS USING CHROMATOGRAPHIC TECHNIQUES
- Author
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Stepanka Kuckova, Richard Hrabal, Martina Vermachova, Petra Junkova, Jan Prchal, and Radovan Hynek
- Subjects
Chromatography ,biology ,Arginine ,Chemistry ,Cytochrome c ,Clinical Biochemistry ,Pharmaceutical Science ,Chemical modification ,Glutamic acid ,Reversed-phase chromatography ,Mass spectrometry ,Biochemistry ,Analytical Chemistry ,Aspartic acid ,biology.protein ,Side chain - Abstract
Specific chemical modification is one of the basic techniques of protein chemistry. Inter alia can be used for detection of surface accessible amino acid residues; this information is of particular importance for studies of the participation of residues in intermolecular interactions of a protein. We achieved an improvement of the technique for arginine, aspartic, and glutamic acid modification using a simple combination of gel permeation and reversed-phase chromatography prior to mass spectrometry analysis. The improved protocol was tested on cytochrome c and M-PMV matrix protein. In both proteins, all accessible arginines and a high number of acidic amino acids were modified. These results indicate that the new protocol can be useful in protein structure analysis, generally.
- Published
- 2013
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