Abstract. With the embedding of EEG (electro-encephalography) sensors in wireless headsets and other consumer electronics, authenticating users based on their brainwave signals has become a realistic possibility. We undertake an experimental study of the usability and performance of user authentication using consumer-grade EEG sensor technology. By choosing custom tasks and custom acceptance thresholds for each subject, we can achieve 99% authentication accuracy using single-channel EEG signals, which is on par with previous research employing multichannel EEG signals using clinical-grade devices. In addition to the usability improvement offered by the single-channel dry-contact EEG sensor, we also study the usability of different classes of mental tasks. We find that subjects have little difficulty recalling chosen "pass-thoughts" (e.g., their previously selected song to sing in their mind). They also have different preferences for tasks based on the perceived difficulty and enjoyability of the tasks. These results can inform the design of authentication systems that guide users in choosing tasks that are both usable and secure.
Rationale
Proteolytic cleavages generate active precursor proteins by creating new N-termini in the proteins. A number of strategies recently published regarding the enrichment of original or newly formed N-terminal peptides using guanidination of lysine residues and amine reactive reagents. For effective enrichment of N-terminal peptides, the efficiency of trypsin proteolysis on homoarginine (guanidinated) modified proteins must be understood and simple and versatile solid-phase N-terminal capture strategies should be developed.
Methods
We present here a mass spectrometry-based study to evaluate and optimize the trypsin proteolysis on a guanidinated modified protein. Trypsin proteolysis was studied using different amount of trypsin to modified protein ratios. To capture the original N-termini, after guanidination of proteins, original N-termini were acetylated and the proteins were digested with trypsin. The newly formed N-terminal tryptic peptides were captured with a new amine reactive acid-cleavable solid-phase reagent. The original N-terminal peptides were then collected from the supernatant of the solution.
Results
We demonstrated a detailed study of the efficiency of enzyme trypsin on homoarginine modified proteins. We observed that the rate of hydrolysis of homoarginine residues compared to their lysine/arginine counter parts were slower but generally cleaved after an overnight digestion period depending on the protein to protease concentration ratios. Selectivity of the solid-phase N-terminal reagent was studied by enrichment of original N-terminal peptides from two standard proteins, ubiquitin and RNaseS.
Conclusion
We found enzyme trypsin is active in guanidinated form of protein depending on enzyme to protein concentrations, time and the proximity of arginine residues in the sequence. The novel solid-phase capture reagent also successfully enriched N-terminal peptides from the standard protein mixtures. We believe this trypsin proteolysis study on homoarginine modified proteins and our simple and versatile solid- phase capture strategy could be very useful for enrichment and sequence determination of proteins N-termini by mass spectrometry.
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