Effective high compression of ECG signals at low level distortion

An effective method for compression of ECG signals, which falls within the transform lossy compression category, is proposed. The transformation is realized by a fast wavelet transform. The effectiveness of the approach, in relation to the simplicity and speed of its implementation, is a consequence of the efficient storage of the outputs of the algorithm which is realized in compressed Hierarchical Data Format. The compression performance is tested on the MIT-BIH Arrhythmia database producing compression results which largely improve upon recently reported benchmarks on the same database. For a distortion corresponding to a percentage root-mean-square difference (PRD) of 0.53, in mean value, the achieved average compression ratio is 23.17 with quality score of 43.93. For a mean value of PRD up to 1.71 the compression ratio increases up to 62.5. The compression of a 30 min record is realized in an average time of 0.14 s. The insignificant delay for the compression process, together with the high compression ratio achieved at low level distortion and the negligible time for the signal recovery, uphold the suitability of the technique for supporting distant clinical health care

The Critical Role of N- and C-Terminal Contact in Protein Stability and Folding of a Family 10 Xylanase under Extreme Conditions

Stabilization strategies adopted by proteins under extreme conditions are very complex and involve various kinds of interactions. Recent studies have shown that a large proportion of proteins have their N- and C-terminal elements in close contact and suggested they play a role in protein folding and stability. However, the biological significance of this contact remains elusive.In the present study, we investigate the role of N- and C-terminal residue interaction using a family 10 xylanase (BSX) with a TIM-barrel structure that shows stability under high temperature, alkali pH, and protease and SDS treatment. Based on crystal structure, an aromatic cluster was identified that involves Phe4, Trp6 and Tyr343 holding the N- and C-terminus together; this is a unique and important feature of this protein that might be crucial for folding and stability under poly-extreme conditions. folding and activity. Alanine substitution with Phe4, Trp6 and Tyr343 drastically decreased stability under all parameters studied. Importantly, substitution of Phe4 with Trp increased stability in SDS treatment. Mass spectrometry results of limited proteolysis further demonstrated that the Arg344 residue is highly susceptible to trypsin digestion in sensitive mutants such as ΔF4, W6A and Y343A, suggesting again that disruption of the Phe4-Trp6-Tyr343 (F-W-Y) cluster destabilizes the N- and C-terminal interaction. Our results underscore the importance of N- and C-terminal contact through aromatic interactions in protein folding and stability under extreme conditions, and these results may be useful to improve the stability of other proteins under suboptimal conditions