Switching variability index based multiple strategy CFAR detector

A switching variability index （SVl） constant false alarm rate （CFAR） detector is proposed for improving the detection performance of VI-CFAR detectors in multiple targets backgrounds. When the presence of non-homogeneity in CFAR reference windows is indicated by a VI-CFAR detector, a switching- CFAR detector is introduced to optimize the performance of the VI-CFAR detector in homogeneous, multiple targets and clutter edge backgrounds. The structure and parameters selection method of the SVI-CFAR detector is presented. Comparisons with classic CFAR detectors and recently proposed detectors are also given. Theoretical analysis and simulation results show that SVICFAR detector maintains the good performance of the VI-CFAR detector in homogeneous and clutter edge backgrounds, while greatly improving the capacity of anti-multi targets.

Computational prediction and validation of specific EmbR binding site on PknH

Tuberculosis drug resistance continues to threaten global health but the underline molecular mechanisms are not clear.Ethambutol(EMB),one of the well-known first-line drugs in tuberculosis treatment is,unfortunately,not free from drug resistance problems.Genomic studies have shown that some genetic mutations in Mycobacterium tuberculosis(Mtb)EmbR,and EmbC/A/B genes cause EMB resistance.EmbR-PknH pair controls embC/A/B operon,which encodes EmbC/A/B genes,and EMB interacts with EmbA/B proteins.However,the EmbR binding site on PknH was unknown.We conducted molecular simulation on the EmbR-peptides binding structures and discovered phosphorylated PknH 273-280(N′-HEALS^(P)DPD-C′)makesβstrand with the EmbR FHA domain,asβ-MoRF(MoRF;molecular recognition feature)does at its binding site.Hydrogen bond number analysis also supported the peptides’β-MoRF forming activity at the EmbR FHA domain.Also,we discovered that previously known phosphorylation residues might have their chronological order according to the phosphorylation status.The discovery validated that Mtb PknH 273-280(N′-HEALSDPD-C′)has reliable EmbR binding affinity.This approach is revolutionary in the computer-aided drug discovery field,because it is the first trial to discover the protein-protein interaction site,and find binding partner in nature from this site.