Non-Invasive Measure of Stenosis Severity Through Spectral Analysis [post-print]

A preliminary study on the effect of stenosis severity in a restricted flow is performed through the spectral analysis of sound signals. A model pulsatile flow that uses differing area reductions through an opening was employed, where contact microphones secured outside of the reduction measured the sound intensity in the flow. A spectral analysis shows the narrowing results in increased magnitude of frequencies in the range of 15 to 170Hz, with different narrowing cases resulting in different peak frequencies. Low frequency content up to 10 Hz remains approximately unchanged. This simplistic approach of signal processing forms a basis for enhanced understanding and diagnosis of the severity of narrowing in an internal flow, and encourages future research into more complicated bispectral methods of analysis. The results show a clear difference between regular turbulence present in an internal flow and enhanced turbulence due to a stenosis or similar restriction in the flow

Crystal structure of the Bacillus subtilis penicillin-binding protein 4a, and its complex with a peptidoglycan mimetic peptide

The genome of Bacillus subtilis encodes 16 penicillin-binding proteins (PBPs) involved in the synthesis and/or remodelling of the peptidoglycan during the complex life cycle of this sporulating Gram-positive rod-shaped bacterium. PBP4a (encoded by the dacC gene) is a low-molecular mass PBP clearly exhibiting in vitro DD-carboxypeptidase activity. We have solved the crystal structure of this protein alone and in complex with a peptide (D-alpha'-aminopymelyl-epsilon-D-alanyl-D-alanine) that mimics the C-terminal end of the Bacillus peptidoglycan stem peptide. PBP4a is composed of three domains: the penicillin-binding domain with a fold similar to the class A 13-lactamase structure and two domains inserted between the conserved motifs 1 and 2 characteristic of the penicillin-recognizing enzymes. The soaking of PBP4a in a solution Of D-alpha-aminopymelyl-epsilon-D-alanyl-D-alanine resulted in an adduct between PBP4a and a D-alpha-aminopimelyl-epsilon-D-alanine dipeptide and an unbound D-alanine, i.e. the products of acylation of PBP4a by D-alpha-aminopymelyl-epsilon-D-alanyl-D-alanine with the release of a D-alanine. The adduct also reveals a binding pocket specific to the diaminopimelic acid, the third residue of the peptidoglycan stem pentapeptide of B. subtilis. This pocket is specific for this class of PBPs. (C) 2007 Elsevier Ltd. All rights reserved