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Objectives: The identification and interpretation of skeletal trauma is an important topic in osteoarchaeology, forensic anthropology and palaeosciences. Trauma analysis is a fast‐moving sub‐discipline with constantly evolving methodological approaches. This paper describes the process of a particular form of fracturing that propagates specifically from the floor of cut marks and proposes new terminology for this subset of fractures. Materials and Methods: This terminological gap was identified during the re‐examination of remains from a minimum of 52 decapitated individuals (52 post‐cranial and 47 cranial remains) found in a mass grave from the 10th–11th century CE on Ridgeway Hill near Weymouth in Dorset (UK) in 2009. Originally analyzed by Oxford Archaeology Ltd., all individuals in this collection were re‐appraised using digital technology to test new techniques for this study. Results: During this investigation, it has become apparent that the length of chop marks can be overestimated during some conventional analysis because the chop transitions into a fracture propagating from the floor of the chop mark. Discussion: To increase awareness of these fractures, the term residual energy dispersal (RED) fractures is proposed as these are distinct from other radiating fractures arising from sharp‐blunt‐force trauma. The ability to distinguish RED fractures from others has the potential to contribute to the identification of previously unidentified chop marks and to the interpretation of events surrounding an injury. Research Highlights: The term "Residual Energy Dispersal" (RED) fracturing is proposed for fractures propagating from the base of a cut mark in sharp‐force or sharp‐blunt‐force trauma analysis.These fractures can make chop marks look longer than they truly are and therefore they can impact the interpretation of the events that caused the trauma. [ABSTRACT FROM AUTHOR]

In the marine environment agar degradation is assured by bacteria that contain large agarolytic systems with enzymes acting in various endo‐ and exo‐modes. Agarase A (AgaA) is an endo‐glycoside hydrolase of family 16 considered to initiate degradation of agarose. Agaro‐oligosaccharide binding at a unique surface binding site (SBS) in AgaA from Zobellia galactanivorans was investigated by computational methods in conjunction with a structure/sequence guided approach of site‐directed mutagenesis probed by surface plasmon resonance binding analysis of agaro‐oligosaccharides of DP 4‐10. The crystal structure has shown that agaro‐octaose interacts via H‐bonds and aromatic stacking along 7 subsites (L through R) of the SBS in the inactive catalytic nucleophile mutant AgaA‐E147S. D271 is centrally located in the extended SBS where it forms H‐bonds to galactose and 3,6‐anhydrogalactose residues of agaro‐octaose at subsites O and P. We propose D271 is a key residue in ligand binding to the SBS. Thus AgaA‐E147S/D271A gave slightly decreasing KD values from 625 ± 118 to 468 ± 13 μM for agaro‐hexaose, ‐octaose, and ‐decaose, which represent 3‐ to 4‐fold reduced affinity compared with AgaA‐E147S. Molecular dynamics simulations and interaction analyses of AgaA‐E147S/D271A indicated disruption of an extended H‐bond network supporting that D271 is critical for the functional SBS. Notably, neither AgaA‐E147S/W87A nor AgaA‐E147S/W277A, designed to eliminate stacking with galactose residues at subsites O and Q, respectively, were produced in soluble form. W87 and W277 may thus control correct folding and structural integrity of AgaA. [ABSTRACT FROM AUTHOR]

The study of anatomy in England during the 18th and 19th century has become infamous for bodysnatching from graveyards to provide a sufficient supply of cadavers. However, recent discoveries have improved our understanding of how and why anatomy was studied during the enlightenment, and allow us to see the context in which dissection of the human body took place. Excavations of infirmary burial grounds and medical school cemeteries, study of hospital archives, and analysis of the content of surviving anatomical collections in medical museums enables us to re-evaluate the field from a fresh perspective. The pathway from a death in poverty, sale of the corpse to body dealer, dissection by anatomist or medical student, and either the disposal and burial of the remains or preservation of teaching specimens that survive today in medical museums is a complex and fascinating one. [ABSTRACT FROM AUTHOR]

NMR-monitored pH titration experiments are routinely used to measure site-specific protein p Ka values. Accurate experimental p Ka values are essential in dissecting enzyme catalysis, in studying the pH-dependence of protein stability and ligand binding, in benchmarking p Ka prediction algorithms, and ultimately in understanding electrostatic effects in proteins. However, due to the complex ways in which pH-dependent electrostatic and structural changes manifest themselves in NMR spectra, reported apparent p Ka values are often dependent on the way that NMR pH-titration curves are analyzed. It is therefore important to retain the raw NMR spectroscopic data to allow for documentation and possible re-interpretation. We have constructed a database of primary NMR pH-titration data, which is accessible via a web interface. Here, we report statistics of the database contents and analyze the data with a global perspective to provide guidelines on best practice for fitting NMR titration curves. Titration_DB is available at . Proteins 2010. © 2009 Wiley-Liss, Inc. [ABSTRACT FROM AUTHOR]

A strain of Vibrio cholerae, which had been engineered to express high levels of the non-toxic B subunit (EtxB) of Escherlchia coli heat-labile enterotoxin, was subjected to transposon (TnphoA) mutagenesis. Two chromosomal TnphoA insertion mutations of the strain were isolated that showed a severe defect in the amount of EtxB produced. The loci disrupted by TnphoA in the two mutant derivatives were cloned and sequenced, and this revealed that the transposon had inserted at different sites in the same gene. The open reading frame of the gene predicts a 200-aminoacid exported protein, with a Cys-X-X-Cys motif characteristic of thioredoxin, protein disulphide isomerase, and DsbA (a periplasmic protein required for disulphide bond formation in E. coli). The V. cholerae protein exhibited 40% identity with the DsbA protein of E. coli, including 90% identity in the region of the active-site motif. Introduction of a plasmid encoding E. coli DsbA into the V. cholerae TnphoA derivatives was found to restore enterotoxin formation, whilst expression of Etx or EtxB in a dsbA mutant of E. coli confirmed that DsbA is required for enterotoxin formation In E. coll. These results suggest that, since each EtxB subunit contains a single intramolecular disulphide bond, a transient intermolecular interaction with DsbA occurs during toxin subunit folding which catalyses formation of the disulphide in vivo. [ABSTRACT FROM AUTHOR]