An approach to high speed ship ride quality simulation

The high speeds attained by certain advanced surface ships result in a spectrum of motion which is higher in frequency than that of conventional ships. This fact along with the inclusion of advanced ride control features in the design of these ships resulted in an increased awareness of the need for ride criteria. Such criteria can be developed using data from actual ship operations in varied sea states or from clinical laboratory experiments. A third approach is to simulate ship conditions using measured or calculated ship motion data. Recent simulations have used data derived from a math model of Surface Effect Ship (SES) motion. The model in turn is based on equations of motion which have been refined with data from scale models and SES of up to 101 600-kg (100-ton) displacement. Employment of broad band motion emphasizes the use of the simulators as a design tool to evaluate a given ship configuration in several operational situations and also serves to provide data as to the overall effect of a given motion on crew performance and physiological status

Superantigen architecture: Functional decoration on a conserved scaffold

A defining and consistent feature of the bacterial superantigens from Staphylococcus aureus and Streptococcus pyogenes is their strongly conserved three-dimensional structure. Structural studies to date show that the array of more than 280 amino acid sequences known for superantigens (SAgs) and staphylococcal superantigen-like (SSL) proteins all have the same fold-a structure in which the same three-dimensional arrangement of α-helices and β-sheets is traced by each amino acid sequence, with the same topology (for recent reviews, see references 29 and 43). A typical SAg structure comprises two domains-an N-terminal β -barrel domain called an OB-fold (4, 25) and a C-terminal β-grasp domain in which a long α-helix packs on to a mixed parallel and antiparallel β-sheet. These two domains are traversed by an α-helix that lies at the N terminus of the protein and packs against the β-grasp domain, thus linking the N- and C-terminal domains

Impact of the Agricultural Sector on the Arkansas Economy in 2001

Agriculture has historically been one of Arkansas’ primary economic sectors. Agriculture is defined as the sum of agricultural production and processing activities unless otherwise specified. Agriculture contributes to the economy through direct agricultural production and value-added processing which generates economic activity in other parts of the economy

A (Thigh) Gap in the Law: Addressing Egregious Digital Manipulation of Celebrity Images

In 2012, world-renowned supermodel Coco Rocha agreed to be photographed for the cover of one of Elle’s magazine publications, Elle Brazil. Rocha posed for the pictures in a dress with significant cutouts, covered only by a sheer layer of skin-toned fabric. In keeping with her firm policy of no full or partial nudity, Rocha wore a bodysuit underneath the dress to limit her exposure. When Elle published the magazine, the final product shocked Rocha; the magazine had altered the image to remove her bodysuit, giving the impression Rocha had shown more skin than she in fact had. Rocha took to her personal blog to express her frustration and disappointment at Elle’s disrespectful editing. Unfortunately, this problem is not limited to Rocha—she is only one of many models and celebrities who have expressed frustration about excessive image manipulation. The right to privacy and right of publicity protect individuals’ abilities to control when their identities are promulgated and when their identities are commercially used, respectively. But these rights only protect people’s decisions regarding when their image is shared by requiring permission; if permission has been granted, the right to privacy and right of publicity do not address individuals’ rights to control how their image is subsequently portrayed. This Note identifies gaps in current relevant law and the resulting need to recognize individuals’ right to control not just when their image is used commercially or otherwise, but how it is used. Part I introduces the right to privacy and the right of publicity, and explains the current state of the law in those areas as it applies to digitally manipulated celebrity images. Part II then offers a critical analysis of current law and evaluates whether it effectively allows individuals to control how their identity is used. Finally, Part III proposes solutions to the law’s shortcomings in an attempt to better protect individuals’ right to determine how their identity is publicly represented

Infinite stacking of alternating polyfluoroaryl rings and bromide anions

The crystal structure of 1-(4-bromo-2,3,5,6-tetrafluorophenyl)-3-benzylimidazolium bromide comprises columns of parallel bromotetrafluorophenyl rings with an interplanar distance of 6.936(6) Å separated by bromide anions

Expression and purification of an adenylation domain from a eukaryotic nonribosomal peptide synthetase: Using structural genomics tools for a challenging target

Nonribosomal peptide synthetases (NRPSs) are large multimodular and multidomain enzymes that are involved in synthesising an array of molecules that are important in human and animal health. NRPSs are found in both bacteria and fungi but most of the research to date has focused on the bacterial enzymes. This is largely due to the technical challenges in producing active fungal NRPSs, which stem from their large size and multidomain nature. In order to target fungal NRPS domains for biochemical and structural characterisation, we tackled this challenge by using the cloning and expression tools of structural genomics to screen the many variables that can influence the expression and purification of proteins. Using these tools we have screened 32 constructs containing 16 different fungal NRPS domains or domain combinations for expression and solubility. Two of these yielded soluble protein with one, the third adenylation domain of the SidN NRPS (SidNA3) from the grass endophyte Neotyphodium lolii, being tractable for purification using Ni-affinity resin. The initial purified protein exhibited poor solution behaviour but optimisation of the expression construct and the buffer conditions used for purification, resulted in stable recombinant protein suitable for biochemical characterisation, crystallisation and structure determination

Structural analysis of the GH43 enzyme Xsa43E from Butyrivibrio proteoclasticus

The rumen of dairy cattle can be thought of as a large, stable fermentation vat and as such it houses a large and diverse community of microorganisms. The bacterium Butyrivibrio proteoclasticus is a representative of a significant component of this microbial community. It is a xylan-degrading organism whose genome encodes a large number of open reading frames annotated as fibre-degrading enzymes. This suite of enzymes is essential for the organism to utilize the plant material within the rumen as a fuel source, facilitating its survival in this competitive environment. Xsa43E, a GH43 enzyme from B. proteoclasticus, has been structurally and functionally characterized. Here, the structure of selenomethionine-derived Xsa43E determined to 1.3 Å resolution using single-wavelength anomalous diffraction is reported. Xsa43E possesses the characteristic five-bladed β-propeller domain seen in all GH43 enzymes. GH43 enzymes can have a range of functions, and the functional characterization of Xsa43E shows it to be an arabinofuranosidase capable of cleaving arabinose side chains from short segments of xylan. Full functional and structural characterization of xylan-degrading enzymes will aid in creating an enzyme cocktail that can be used to completely degrade plant material into simple sugars. These molecules have a range of applications as starting materials for many industrial processes, including renewable alternatives to fossil fuels

Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU

Hsc66 and Hsc20 comprise a specialized chaperone system important for the assembly of iron-sulfur clusters in Escherchia coli. Only a single substrate, the Fe/S template protein IscU, has been identified for the Hsc66/Hsc20 system, but the mechanism by which Hsc66 selectively binds IscU is unknown. We have investigated Hsc66 substrate specificity using phage display and a peptide array of IscU. Screening of a heptameric peptide phage display library revealed that Hsc66 prefers peptides with a centrally located Pro-Pro motif. Using a cellulose-bound peptide array of IscU we determined that Hsc66 interacts specifically with a region (residues 99-103, LPPVK) that is invariant among all IscU family members. A synthetic peptide (ELPPVKIHC) corresponding to IscU residues 98-106 behaves in a similar manner to native IscU, stimulating the ATPase activity of Hsc66 with similar affinity as IscU, preventing Hsc66 suppression of bovine rhodanese aggregation, and interacting with the peptide-binding domain of Hsc66. Unlike native IscU, however, the synthetic peptide is not bound by Hsc20 and does not synergistically stimulate Hsc66 ATPase activity with Hsc20. Our results indicate that Hsc66 and Hsc20 recognize distinct regions of IscU and further suggest that Hsc66 will not bind LPPVK motifs with high affinity in vivo unless they are in the context of native IscU and can be directed to Hsc66 by Hsc20

The Structure of the Oligomerization Domain of Lsr2 from Mycobacterium tuberculosis Reveals a Mechanism for Chromosome Organization and Protection

Lsr2 is a small DNA-binding protein present in mycobacteria and related actinobacteria that regulates gene expression and influences the organization of bacterial chromatin. Lsr2 is a dimer that binds to AT-rich regions of chromosomal DNA and physically protects DNA from damage by reactive oxygen intermediates (ROI). A recent structure of the C-terminal DNA-binding domain of Lsr2 provides a rationale for its interaction with the minor groove of DNA, its preference for AT-rich tracts, and its similarity to other bacterial nucleoid-associated DNA-binding domains. In contrast, the details of Lsr2 dimerization (and oligomerization) via its N-terminal domain, and the mechanism of Lsr2-mediated chromosomal cross-linking and protection is unknown. We have solved the structure of the N-terminal domain of Lsr2 (N-Lsr2) at 1.73 Å resolution using crystallographic ab initio approaches. The structure shows an intimate dimer of two ß-ß-a motifs with no close homologues in the structural databases. The organization of individual N-Lsr2 dimers in the crystal also reveals a mechanism for oligomerization. Proteolytic removal of three N-terminal residues from Lsr2 results in the formation of an anti-parallel β-sheet between neighboring molecules and the formation of linear chains of N-Lsr2. Oligomerization can be artificially induced using low concentrations of trypsin and the arrangement of N-Lsr2 into long chains is observed in both monoclinic and hexagonal crystallographic space groups. In solution, oligomerization of N-Lsr2 is also observed following treatment with trypsin. A change in chromosomal topology after the addition of trypsin to full-length Lsr2-DNA complexes and protection of DNA towards DNAse digestion can be observed using electron microscopy and electrophoresis. These results suggest a mechanism for oligomerization of Lsr2 via protease-activation leading to chromosome compaction and protection, and concomitant down-regulation of large numbers of genes. This mechanism is likely to be relevant under conditions of stress where cellular proteases are known to be upregulated