The Effect of Drying Temperature on Physical Properties of Thin Gelatin Films

The molecular morphology of thin gelatin films, controlled through the casting temperature, was monitored by wide angle X-ray diffraction (WAXD) and differential scanning calorimetry (DSC). Gelatin films dried at lower temperatures had a markedly higher crystalline or helical structure with a slightly higher T_g and lower ΔC_p compared with hot dried films, which had a more coiled structure. The relationship between molecular morphology and gelatin-water interaction in terms of hydration behavior and water diffusivity was assessed using dynamic vapor sorption (DVS). The sorption capacity increased and the level of hysteresis decreased with increasing the degree of crystallinity. The difference in the aging behavior of the films was explained in terms of the difference between the glass transition and aging temperatures, (Tg – Ta).     

The Physical Properties and Self‐Assembly Potential of the RFFFR Peptide

The self‐assembly of fibers from peptides has attracted a tremendous amount of attention due to its many applications, such as in drug‐delivery systems, in tissue engineering, and in electronic devices. Recently, the self‐assembly potential of the designer peptide RFFFR has been reported. Here it is experimentally verified that the peptide forms fibers that are entangled and form solid spheres without water inside. Upon dilution below the critical fiber concentration, the fibers untangle and become totally separated prior to dissolution. These structures readily bind thioflavin T, resulting in a characteristic change in fluorescent properties consistent with β‐sheet‐rich amyloid structures with aromatic/hydrophobic grooves. The circular dichroism spectroscopy data are dominated by a π→π* transition, thus indicating that the fibers are stabilized by π‐stacking. Contrary to what was expected, the dissolution of the spheres/fibers results in increasing fluorescence anisotropy over time. This is explained in terms of HomoFRET between phenylalanine residues with a T‐shaped π‐stacking mode, which was determined in another study to be the dominant mode through atomistic simulations and semiempirical calculations. Kelvin probe force microscopy measurements indicate that the spheres and fibers have a conductivity comparable to that of gold. Hence, these self‐assembled structures might be applicable in organic solid‐state electronic devices. The dissolution properties of the spheres further suggest that they might be used as drug‐delivery systems.     

Atomic force microscopy study of the interaction of Fusarium solani pisi cutinase with lipid surfaces

We present an atomic force microscopy (AFM) study of a supported triacylglyceride multilayer phase and its interaction with lipolytic enzyme cutinase from Fusarium solani pisi. The multilayer triacylglyceride phase of coconut oil showed a rippled surface structure in the AFM images. Upon enzymatic degradation of the triacylglyceride phase, the ripple structure vanished rapidly. The apparent catalytic rate constants could be estimated based on the AFM image information. Interestingly, in one sample we observed what we interpret as a recurrent structural collapse of the cavity dug out by the protein. We interpret the cavities seen in the AFM images as molten surfaces or surface holes filled with liquidified phase containing product molecules, which appear transparent during the image recording.     

PH-dependent self-assembly of the short Surfactant-like peptide KA6

Self-assembly of amphiphilic peptides designed during the last ten years by different research groups lead to a large variety of 3D-structures that already found applications in e.g., for stabilization of large protein complexes, cell culturing systems etc. We present synthesis and characterization of a novel amphiphilic peptide KA6 that exhibits clear charge separation controllable by the pH of the environment. The self-assembly in this system is largely governed by electrostatic interaction, thus a change in pH will not only lead to a change in critical micellar concentration (CMC) of the peptide but also to the changes in micellar structure as revealed by atomic force microscopy (AFM) and circular dichroism (CD) study. At basic pH the micellar structure inverts exposing the opposite end of the peptide chain to the solution. This interesting phenomenon could provide basis for novel pH sensitive materials including drug delivery and controlled release systems.     

Elucidation of protein aggregation in frozen cod and haddock by transmission electron microscopy/immunocytochemistry,light microscopy and atomic force microscopy

Polyclonal antibodies raised to both native cod myosin and actin as well as to aggregated proteins obtained from frozen cod stored for 11 months at ?10 °C were used to investigate disposition of muscle proteins in frozen cod and haddock fillets by transmission electron microscopy. Specimens from cod and haddock fillets, stored at ?10 °C, treated with anti‐aggregate antibody as the primary antibody, showed significantly more gold particles, especially around the protein aggregates and muscle fibres compared with fish stored at ?30 °C. Samples that were treated with anti‐myosin or anti‐actin antibody showed opposite results. Similar binding properties were observed in ELISA experiments involving the reaction of actin and myosin to both native and aggregate antibodies; thus immunological tests can be used for monitoring aggregate and texture changes in frozen stored fish. In addition, atomic force microscopy images obtained from cod muscle also indicated structural changes in frozen cod muscle proteins. The mica surface was covered with a continuous layer of muscle proteins comprising mainly small globular particles and a few large particles for the control cod sample stored at ?30 °C for 11 months. In contrast, cod fillets stored at ?10 °C showed a thin layer of proteins with small holes and an increased number of large particles denoting aggregates. Formation of ice crystals between the muscle fibres of frozen cod and haddock muscle was monitored without thawing by light microscopy at ?20 °C. The micrographs showed a greater proportion of large ice crystals and extensive protein fibre changes in fillets stored at ?10 °C compared with the control at ?30 °C. Copyright © 2004 Society of Chemical Industry     

Semi-automatic knowledge extraction, representation and context-sensitive intelligent retrieval of video content using collateral context modelling with scalable ontological networks

Automatic indexing and retrieval of digital data poses major challenges. The main problem arises from the ever increasing mass of digital media and the lack of efficient methods for indexing and retrieval of such data based on the semantic content rather than keywords. To enable intelligent web interactions, or even web filtering, we need to be capable of interpreting the information base in an intelligent manner. For a number of years research has been ongoing in the field of ontological engineering with the aim of using ontologies to add such (meta) knowledge to information. In this paper, we describe the architecture of a system (Dynamic REtrieval Analysis and semantic metadata Management (DREAM)) designed to automatically and intelligently index huge repositories of special effects video clips, based on their semantic content, using a network of scalable ontologies to enable intelligent retrieval. The DREAM Demonstrator has been evaluated as deployed in the film post-production phase to support the process of storage, indexing and retrieval of large data sets of special effects video clips as an exemplar application domain. This paper provides its performance and usability results and highlights the scope for future enhancements of the DREAM architecture which has proven successful in its first and possibly most challenging proving ground, namely film production, where it is already in routine use within our test bed Partners’ creative processes.     

The effect of shear on the rheology and structure of heat‐induced whey protein gels

The influence of mechanical shearing on the small deformation properties and microstructure of heat‐induced whey protein gel has been studied. The viscoelastic properties of these gels at different concentrations of 10% and 20% (w/w) exposed to different shear rates of 0, 50, 100, 200 and 500 s^?1 during gelation were measured using dynamic oscillatory rheometry. The structure of both the shear treated and unsheared gels was then investigated using light microscopy. The results showed that the storage modulus of the gels at both concentrations was increased by increasing the shear rate exposure during gelation while the shear‐treated gels were more elastic and showed frequency‐independent behaviour. As the total protein concentration of the gel increased, the viscoelastic properties of the gels also increased significantly and the gels showed greater elasticity. The gels obtained from the higher shear rate exposure were stronger with higher elastic moduli at both protein concentrations. Images of the gels obtained using light microscopy showed that shearing resulted in phase separation and some aggregation in the structure of the gels at both concentrations. However, the shearing rates applied in this study were not enough to cause aggregation breakdown in the gel network.     

Wind Field in Greater Tehran Area（GTA） in Autumn Season

IntroductionTehran, the Capital of I.R. Iran, is a huge city with acurrent population more than 12 millions, and an area ofapproximately 2000 km', including its suburban. Itlocates at latitode 35" 31' north and longitllde sl" 19,east, in the south part of the Alborz Mountains andsurmunded by mountains from north-west, north, to eastand central desert of iran from west and south. Therefore,Tehran has upward slope from south to north and fromwest to east. There are only some hills (with compa…