Automatic algorithm for the characterization of sweat ducts in a three-dimensional fingerprint

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.

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convergent-beam diffraction from surfaces

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100125208 ◽

1987 ◽

Vol 45 ◽

pp. 30-33

Author(s):

J. A. Eades ◽

A. E. Smith ◽

D. F. Lynch

Keyword(s):

Reciprocal Lattice ◽

Three Dimensional ◽

Grazing Incidence ◽

Three Dimensions ◽

Plane Figure ◽

Transmission Electron ◽

Convergent Beam ◽

Beam Patterns ◽

Beam Diffraction

It is quite simple (in the transmission electron microscope) to obtain convergent-beam patterns from the surface of a bulk crystal. The beam is focussed onto the surface at near grazing incidence (figure 1) and if the surface is flat the appropriate pattern is obtained in the diffraction plane (figure 2). Such patterns are potentially valuable for the characterization of surfaces just as normal convergent-beam patterns are valuable for the characterization of crystals.There are, however, several important ways in which reflection diffraction from surfaces differs from the more familiar electron diffraction in transmission.GeometryIn reflection diffraction, because of the surface, it is not possible to describe the specimen as periodic in three dimensions, nor is it possible to associate diffraction with a conventional three-dimensional reciprocal lattice.

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Construction of plastic contact deformation maps on ceramics: a case study on aluminum nitride

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100165641 ◽

1996 ◽

Vol 54 ◽

pp. 636-637

Author(s):

D. L. Callahan

Keyword(s):

Plastic Deformation ◽

Aluminum Nitride ◽

Mechanical Response ◽

Three Dimensional ◽

Bright Field Image ◽

Perfectly Plastic ◽

Contrast Analysis ◽

Deformation Patterns

Modern polishing, precision machining and microindentation techniques allow the processing and mechanical characterization of ceramics at nanometric scales and within entirely plastic deformation regimes. The mechanical response of most ceramics to such highly constrained contact is not predictable from macroscopic properties and the microstructural deformation patterns have proven difficult to characterize by the application of any individual technique. In this study, TEM techniques of contrast analysis and CBED are combined with stereographic analysis to construct a three-dimensional microstructure deformation map of the surface of a perfectly plastic microindentation on macroscopically brittle aluminum nitride.The bright field image in Figure 1 shows a lg Vickers microindentation contained within a single AlN grain far from any boundaries. High densities of dislocations are evident, particularly near facet edges but are not individually resolvable. The prominent bend contours also indicate the severity of plastic deformation. Figure 2 is a selected area diffraction pattern covering the entire indentation area.

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Characterization of a monolayer graphitic structure

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100171535 ◽

1994 ◽

Vol 52 ◽

pp. 760-761

Author(s):

X. Lin ◽

X. K. Wang ◽

V. P. Dravid ◽

J. B. Ketterson ◽

R. P. H. Chang

Keyword(s):

Three Dimensional ◽

Single Layer ◽

Synthesis Process ◽

Graphitic Structure ◽

Positive Gaussian Curvature ◽

Graphitic Sheet ◽

Structural And Electronic Properties ◽

New Material ◽

Hexagonal Network

For small curvatures of a graphitic sheet, carbon atoms can maintain their preferred sp2 bonding while allowing the sheet to have various three-dimensional geometries, which may have exotic structural and electronic properties. In addition the fivefold rings will lead to a positive Gaussian curvature in the hexagonal network, and the sevenfold rings cause a negative one. By combining these sevenfold and fivefold rings with sixfold rings, it is possible to construct complicated carbon sp2 networks. Because it is much easier to introduce pentagons and heptagons into the single-layer hexagonal network than into the multilayer network, the complicated morphologies would be more common in the single-layer graphite structures. In this contribution, we report the observation and characterization of a new material of monolayer graphitic structure by electron diffraction, HREM, EELS.The synthesis process used in this study is reported early. We utilized a composite anode of graphite and copper for arc evaporation in helium.

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Characterization of Monoclonal Anti-human Factor VII Antibody (B101/B1) that Recognized Three-dimensional Structures near Arg at Position 79 in the First EGF-like Domain

Thrombosis and Haemostasis ◽

10.1055/s-0037-1614229 ◽

1998 ◽

Vol 79 (01) ◽

pp. 104-109 ◽

Cited By ~ 6

Author(s):

Osamu Takamiya

Keyword(s):

Monoclonal Antibodies ◽

Tissue Factor ◽

Human Factor ◽

Solid Phase ◽

Three Dimensional ◽

Coagulation Factors ◽

Factor Vii ◽

Dimensional Structure ◽

Epidermal Growth

SummaryMurine monoclonal antibodies (designated hVII-B101/B1, hVIIDC2/D4 and hVII-DC6/3D8) directed against human factor VII (FVII) were prepared and characterized, with more extensive characterization of hVII-B101/B1 that did not bind reduced FVIIa. The immunoglobulin of the three monoclonal antibodies consisted of IgG1. These antibodies did not inhibit procoagulant activities of other vitamin K-dependent coagulation factors except FVII and did not cross-react with proteins in the immunoblotting test. hVII-DC2/D4 recognized the light chain after reduction of FVIIa with 2-mercaptoethanol, and hVIIDC6/3D8 the heavy chain. hVII-B101/B1 bound FVII without Ca2+, and possessed stronger affinity for FVII in the presence of Ca2+. The Kd for hVII-B101/B1 to FVII was 1.75 x 10–10 M in the presence of 5 mM CaCl2. The antibody inhibited the binding of FVII to tissue factor in the presence of Ca2+. hVII-B101/B1 also inhibited the activation of FX by the complex of FVIIa and tissue factor in the presence of Ca2+. Furthermore, immunoblotting revealed that hVII-B101/B1 reacted with non-reduced γ-carboxyglutaminic acid (Gla)-domainless-FVII and/or FVIIa. hVII-B101/B1 showed a similar pattern to that of non-reduced proteolytic fragments of FVII by trypsin with hVII-DC2/D4 on immunoblotting test. hVII-B101/B1 reacted differently with the FVII from the dysfunctional FVII variant, FVII Shinjo, which has a substitution of Gln for Arg at residue 79 in the first epidermal growth factor (1st EGF)-like domain (Takamiya O, et al. Haemosta 25, 89-97,1995) compared with normal FVII, when used as a solid phase-antibody for ELISA by the sandwich method. hVII-B101/B1 did not react with a series of short peptide sequences near position 79 in the first EGF-like domain on the solid-phase support for epitope scanning. These results suggested that the specific epitope of the antibody, hVII-B101/B1, was located in the three-dimensional structure near position 79 in the first EGF-like domain of human FVII.

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Thermal characterization of ABS-Graphene blended three dimensional printed functional prototypes for electro chemical energy storage

International Journal of Computational Physics Series ◽

10.29167/a1i1p1-11 ◽

2018 ◽

Vol 1 (1) ◽

pp. 1-11 ◽

Cited By ~ 1

Author(s):

Kamaljit Singh Boparai ◽

Rupinder Singh

Keyword(s):

Energy Storage ◽

Structural Changes ◽

Fused Deposition Modeling ◽

Morphological Changes ◽

Three Dimensional ◽

Thermal Characterization ◽

Chemical Energy ◽

Flow Index ◽

Fused Deposition

This study highlights the thermal characterization of ABS-Graphene blended three dimensional (3D) printed functional prototypes by fused deposition modeling (FDM) process. These functional prototypes have some applications as electro-chemical energy storage devices (EESD). Initially, the suitability of ABS-Graphene composite material for FDM applications has been examined by melt flow index (MFI) test. After establishing MFI, the feedstock filament for FDM has been prepared by an extrusion process. The fabricated filament has been used for printing 3D functional prototypes for printing of in-house EESD. The differential scanning calorimeter (DSC) analysis was conducted to understand the effect on glass transition temperature with the inclusion of Graphene (Gr) particles. It has been observed that the reinforced Gr particles act as a thermal reservoir (sink) and enhances its thermal/electrical conductivity. Also, FT-IR spectra realized the structural changes with the inclusion of Gr in ABS matrix. The results are supported by scanning electron microscopy (SEM) based micrographs for understanding the morphological changes.

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Faculty Opinions recommendation of RNA CoSSMos: Characterization of Secondary Structure Motifs--a searchable database of secondary structure motifs in RNA three-dimensional structures.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.13411018.14782140 ◽

2011 ◽

Author(s):

Martin Egli

Keyword(s):

Secondary Structure ◽

Three Dimensional ◽

Searchable Database

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In Silico Identification and Molecular Characterization of Extracellular Cathepsin L Proteases from Giardia duodenalis

Current Proteomics ◽

10.2174/1570164617666191016170628 ◽

2020 ◽

Vol 17 (4) ◽

pp. 342-351

Author(s):

Sergio A. Durán-Pérez ◽

José G. Rendón-Maldonado ◽

Lucio de Jesús Hernandez-Diaz ◽

Annete I. Apodaca-Medina ◽

Maribel Jiménez-Edeza ◽

...

Keyword(s):

In Silico ◽

Cathepsin L ◽

Three Dimensional ◽

Giardia Duodenalis ◽

Evolutionary Genetics ◽

Extracellular Proteins ◽

In Silico Identification ◽

Dimensional Models ◽

Three Dimensional Models

Background: The protozoan Giardia duodenalis, which causes giardiasis, is an intestinal parasite that commonly affects humans, mainly pre-school children. Although there are asymptomatic cases, the main clinical features are chronic and acute diarrhea, nausea, abdominal pain, and malabsorption syndrome. Little is currently known about the virulence of the parasite, but some cases of chronic gastrointestinal alterations post-infection have been reported even when the infection was asymptomatic, suggesting that the cathepsin L proteases of the parasite may be involved in the damage at the level of the gastrointestinal mucosa. Objective: The aim of this study was the in silico identification and characterization of extracellular cathepsin L proteases in the proteome of G. duodenalis. Methods: The NP_001903 sequence of cathepsin L protease from Homo sapienswas searched against the Giardia duodenalisproteome. The subcellular localization of Giardia duodenaliscathepsin L proteases was performed in the DeepLoc-1.0 server. The construction of a phylogenetic tree of the extracellular proteins was carried out using the Molecular Evolutionary Genetics Analysis software (MEGA X). The Robetta server was used for the construction of the three-dimensional models. The search for possible inhibitors of the extracellular cathepsin L proteases of Giardia duodenaliswas performed by entering the three-dimensional structures in the FINDSITEcomb drug discovery tool. Results: Based on the amino acid sequence of cathepsin L from Homo sapiens, 8 protein sequences were identified that have in their modular structure the Pept_C1A domain characteristic of cathepsins and two of these proteins (XP_001704423 and XP_001704424) are located extracellularly. Threedimensional models were designed for both extracellular proteins and several inhibitory ligands with a score greater than 0.9 were identified. In vitrostudies are required to corroborate if these two extracellular proteins play a role in the virulence of Giardia duodenalisand to discover ligands that may be useful as therapeutic targets that interfere in the mechanism of pathogenesis generated by the parasite. Conclusion: In silicoanalysis identified two proteins in the Giardia duodenalisprotein repertoire whose characteristics allowed them to be classified as cathepsin L proteases, which may be secreted into the extracellular medium to act as virulence factors. Three-dimensional models of both proteins allowed the identification of inhibitory ligands with a high score. The results suggest that administration of those compounds might be used to block the endopeptidase activity of the extracellular cathepsin L proteases, interfering with the mechanisms of pathogenesis of the protozoan parasite Giardia duodenalis.

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