Structural Principles (structural + principle)

Distribution by Scientific Domains


Selected Abstracts


Influence of Structural Principles on the Mechanics of a Biological Fiber-Based Composite Material with Hierarchical Organization: The Exoskeleton of the Lobster Homarus americanus

ADVANCED MATERIALS, Issue 4 2009
Helge-Otto Fabritius
Abstract The cuticle of the lobster Homarus americanus is a nanocomposite, such as most structural biological materials. It consists of a matrix of chitin-protein fibers associated with various amounts of crystalline and amorphous calcium carbonate in the rigid parts of the body, and is organized hierarchically at all length scales. One prominent design principle found in the hierarchical structure of such biological fibrous composite materials is the twisted plywood structure. In the lobster cuticle, it is formed by superimposing and gradually rotating planes of parallel aligned chitin-protein fibers. To adjust the mechanical properties to the requirements on the macroscopic level, the spatial arrangement and the grade of mineralization of the fibers can be modified. A second design principle of lobster cuticle is its honeycomb-like structure, generated by the well-developed pore canal system, whose twisted ribbon-shaped canals penetrate the cuticle perpendicular to its surface. Due to the hierarchical structure, the mechanical properties of the lobster cuticle have to be investigated at different length scales, which is essential for the understanding of the structure,mechanical function relations of mineralized tissues (e.g., potentially also bone and teeth). In order to investigate the influence of the structural principles on the mechanical properties on the macroscopic scale miniaturized tensile, compression, and shear tests were carried out to obtain integral mechanical data. Characterization of the microstructure included scanning electron microscopy (SEM) combined with energy dispersive X-ray (EDX) measurements. [source]


Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease

BRAIN PATHOLOGY, Issue 1 2007
Eckhard Mandelkow
Tau, a major microtubule-associated protein in brain, forms abnormal fibers in Alzheimer's disease and several other neurodegenerative diseases. Tau is highly soluble and adopts a natively unfolded structure in solution. In the paired helical filaments of Alzheimer's disease, small segments of tau adopt a ,-conformation and interact with other tau molecules. In the filament core, the microtubule-binding repeat region of tau has a cross-, structure, while the rest of the protein retains its largely unfolded structure and gives rise to the fuzzy coat of the filaments. [source]


Cluster Growing Through Ionic Aggregation: Synthesis and Structural Principles of Main Group Metal,Rich Nitrogen, Phosphorus and Arsenic Clusters

CHEMINFORM, Issue 26 2005
Matthias Driess
Abstract For Abstract see ChemInform Abstract in Full Text. [source]


Influence of Structural Principles on the Mechanics of a Biological Fiber-Based Composite Material with Hierarchical Organization: The Exoskeleton of the Lobster Homarus americanus

ADVANCED MATERIALS, Issue 4 2009
Helge-Otto Fabritius
Abstract The cuticle of the lobster Homarus americanus is a nanocomposite, such as most structural biological materials. It consists of a matrix of chitin-protein fibers associated with various amounts of crystalline and amorphous calcium carbonate in the rigid parts of the body, and is organized hierarchically at all length scales. One prominent design principle found in the hierarchical structure of such biological fibrous composite materials is the twisted plywood structure. In the lobster cuticle, it is formed by superimposing and gradually rotating planes of parallel aligned chitin-protein fibers. To adjust the mechanical properties to the requirements on the macroscopic level, the spatial arrangement and the grade of mineralization of the fibers can be modified. A second design principle of lobster cuticle is its honeycomb-like structure, generated by the well-developed pore canal system, whose twisted ribbon-shaped canals penetrate the cuticle perpendicular to its surface. Due to the hierarchical structure, the mechanical properties of the lobster cuticle have to be investigated at different length scales, which is essential for the understanding of the structure,mechanical function relations of mineralized tissues (e.g., potentially also bone and teeth). In order to investigate the influence of the structural principles on the mechanical properties on the macroscopic scale miniaturized tensile, compression, and shear tests were carried out to obtain integral mechanical data. Characterization of the microstructure included scanning electron microscopy (SEM) combined with energy dispersive X-ray (EDX) measurements. [source]


Breaking symmetry in protein dimers: Designs and functions

PROTEIN SCIENCE, Issue 1 2006
Jerry H. Brown
Abstract Symmetry, and in particular point group symmetry, is generally the rule for the global arrangement between subunits in homodimeric and other oligomeric proteins. The structures of fragments of tropomyosin and bovine fibrinogen are recently published examples, however, of asymmetric interactions between chemically identical chains. Their departures from strict twofold symmetry are based on simple and generalizable chemical designs, but were not anticipated prior to their structure determinations. The current review aims to improve our understanding of the structural principles and functional consequences of asymmetric interactions in proteins. Here, a survey of >100 diverse homodimers has focused on the structures immediately adjacent to the twofold axis. Five regular frameworks in ,-helical coiled coils and antiparallel ,-sheets accommodate many of the twofold symmetric axes. On the basis of these frameworks, certain sequence motifs can break symmetry in geometrically defined manners. In antiparallel ,-sheets, these asymmetries include register slips between strands of repeating residues and the adoption of different side-chain rotamers to avoid steric clashes of bulky residues. In parallel coiled coils, an axial stagger between the ,-helices is produced by clusters of core alanines. Such simple designs lead to a basic understanding of the functions of diverse proteins. These functions include regulation of muscle contraction by tropomyosin, blood clot formation by fibrin, half-of-site reactivity of caspase-9, and adaptive protein recognition in the matrix metalloproteinase MMP9. Moreover, asymmetry between chemically identical subunits, by producing multiple equally stable conformations, leads to unique dynamic and self-assembly properties. [source]


Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxins

CHEMICAL BIOLOGY & DRUG DESIGN, Issue 6 2004
B. Stec
Abstract:, We propose a molecular model for phospholipid membrane lysis by the ubiquitous plant toxins called thionins. Membrane lysis constitutes the first major effect exerted by these toxins that initiates a cascade of cytoplasmic events leading to cell death. X-ray crystallography, solution nuclear magnetic resonance (NMR) studies, small angle X-ray scattering and fluorescence spectroscopy provide evidence for the mechanism of membrane lysis. In the crystal structures of two thionins in the family, ,1 - and , -purothionins (MW: approximately 4.8 kDa), a phosphate ion and a glycerol molecule are modeled bound to the protein. 31P NMR experiments on the desalted toxins confirm phosphate-ion binding in solution. Evidence also comes from phospholipid partition experiments with radiolabeled toxins and with fluorescent phospholipids. This data permit a model of the phospholipid,protein complex to be built. Further, NMR experiments, one-dimensional (1D)- and two-dimensional (2D)-total correlation spectroscopy (TOCSY), carried out on the model compounds glycerol-3-phosphate (G3P) and short chain phospholipids, supported the predicted mode of phospholipid binding. The toxins' high positive charge, which renders them extremely soluble (>300 mg/mL), and the phospholipid-binding specificity suggest the toxin,membrane interaction is mediated by binding to patches of negatively charged phospholipids [phosphatidic acid (PA) or phosphatidyl serine (PS)] and their subsequent withdrawal. The formation of proteolipid complexes causes solubilization of the membrane and its lysis. The model suggests that the oligomerization may play a role in toxin's activation process and provides insight into the structural principles of protein,membrane interactions. [source]


Structure Formation Principles and Reactivity of Organolithium Compounds

CHEMISTRY - A EUROPEAN JOURNAL, Issue 14 2009
Viktoria
Abstract Organolithium chemistry! An overview of the structure formation principles and the strong structure,reactivity relationship of lithium organics is given. By means of the commonly used lithium bases the deaggregation of the oligomeric parent structures to small adducts is presented (see examples) and compared to the related chemistry of lithiosilanes. The structure,reactivity relationship is an important feature of organolithium compounds. The knowledge of the structure of reactive species is crucial for the elucidation of reaction mechanisms and the understanding of observed selectivities. This concept article gives an overview over the structural principles of lithium organics and their Lewis base coordinated complexes in the solid state. The transition from the oligomeric parent structures to smaller adducts, such as dimers and monomers, as well as special degrees of aggregation is presented. Besides the commonly used alkyllithium compounds, a short overview over the structural principles of the higher homologous silyllithium compounds is given. Moreover, the structure,reactivity relationship is depicted by means of the reactivity of the Lewis bases towards intramolecular decomposition reactions with the organolithium compound. Selected examples confirm the importance of structure elucidation for the understanding of mechanistic pathways and selectivities. [source]