Dumbbell-shaped structures

The evidence of interference microscopy nicely correlates with the models of crystallization, which in the case of SAPO-5 favor a pencil-like crystallization core [79,80], while in CrAPO-5 crystalUzation proceeds via the formation of dumbbell-shaped structures [81,82]. In no case coifid a nanoporous material with the desired structure of microscopic, ideal macaronis be identified. The appearing dramatic deviation from an ideal channel structure excludes the appHcation of simple model assiunptions for interpretation of the time evolution of the concentration profiles, hi fact, in [83] the experimentally monitored concentration profiles during... 

Figure 35.S Mechanically bonded nucleic acid architectures consisting of ss- and ds circular DMAs, (a) Strand invasion of the ss DNA (blue) at an A+T-rich sequence of supercoiled ds plasmid DNA. (Adapted from Ref. [50]) (b) Catenated DNA structure of a ds plasmid DNA and an ss circular DNA. (Adapted from Ref [51]) (c) Dumbbell-shaped structure consisting of...

On the other hand, the dumbbell-shaped structure does not interfere with the specificity of R-ODN, but is still less stable in serum than S-ODN incubation with 5% fetal bovine serum for 24 h completely degraded R-ODN, while S-ODN remained almost intact [14]. 

The x-ray structure of free calmodulin was determined by the group of Charles Bugg, University of Alabama. It is a dumbbell-shaped molecule... 

An atom consists of a positively charged nucleus surrounded by one or more negatively charged electrons. The electronic structure of an atom can be described by a quantum mechanical wave equation, in which electrons are considered to occupy orbitals around the nucleus. Different orbitals have different energy levels and different shapes. For example, s orbitals are spherical and p orbitals are dumbbell-shaped. The ground-state electron configuration of an... 

Actin is a 42 kDa bent dumbbell-shaped globular monomer which is found in most eukaryotic cells. It is the primary protein of the thin (or actin) filaments. Also, by mass or molarity, actin is the largest constituent of the contractile apparatus, actually reaching millimolar concentrations. Actins from different sources seem to be more similar than myosins from the same sources. Actin binds ATP which is hydrolyzed to ADP, if the monomeric actin polymerizes. The backbone structure of the actin filament is a helix formed by two linear strands of polymerized actins like two strings of actin beads entwined. 

The superstructure of smooth muscle actin filaments is differentiated from those of striated muscle by the absence of the troponins and the lateral organization by association of the filaments with dense bodies instead of with the Z-line. How these differences are encoded is again not at all clear. However, the myofibrillar structure and the alignment of the alternating actin and myosin filaments is apparently due primarily to dense bodies and the actin-actinin macrostructures. As the bent dumbbell shaped actins assemble into filaments they are all oriented in the same direction. The S-1 fragments of myosin will bind to actin filaments in vitro and in... 

Hie chromatinic structures in E. coli from old cultures were too small to be resolved accurately. After transfer to fresh medium the chromatinic structures increased in size and gave rise to short, often dumbbell-shaped rods or chromosomes, which multiplied by splitting lengthwise in a plane more or less parallel to the short axis of the cell. A single cell of E. coli contained one chromatinic body or one or two pairs of these representing primary and secondary division products. 

For Elg2Se03 three modifications have been described.133 They all contain dumbbell-shaped EIg22+ ions that are linked by the selenite ions. A common feature of all crystal structures is the formation of channels, which obviously incorporate the lone electron pairs of the selenite ions. 

Calmodulin Structure by X-Ray and NMR. Babu and co-workers published the first X-ray crystallographic structure of Ca " -saturated mammalian calmodulin in 1986 (PDB ascension number 3CLN). As can be seen in Figure 6.21, the molecule is dumbbell-shaped, with an overall length of 65 A. There are two two-EF-hand domains or lobes— N-terminal, residues 5-73 and C-terminal, residues 74-148—connected by a central seven-turn a-helix. The center part of the connecting helix is unwound between residues asp78 and... 

The possibility of this binding mode was shown recently with the synthesis and structural analysis of the dumbbell-shaped bis-fullerene complexes of molybdenum and timgsten. The X-ray crystal structure proves the (71 -0 0)21 1 binding mode (Figure 7.9) [87]. 

Figure 13.26 Structure formula of rotaxane 294+ and the electrochemically induced shuttling of the cyclophane along the dumbbell-shaped component (CH3CN, 298 K).

Figure 13.29 Structure formulas of rotaxane 316+, its dumbbell-shaped component 326+,...

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