Snap-back structures

DNase I stock solutions are stored at -2O C (1 mg/ml) in 5- xl aliquots (each aliquot is used once). Variation in the activity of DNase I preparations is often observed and the exact amount needed to introduce the desired number of nicks should be determined for each enzyme batch. Sometimes template switches occur which will result in snap-back structures (zero-binding nucleic acid), which remain S, nuclease-resistant upon denaturation. Rigby et al. (1977) suggested that this effect was due to a differential loss of 5 - 3 exonuclease activity upon storage leading to a displacement of the nicked strand and a template switch from the complementary... 

In viw PAI and antithrombin are stabilized in their active forms by binding to vitronectin and heparin, respectively. These two serpins seem to have evolved what Max Perutz has called "a spring-loaded safety catch" mechanism that makes them revert to their latent, stable, inactive form unless the catch is kept in a loaded position by another molecule. Only when the safety catch is in the loaded position is the flexible loop of these serpins exposed and ready for action otherwise it snaps back and is buried inside the protein. This remarkable biological control mechanism is achieved by the flexibility that is inherent in protein structures. 

The rather low coordination in the (100) and (110) surfaces will clearly lead to some instability and it is perhaps not surprising that the ideal surface structures shown in Figure 1.2 are frequently found in a rather modified form in which the structure changes to increase the coordination number. Thus, the (100) surfaces of Ir, Pt and Au all show a topmost layer that is close-packed and buckled, as shown in Figure 1.3, and the (110) surfaces of these metals show a remarkable reconstruction in which one or more alternate rows in the <001 > direction are removed and the atoms used to build up small facets of the more stable (111) surface, as shown in Figure 1.4, These reconstructions have primarily been characterised on bare surfaces under high-vacuum conditions and it is of considerable interest and importance to note that chemisorption on such reconstructed surfaces can cause them to snap back to the unreconstructed form even at room temperature. Recently, it has also been shown that reconstructions at the liquid-solid interface also... 

A type of material known as shape memory alloy (SMA) can perform this trick. SMAs are more complicated than electrorheological fluids and the other smart materials previously described in this chapter. An SMA does not only react or respond to environmental conditions, it also has a memory that enables it to return to a specific structure, or sometimes switch between two different structures. After the material has been set, it can recover from a deformation that would be permanent in other materials. When the temperature is raised by an amount that depends on the specific material, it snaps back into shape automatically. The memory is based on phase transitions, as described in the sidebar on page 120. 

Alloy with Memory. In seeking a way to reduce the brittleness of titanium, U.S. Navy researchers serendipitously discovered a nickel-titanium alloy having an amazing memory. Previously cooled clamps made of the alloy (nitinol) are flexible and can be placed easily in position. When warmed to a given temperature, the alloy hardware then exerts tremendous pressure. Use of conventional clamps for holding bundles of wires or cables in a ship or aircraft structure requires special tools. For this and other applications in industry and medicine, nitinol has been in demand. The alloy, however, is not easy to produce because only minor variations in composition can affect the snap back" temperature by several degrees of temperature. 

Zero-time reassociation comes from palindromic sequences that can form "snap-back" or "hairpin" structures. Such molecules reassociate very rapidly, at a rate independent of their concentration, because they do not need to interact with another molecule to form a double-stranded structure. 

The polypeptide chain of elastin is rich in glycine, alanine, and valine and is very flexible and easily extended. In fact, its conformation probably approximates that of a random coil, with little secondary structure at all. However, the sequence also contains frequent lysine side chains, which can be involved in cross-links. These cross-links prevent the elastin fibers from being extended indefinitely, causing the fibers to snap back when tension is removed. The cross-links in elastin are rather different from those in collagen, for they are designed to hold several chains together. Four lysine side chains can be combined to yield a desmosine cross-link (see here)... 

The role of dislocations is useful in explaining the yield strength and ductility of certain crystalline solids. One could account for elasticity by imagining a regular crystal structure without dislocations such as those of Fig. 3.2. If a certain horizontal shearing stress were applied to the top of the crystal lattice, then the structure would bend, but snap back to its original... 

Amorphous materials can be thermoformed with less residual stress than semi-crystalline resins. Retained volume is nearly 100 percent for monolayer COC-LLDPE films with COC content between 15 and 30 weight percent. This result reflects the amorphous nature of COC which is imparted into the films, even at relatively small amount. Less stress means less post-form shrinkage or snap-back, giving the flexible package the appearance of a rigid one. Film structures with high LDPE content tend to have lower retained volume. Formed cavities from other semicrystalline materials, such as nylon and PP, usually suffer some loss in volume. 

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