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Crystalline polymers do have a glass transition temperature (Tg), but its significance differs from that in amorphous polymers. In a crystalline region, polymer chains are tightly packed in a regular structure, minimizing their movement. However, these polymers also contain amorphous regions because complete crystallization is nearly impossible. The glass transition occurs in these amorphous areas where the chains have more freedom to move. Therefore, the Tg in crystalline polymers is observed but it is much less pronounced compared to amorphous polymers, as the bulk of the material's mechanical properties are dictated by the crystalline regions, which overshadow the contributions of the amorphous areas to the overall polymer behavior at temperatures around the Tg.
Bending epoxy resin, while challenging, is achievable by manipulating its state before it fully cures. The key lies in timing and temperature. Epoxy resin starts as a liquid and gradually hardens. To bend it, you must catch it during the gel-like intermediary phase, which varies depending on the resin's formula and volume. Heating the resin gently can extend this phase, making it more pliable. Use a heat gun carefully to warm the resin without causing it to bubble or cure prematurely. Forming it around a mold or shape while it’s warm and flexible allows for bending. Ensure the resin is evenly heated to avoid weak spots. Once shaped, let it cool and fully cure. It's a delicate balance of timing, temperature, and handling. Always wear protective gear and work in a well-ventilated area.
Basic amino acids, including lysine, arginine, and histidine, are characterized by their side chains that contain nitrogen and carry a positive charge at physiological pH (around 7.4). The term "basic" refers to their ability to accept protons, which is a feature of their amine group side chains. This proton-accepting property is in contrast with acidic amino acids, such as glutamate and aspartate, which have side chains that donate protons and carry a negative charge at physiological pH. Therefore, basic amino acids are positively charged due to their side chains that accept protons and bind negatively charged molecules, playing crucial roles in protein structure and function, including enzyme activity, cellular signaling, and molecular recognition processes.
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