Tutorial:Basic Chemistry Topics: Difference between revisions
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='''Secondary Structures'''= | ='''Secondary Structures'''= | ||
Secondary structures are <scene name='Tutorial:Basic_Chemistry_Topics/Alpha_beta_2ndstructures/1'>alpha helices and beta sheets</scene>. The helices and sheets provide stability to the compound as a whole. The alpha helices are represented with pink arrows and the beta sheets are represented with yellow arrows. This molecule has approximately eight alpha helices and four beta sheets. <scene name='Tutorial:Basic_Chemistry_Topics/Alpha_helix/1'>Alpha Helices </scene>have a cylinder-like structure with a parallel formation. In this representation you can see the parallel formation within the cylinder structure. The parallel alpha helices are held in its cylinder structure by hydrogen bonds. <scene name='Tutorial:Basic_Chemistry_Topics/Beta_sheets/1'>Beta sheets</scene> are often anti-parallel. The folding of a protein, alpha helices and beta sheets, gives the compound its function. When there is a change in protein folding, the function will change. As previously stated, the study discovered ACC(2’)-Ic to have a GNAT fold, and the GNAT family are enzymes capable of acetylation. <"Wikipedia. N.p., n.d. Web. 12 Nov. 2012. <http://en.wikipedia.org/wiki/Protein_secondary_structure>. </ref> | Secondary structures are <scene name='Tutorial:Basic_Chemistry_Topics/Alpha_beta_2ndstructures/1'>alpha helices and beta sheets</scene>. The helices and sheets provide stability to the compound as a whole. The alpha helices are represented with pink arrows and the beta sheets are represented with yellow arrows. This molecule has approximately eight alpha helices and four beta sheets. <scene name='Tutorial:Basic_Chemistry_Topics/Alpha_helix/1'>Alpha Helices </scene>have a cylinder-like structure with a parallel formation. In this representation you can see the parallel formation within the cylinder structure. The parallel alpha helices are held in its cylinder structure by hydrogen bonds. <scene name='Tutorial:Basic_Chemistry_Topics/Beta_sheets/1'>Beta sheets</scene> are often anti-parallel. The folding of a protein, alpha helices and beta sheets, gives the compound its function. When there is a change in protein folding, the function will change. As previously stated, the study discovered ACC(2’)-Ic to have a GNAT fold, and the GNAT family are enzymes capable of acetylation. <ref> "Wikipedia. N.p., n.d. Web. 12 Nov. 2012. <http://en.wikipedia.org/wiki/Protein_secondary_structure>. </ref> | ||
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! scope="col" width="5000px" | Coenzyme A (CoA) | ! scope="col" width="5000px" | Coenzyme A (CoA) | ||
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| scope="col" width="5000px" | Coenzyme A (CoA) is involved in many physiological processes such as, synthesizing and oxidizing fatty acids. This process is essential for the utilization of fatty acids for energy. Coenzyme A is used as a substrate in the citric acid cycle. The citric acid cycle is also known as the Krebs cycle or tricarboxylic acid cycle (TCA). This process is important to the production of ATP, which is an energy source used by the body. | | scope="col" width="5000px" | Coenzyme A (CoA) is involved in many physiological processes such as, synthesizing and oxidizing fatty acids. This process is essential for the utilization of fatty acids for energy. Coenzyme A is used as a substrate in the citric acid cycle. The citric acid cycle is also known as the Krebs cycle or tricarboxylic acid cycle (TCA). This process is important to the production of ATP, which is an energy source used by the body.<ref>Maňas, Michal, trans. "File:3D model hydrogen bonds in water.jpg." "Coenzyme A." Wikipedia. N.p., n.d. Web. 11 Nov. 2012. <http://en.wikipedia.org/wiki/Coenzyme_A>. </ref> | ||
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