Tutorial:Basic Chemistry Topics: Difference between revisions

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[[Image:3D hydrogen Bonding.jpg | thumb | left | 200px | Hydrogen Bonding<ref>Maňas, Michal, trans. "File:3D model hydrogen bonds in water.jpg." Wikimedia Commons. Wikimedia Commons, 3 Dec. 2007. Web. 31 Oct. 2012 <http://commons.wikimedia.org/wiki/File:3D_model_hydrogen_bonds_in_water.jpg.</ref>]]
[[Image:3D hydrogen Bonding.jpg | thumb | left | 200px | Hydrogen Bonding<ref>Maňas, Michal, trans. "File:3D model hydrogen bonds in water.jpg." Wikimedia Commons. Wikimedia Commons, 3 Dec. 2007. Web. 31 Oct. 2012 <http://commons.wikimedia.org/wiki/File:3D_model_hydrogen_bonds_in_water.jpg.</ref>]]


The weakest bond discussed here, the hydrogen bond is an attractive intermolecular attraction between an electronegative atom and hydrogen. When the electronegative atom pulls the electrons, it leaves the other atom with a slightly positive charge. A common example of this is water. The image to the left demonstrates the hydrogen bonding of water. The highly electronegative oxygen pulls hydrogen's electrons closer. When oxygen pulls the electrons, it leaves hydrogen with a slight positive charge. In this representation the <scene name='Tutorial:Basic_Chemistry_Topics/Hydrogen_bonds/2'>hydrogen bonds</scene> are represented as yellow-dashed lines. The hydrogen bonds are important to the compound used by the study because they offer stability to the secondary structures.  
The weakest bond discussed here, the hydrogen bond is an attractive intermolecular attraction between an electronegative atom and hydrogen. When the electronegative atom pulls the electrons, it leaves the other atom with a slightly positive charge. A common example of this is water. The image to the left demonstrates the hydrogen bonding of water. The highly electronegative oxygen pulls hydrogen's electrons closer. When oxygen pulls the electrons, it leaves hydrogen with a slight positive charge. In this representation the <scene name='Tutorial:Basic_Chemistry_Topics/Hydrogen_bonds/2'>hydrogen bonds</scene> are represented as yellow-dashed lines. The hydrogen bonds are important to the compound used by the study because they offer stability to the secondary structures. <ref name="hydrogen bonds">"Hydrogen Bond." wikipedia. N.p., n.d. Web. 4 Nov. 2012.<http://en.wikipedia.org/wiki/Hydrogen_bond>. </ref>




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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.  
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 name="Protein Secondary Structure." Wikipedia. N.p., n.d. Web. 12 Nov. 2012. <http://en.wikipedia.org/wiki/Protein_secondary_structure>. </ref>