Phillips Academy Computer-Aided Protein Visualization Lab: Difference between revisions
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[Put in manipulations of cartoon view to stick, backbone only then backbone with side chains.......adjust color scheme to emphasize secondary structure. Isolate secondary structures if possible, etc] | [Put in manipulations of cartoon view to stick, backbone only then backbone with side chains.......adjust color scheme to emphasize secondary structure. Isolate secondary structures if possible, etc] | ||
2. <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene> | 2. <scene name='71/713432/Protein_secondary_structure_bs/2'>Click to see beta sheet</scene><scene name='79/795987/Pg/8'>Click to see beta sheet in isolation</scene> | ||
<br> | <br> | ||
The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape. | The second step of protein folding results in the '''tertiary structure''' (or 3° structure). Tertiary structure gives the protein an overall three-dimensional structure. The tertiary structure of a protein is determined by a combination of factors including hydrogen bonds, '''ionic bonds''' (between positively and negatively charged amino acids), '''covalent''' '''disulfide bonds''' (between cysteine residues), and '''Van der Waals''' interactions. Tertiary structure can also be affected by repulsive forces between similarly charged amino acids, as well as '''hydrophobic''' and '''hydrophilic''' interactions with a solvent (commonly water). At a distance many proteins form what look to be large globs at this point, and it is only upon more careful and close up inspection that one can see the true uniqueness of the shape. | ||
