User:Tommie Hata/Protein Structure Tutorial: Difference between revisions
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'''Amino acids and primary structure''' | '''Amino acids and primary structure''' | ||
Proteins are polymers of [http://en.wikipedia.org/wiki/Amino_acid amino acids]. The "backbone" of the protein is made up of carbons and nitrogens. The amino acid sidechain extends out of the backbone. <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Amino_acids_and_sidechains/2'>Here, the backbone is colored in CPK coloring and the sidechains are colored green.</scene> The linear sequence of amino acids in a polypeptide is referred to as its [http://en.wikipedia.org/wiki/Primary_structure "primary structure"]. | Proteins are polymers of [http://en.wikipedia.org/wiki/Amino_acid amino acids]. The "backbone" of the protein is made up of carbons and nitrogens. The amino acid sidechain extends out of the backbone. <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Amino_acids_and_sidechains/2'>Here, the backbone is colored in CPK coloring and the sidechains are colored green.</scene> The linear sequence of amino acids in a polypeptide is referred to as its [http://en.wikipedia.org/wiki/Primary_structure "primary structure"]. | ||
'''Interactions between the protein backbone: secondary structure''' | '''Interactions between the protein backbone: secondary structure''' | ||
[http://en.wikipedia.org/wiki/Hydrogen_bond Hydrogen bonds] between backbone amide and carboxyl groups maintain some local structural characteristics referred to as [http://en.wikipedia.org/wiki/Secondary_structure secondary structure]. Two common types of secondary structure are the [http://en.wikipedia.org/wiki/Alpha_helices alpha helices] and the [http://en.wikipedia.org/wiki/Beta_sheet beta pleated sheet]. <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Secondary_structure/2'>Here, alpha helices are colored red and beta pleated sheets colored blue in a "ribbons" display</scene>. | |||
'''3D structure of a protein maintained by interactions between amino acid sidechains: tertiary structure''' | |||
The overall shape of a protein is maintained by the interaction between amino acid sidechains. The distribution of these sidechains across the protein (the primary structure) is largely responsible for determining [http://en.wikipedia.org/wiki/Tertiary_structure tertiary structure]. | |||
Types of tertiary interactions | |||
<scene name='User:Tommie_Hata/Protein_Structure_Tutorial/ | <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Hydrophobic_core/1'>Nonpolar sidechains and the hydrophobic core</scene>. | ||
<scene name='User:Tommie_Hata/Protein_Structure_Tutorial/ | <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Ionic_interaction/1'>Charged sidechains and ionic interactions</scene>. | ||
<scene name='User:Tommie_Hata/Protein_Structure_Tutorial/ | <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Ionic_interaction_with_surface/1'>Ionic Interactions with surface</scene>. | ||
<scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Polar_and_charged/1'>Polar and charged sidechains</scene>. | |||
<scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Ssbond-sidechain/1'> | <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Ssbond-sidechain/1'>Cysteines and disulfide bond formation in oxidizing environments</scene>. | ||
<scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Ssbond-alpha-carbon/1'>SS bond | <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Ssbond-alpha-carbon/1'>SS bond shown between alpha carbons in backbone view</scene>. | ||
<scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Default/5'> | <scene name='User:Tommie_Hata/Protein_Structure_Tutorial/Default/5'>Return to default view</scene> | ||