Sandbox Reserved 1640: Difference between revisions
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Our protein comes from the Bacillus cereus HuA2-4 organism. It includes the Epimerase domain. Our protein has a fair amount of secondary structures. These structures are important because of hydrogen bonding between carbonyl and amino groups in the peptide backbone. Our protein also consists of many Rossmann folds. This is a super secondary structure. It is composed of alternating alpha and beta sheets. The first Rossmann fold in a series is the one in contact with the nucleotide. In our protein, our nucleotide is the NAD. It contains a <scene name='86/861622/Rossmann_folds/1'>Rossmann folds</scene> that had 7 𝛃- strands and 6 𝜶-helices. The '''Rossman folds''' help stabilize the binding in the protein, which helps the '''catalytic triad''' have more efficient binding. This <scene name='86/861622/Quaternary_structure/1'>quaternary</scene> structure contains many hydrophobic interactions. This is true because of the association of several protein chains or subunits into a closely packed arrangement. Each of the subunits has its own primary, secondary, and tertiary structure. The subunits are held together by hydrogen bonds and van der Waals forces between nonpolar side chains. Our protein is made up of two or more polypeptide chains. Our protein is a strong homodimer with a hydrophobic interaction face. This means that the amino acids at the <scene name='86/861622/Active_site/1'>binding sites</scene> have nonpolar R groups cluster together, on the inside of the protein. This leaves the hydrophilic amino acids on the outside of the structure. | Our protein comes from the Bacillus cereus HuA2-4 organism. It includes the Epimerase domain. Our protein has a fair amount of secondary structures. These structures are important because of hydrogen bonding between carbonyl and amino groups in the peptide backbone. Our protein also consists of many Rossmann folds. This is a super secondary structure. It is composed of alternating alpha and beta sheets. The first Rossmann fold in a series is the one in contact with the nucleotide. In our protein, our nucleotide is the NAD. It contains a <scene name='86/861622/Rossmann_folds/1'>Rossmann folds</scene> that had 7 𝛃- strands and 6 𝜶-helices. The '''Rossman folds''' help stabilize the binding in the protein, which helps the '''catalytic triad''' have more efficient binding. This <scene name='86/861622/Quaternary_structure/1'>quaternary</scene> structure contains many hydrophobic interactions. This is true because of the association of several protein chains or subunits into a closely packed arrangement. Each of the subunits has its own primary, secondary, and tertiary structure. The subunits are held together by hydrogen bonds and van der Waals forces between nonpolar side chains. Our protein is made up of two or more polypeptide chains. Our protein is a strong homodimer with a hydrophobic interaction face. This means that the amino acids at the <scene name='86/861622/Active_site/1'>binding sites</scene> have nonpolar R groups cluster together, on the inside of the protein. This leaves the hydrophilic amino acids on the outside of the structure. | ||
The hydrophobic amino acids include THR, ILE, ALA, and PHE. This protein contains a few sugar rings in its metabolic pathway. The process creates sugar products. This enzyme creates a cavity where the sugar group binds and modifies itself | The hydrophobic amino acids include THR, ILE, ALA, and PHE. This protein contains a few sugar rings in its metabolic pathway. The process creates sugar products. This enzyme creates a cavity where the sugar group binds and modifies itself.The paper also mentions the le loir pathway. This pathway is used in the catabolism of Galactose. [https://en.wikipedia.org/wiki/File:Leloir_pathway.png] | ||
== Other important features == | == Other important features == | ||
