Sandbox Reserved 1640: Difference between revisions

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== Structural highlights ==

Our protein comes from the Bacillus cereus HuA2-4 organism. It includes the Epimerase domain. Our protein has a fair amount of secondary structures. Our protein also consists of many Rossman 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 tertiary structure contains many hydrophobic interactions. There are 3 major ligand binding sites.: UGA, NAD, and UGB. 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 Rossman 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 tertiary structure contains many hydrophobic interactions. There are 3 major ligand binding sites.: UGA, NAD, and UGB. 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. It has one ''' Ramachandran Outlier'''. the total structure Weight is 153.40 kDa.The way that the protein is folded denotes that it might also be a quaternary structure.

Sandbox Reserved 1640: Difference between revisions

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 == Structural highlights ==
-Our protein comes from the Bacillus cereus HuA2-4 organism. It includes the Epimerase domain.  Our protein has a fair amount of secondary structures. Our protein also consists of many Rossman 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 tertiary structure contains many hydrophobic interactions. There are 3 major ligand binding sites.: UGA, NAD, and UGB. 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 Rossman 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 tertiary structure contains many hydrophobic interactions. There are 3 major ligand binding sites.: UGA, NAD, and UGB. 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. It has one ''' Ramachandran Outlier'''. the total structure Weight is 153.40 kDa.The way that the protein is folded denotes that it might also be a quaternary structure.