PART 2: PROTEIN FOLDING Protein folding is the process by which a chain of amino

Question

PART 2: PROTEIN FOLDING Protein folding is the process by which a chain of amino acids forms its final shape. This shape will dictate the function of the protein. The primary structure, the peptide chain fold s into common secondary shapes, an alpha helix and beta pleated sheet. The tertiary structure sometimes be the final structure of a protein. However some proteins form quaternary structures, when two or more tertiary folded proteins (called subunits) come t the final active protein. An example of a tertiary protein is hexokinase, an enzyme that phos- phorylates glucose in glycolysis, and an example of a quaternary protein is ATP synthetase. 1. Below, draw in the two shapes commonly associated with the secondary structure of a two protein into the blank space. 2. Label the types of interactions/bonds that occur in the secondary-quaternary structures. 0n HC NH3+ Primary Secondary Tertiary Quaternary 3. What types of interactions/bonds are primarily responsible for alpha helixes and beta sheets? What components of the amino acid chain are participating in the interactions/ bonds (R-groups, peptide backbone, etc.)? 4. What types of interactions/bonds are primarily responsible for the tertiary structure of pro- teins? What components of the amino acid chain are participating in the interactions/bonds (R-groups, peptide backbone, etc.)? 42

Explanation / Answer

Allosteric enzymes are the substrates that bind to the allosteric site (the secondary site other than active site) and modify their activity. It can be a positive regulator that can change the shape of the active site that allows the substrate to bind more efficiently and also acts as a negative regulator that changes the shape of the active site and prevent the proper binding of the substrate thereby decreasing the activity of the protein.

Here we can see that pyruvate binds to N-terminal Arg11 with its c-terminal which confers stability. So, maybe pyruvate acts as a positive regulator that helps substrate to bind more efficiently to the active site and thereby increasing the activity of the protein.  

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