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11 Cards in this Set
- Front
- Back
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What are some general functions of a protein? Hint: there are six |
1. Catalysis - enzymes 2. movement 3. signalling 4. structure 5. transport 6. defence- antibodies |
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What are the types of bonds that holds together the different levels of protein structure? |
1. Primary - peptide 2. secondary (alpha helix or beta pleated sheets) - hydrogen bonds 3. tertiary- ionic bonds, hydrophobic interactions or Vander Waals interactions, hydrogen bonds, and disulphide bonds 4. Quaternary- hydrogen bonds, hydrophobic interactions or Vander Waals interactions, ionic bonds, and disulphide bonds |
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What determines the shape of a protein? |
The side chains of the amino acids (the R-groups) |
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What does a spontaneous reaction mean? |
That this reaction will occur without any outside interactions. That it doesn't need any help to react. It doesn't have to mean that the reaction happens quickly. |
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Describe the transition state in a catalyzed reaction. |
It is a molecule that looks like the substrate and the products, but is highly unstable with high energy. |
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How do enzymes work? |
The substrate (reactants) bind to the active site in the enzyme that is highly specific to the substrates that it is catalyzing. This causes a shape change in the enzyme to fit the substrates more snugly. Part way through the reaction, the enzyme bends the substrates into the transition state and is then converted into the product before being released. |
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What do enzymes do? |
They provide a lower energy pathway (a pathway with a lower activation energy) that the molecules can use. |
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What is the active site of an enzyme? |
It is a pocket in the tertiary structure of an enzyme. It is the place where the substrate binds. |
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How do physical conditions effect the rate of a reaction? Temperature, pH, ect. |
Every enzyme has an optimum condition, a point where the reaction will preform at its best. If you go too high above or too beneath the optimum, the reaction will go slower. |
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What are competitive inhibitors? |
Molecules that bind at the active site and prevent substrate form binding. They are a similar shape, charge and polarity as the substrate. Increasing the concentration of the substrate, can once again raise the reaction rate. |
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What are allosteric regulators (non-competitive inhibitors)? |
Molecules that binds not at the active site of an enzyme, but on the enzyme, changing its shape (either opening or closing the active site). This effectively helps or hinders the reaction. Increasing the concentration of the substrate, can not raise the e reaction rate as the shape as the enzyme has changed shape. |
