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21 Cards in this Set
- Front
- Back
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Describe the induced fit of enzyme action and how an enzyme acts as a catalyst |
The substrate binds to the active site/enzyme Then the active site changes shape slightly so it is complementary to substrate This reduces the activation energy |
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Describe how the structure of a protein depends on the amino acids it contains |
The structure is determined by the relative position of amino acid interactions The primary structure is the sequence of amino acids Second structure is formed by hydrogen bonds Tertiary structure is formed by interactions between R groups This creates active sites in enzymes |
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Explain how the active site of an enzyme causes a high rate of reaction |
Lowers activation energy The induced fit causes active site of enzymes to change shape So the enzyme-substrate complex causes bonds to form |
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Describe a biochemical test to confirm the presence of protein in a solution |
Add biuret reagent If it’s a positive result it will turn purple |
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Describe two other ways in which all dipeptides are similar and one way in which they might differ |
Amine group at the end Carboxyl group at the end Different R groups |
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Describe how a non-competitive inhibitor can reduce the rate of an enzyme-controlled reaction |
Attaches to the enzyme at a site other than the active site Changes tertiary structure of an enzyme So active site and substrate are no longer complementary less substrate can bind |
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Describe how a peptide bond is formed between two amino acids to form a dipepetide |
A condensation reaction happens Between the amine group and the carboxylate group |
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The secondary structure of a polypeptide is produced by bonds between amino acids Describe how? |
Hydrogen bonds between NH group and C=O group |
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Describe a biochemical test to confirm the presence of protein in a solution |
Add biuret reagent If it’s a positive result it will turn purple |
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Describe two other ways in which all dipeptides are similar and one way in which they might differ |
Amine group at the end Carboxyl group at the end Different R groups |
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Describe how a non-competitive inhibitor can reduce the rate of an enzyme-controlled reaction |
Attaches to the enzyme at a site other than the active site Changes tertiary structure of an enzyme So active site and substrate are no longer complementary less substrate can bind |
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Describe how a peptide bond is formed between two amino acids to form a dipepetide |
A condensation reaction happens Between the amine group and the carboxylate group |
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The secondary structure of a polypeptide is produced by bonds between amino acids Describe how? |
Hydrogen bonds between NH group and C=O group |
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Two proteins have to same number and type of amino acids and different tertiary structures Explain why? |
Different sequence of amino acids This forms ionic, hydrogen and disulfide bonds in different places |
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Describe a biochemical test to confirm the presence of protein in a solution |
Add biuret reagent If it’s a positive result it will turn purple |
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Describe two other ways in which all dipeptides are similar and one way in which they might differ |
Amine group at the end Carboxyl group at the end Different R groups |
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Describe how a non-competitive inhibitor can reduce the rate of an enzyme-controlled reaction |
Attaches to the enzyme at a site other than the active site Changes tertiary structure of an enzyme So active site and substrate are no longer complementary less substrate can bind |
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Describe how a peptide bond is formed between two amino acids to form a dipepetide |
A condensation reaction happens Between the amine group and the carboxylate group |
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The secondary structure of a polypeptide is produced by bonds between amino acids Describe how? |
Hydrogen bonds between NH group and C=O group |
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Two proteins have to same number and type of amino acids and different tertiary structures Explain why? |
Different sequence of amino acids This forms ionic, hydrogen and disulfide bonds in different places |
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The formation of an enzyme-substrate complex increases the rate of reaction explain how? |
Reduces activation energy Without enzyme, very few substrates have sufficient energy for reaction |
