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Bio. U2 Yr. 1
| Question | Answer |
|---|---|
| How can the rate of an enzyme-catalyzed reaction be measured? | Measuring the rate of disappearance of the substrate; measuring the rate of product formation |
| Which of the following is always true regarding an enzyme-catalyzed reaction? | The rate of the reaction depends on the frequency of collisions between the substrate and the enzyme. |
| In end product inhibition, | the product of the reaction acts as an inhibitor of the enzyme |
| Generally, increasing the temperature of a solution _ the rate of an enzyme-catalyzed reaction by increasing the _. Proteins, including enzymes, can be _ by high _ or extreme changes in _. | increases; frequency of collisions between enzyme and substrate; denatured; temperature; pH |
| Which level of protein structure involves more than one polypeptide chain? | quaternary |
| When a non-competitive inhibitor is present, increasing the substrate concentration | has no effect on the rate of the reaction |
| True or False? The rate of an enzyme-catalyzed reaction stays the same for the duration of the reaction. | False |
| True or False? Enzymes are made up of amino acid monomers. | True |
| True or False? Enzymes are biological catalysts. | True |
| True or False? Enzymes are made up of carbon, oxygen, and hydrogen atoms only. | False |
| True or False? A particular enzyme can catalyze a wide range of chemical reactions. | False |
| True or False? Enzymes are highly specific to their substrate. | True |
| True or False? Denaturation of an enzyme causes it to lose its shape. | True |
| True or False? Enzyme function depends on collisions between substrates and active sites. | True |
| True or False? The 3D shape and therefore the functioning of an enzyme is dependent on the primary structure. | True |
| Competitive inhibitors prevent enzyme function by... | bonding to the active site on the enzyme and therefore preventing the substrate from entering |
| What is a difference between fibrous and globular proteins? | Fibrous proteins have a linear shape, while globular proteins have a round shape |
| Isoleucine is_aminoacid canbe formed from aminoacidthreonine through linear metabolic pathway. When there are_concentrations of isoleucine, startsbindingto_ site of enzymethreoninedeaminase, changingshapeofactive site. Isoleucine (the_) acts as_inhibitor. | a non-essential; high; allosteric; end-product; non-competitive |
| What is an example of a conjugated protein? | Hemoglobin |
| What types of R groups would you most likely find folded into the center of a 3D protein? | Non-polar |
| What stabilizes a protein's tertiary structure? | Ionic bonds, disulfide bridges, hydrophobic interactions, hydrogen bonds, and NOT peptide bonds |
| What are functions of proteins in the body? | Catalyzing chemical reactions, storing materials for later use, signalling and communicating messages between cells, providing strength and structure, transport of materials into or out of cells, and NOT insulating the body to help maintain homeostasis |
| What types of bonds are responsible for a protein's primary structure? | peptide bonds |
| How many different amino acids are coded for by DNA which can become part of a polypeptide? | 20 |
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user-1907392