61246
Description
Flashcards by alexlpeart, updated more than 1 year ago
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Created by alexlpeart
over 11 years ago
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| Question | Answer |
| Amino acids make up ____. How many amino acids are there in our body? | Proteins, 20 amino acids |
| How are ketoacids made? | When the amide group is removed from an amino acid leaving just the carboxyl group. |
| Where does deamination occur? | Matrix of the mitochondria |
| What is deamination? what products do we get from it? What is the problem with its products, what do we do about this? | removing the amide group from an amino acid and creating ammonia (NH4) and NADH. Ammonia is toxic so we need to get it out our body. This is done via glutamate and then excreted from in the urine. |
| What is transamination? | The swapping the amide group with the keto group (=o) meaning the amino acid becomes a alpha-ketoacid and the alpha-ketoacid becomes an amino acid. You could think of it as them swapping their R groups. |
| complete the following equation; Glutimate + H2O + ____ --> | Glutimate + H2O + NAH(+) -->Alpha-ketoglutimate +NH4(+) +NADH |
| What is alanine converted into when energy demand is high? and where is this product taken? | Pyruvate, to the liver to undergo gluconeogenesis |
| Describe the process of forming a protein. | mRNA is created from DNA template. mRNA if transferred to the ribosome where it is used to determine the sequence of amino acids. tRNA binds to the complimentary section of mRNA and its amino acids becomes attached to the sequence. This continues untill the primary structure of the protein is complete. The amino acid chain is then folded into its functional form by chaparonins. |
| What are Chaperonins? | Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins. Chaperonins belong to a large class of molecules that assist protein folding, called molecular chaperones |
| What bond are amino acids connected by? What part of the amino acids join, and what is released during this reaction? | Peptide bonds, formed when a hydrogen from the amide group and the O-H from the carboxyl group combine to make water. |
| Describe the process a chaperonin molecule undergoes for help a protein form. | Binds to the N terminus of the polypeptide. Completion of translation of the protein while still bound to the chaperonin. Folding of the protein after synthesis has been complete. Release of the folded protein. |
| Give three reasons post-transnational processing is required. | Targeting, Folding and Activation |
| What type of enzyme breaks down proteins? | Proteases |
| Why is protein breakdown necessary? | Quality control, Enable muscle growth and for energy production. |
| What processes can amino acids be used in to create energy? | TCA cycle and or gluconeogenesis |
| What macronutrients can reduce the breakdown of protein as an energy source? | Carbohydrates |
| Give details of the Ubiquitin-proteasome pathway. | Ubiquitin marks protein for degradation. Inactive 20S proteasome is activated by a regulatory protein to become active now called 26S. 26S breaks down protein into small peptides and the small peptides are then broken down into AA by other cellular processes. |
| What process must proteins undertake before they can be broken down by lysosomes? | Endocytosis to get them into the cell, then the endocitic vesicle must fuse with lysosomal vesicles where the protein is broken down by the low pH. |
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