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Proteins

Proteins. What elements are found in proteins?. Carbon, hydrogen, oxygen and nitrogen. A monomer of a protein is called?. An amino acid. In the term “Amino Acid”, where does the “amino” part come from. From the amino group (NH 2 ) one one end of every amino acid.

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Proteins

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  1. Proteins

  2. What elements are found in proteins? • Carbon, hydrogen, oxygen and nitrogen

  3. A monomer of a protein is called? • An amino acid

  4. In the term “Amino Acid”, where does the “amino” part come from • From the amino group (NH2) one one end of every amino acid

  5. In the term “Amino Acid”, where does the “acid” part come from • From the carboxylic acid group at the end of every amino acid molecule

  6. What is the “R” variable? • It is a side chain (usually made of hydrogen and carbon) • This chain is different for every amino acid

  7. What are the other two parts common to every amino acid? • The side hydrogen and the central carbon

  8. The bond between amino acids has a special name – what is it? • Peptide Bond

  9. When amino acids “link” – what groups become bonded together? • Amino group of one bonds to the carboxyl group of another

  10. A small chain of amino acids is called? • A polypeptide

  11. A long(er) chain of amino acids is called? • A protein

  12. What happens to a chain of amino acids in a protein and polypeptide? • They are twisted and then folded

  13. What makes one protein different from another protein? • The types of amino acids involved • The sequence of amino acids involved • The amount of amino acids linked ( the length of the protein chain)

  14. Why do the types, sequence and amount of amino acids make a difference? • They determine how the protein will coil up and then fold • This gives the protein a specific shape • The shape allows the protein to do its job

  15. What kinds of foods would you expect to give you amino acids/proteins? • Meat, Chicken, Fish, Eggs, Dairy (some), Soy

  16. If you add water to a protein and it breaks – what do you get? • A bunch of amino acids

  17. If you remove water and join two amino acids – what have you begun to build? • A polypeptide or protein

  18. Enzymes: Organic Catalysts

  19. What’s a catalyst and why do we need them?

  20. Catalysts: an analogy… • You are at the American Museum of Natural History (because you are a science nerd and like to look at Dinosaur Bones • You need to get to Babo (because you are a big fan of Iron Chef) • What are your transportation options?

  21. Catalysts: an analogy • You can walk… • If you walk like a New Yorker – about 1 block a minute – you would walk over 80 blocks – so an hour and 20 minutes. • Longer if you walk like a Livingston High School student on their way to class • You can take the C from 81st to West 4th St • Once the train arrives – about 15-17 minutes. • Less time if you can transfer to the A

  22. The train is the “enzyme” that catalyzes your transportation

  23. Enzymes: Lock and Key Model

  24. Enzymes are proteins • This means they are folded into a specific shape • The chemical that an enzyme works with is called the substrate

  25. How do enzymes work?

  26. What is the active site?

  27. What is the enzyme-substrate complex?

  28. Does the enzyme actively break or form the bonds in the substrate?

  29. How do enzymes lower the activation energy for chemical reactions?

  30. Is there any change in the free energy?

  31. Why could changing one amino acid potentially alter the activity of the enzyme?

  32. Enzymes: Induced Fit Model

  33. What is the difference between lock and key and induced fit enzymes?

  34. How specific are enzymes? Absolute Specificity Relative Specificity Enzyme can react with similar molecules for the same type of reaction • Enzyme can ONLY react with ONE specific type of substrate molecules

  35. What factors can affect the reactivity of an enzyme?

  36. Substrate Concentration • Enzymes must “bump into” substrate molecules • This means that if there is more substrate – there will be more collisions – and more enzymes being used • At some point activity levels off because all possible enzymes are already in use

  37. Enzyme Concentration • Similar to substrate concentration… • More enzymes  more collisions  more activity • At some point all substrates are being broken down and so increasing enzymes no longer increases activity

  38. pH • Every enzyme has an “optimal” pH – or a pH that the enzyme functions most quickly at • Most enzymes in the human body work best at near neutral pH….why do you think this is?

  39. What happens if you alter the pH? • Changing the pH can affect bonding between R groups? What does this do to the protein? • What does this do to the functionality of the protein? • Denaturing….

  40. Temperature • Increase in Temp  increase in molecular collisions  increase in enzyme activity • HOWEVER – too much heat can denature the protein and slow activity down

  41. What can increase enzyme activity?

  42. What can slow down enzyme activity?

  43. How could having a high fever for a long enough period of time damage your bodies metabolism?

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