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Biochemistry Review #1 Functional Groups, Proteins, Enzymes, Carbohydrates

Biochemistry Review #1 Functional Groups, Proteins, Enzymes, Carbohydrates. Functional Groups. Identify the functional groups below:. H. H. O. N. C. H. O. C. O. Draw & label the functional groups below:. O. C. H. H. O. P. O. H. O. O. H. Macromolecules as Polymers.

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Biochemistry Review #1 Functional Groups, Proteins, Enzymes, Carbohydrates

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  1. Biochemistry Review #1 Functional Groups, Proteins, Enzymes, Carbohydrates

  2. Functional Groups

  3. Identify the functional groups below: H H O N C H O C O

  4. Draw & label the functional groups below: O C H H O P O H O O H

  5. Macromolecules as Polymers

  6. Long molecules • A _______ is a molecule that is chain-like in form; (i.e.- it is made up of lots of smaller parts all linked together like a chain.) • A _______ is the scientific term for one link in that chain

  7. 3 Examples of Biological Polymers: 1. Protein (polypeptides); a polymer made of amino acids linked together. Arg. Trp. Leu. Iso. Trp. Ser. 2. Nucleic Acids (Like DNA); polymers made of nucleotides linked together. G A C T C T G A 3. Polysaccharides (complex carbs); simple sugar molecules linked together. o o o o o

  8. Proteins

  9. 5 Parts of an amino acid(Alpha carbon, Carboxyl group, amino group, H+ atom, side chain)

  10. 1 4 3 • The 5 parts of an amino acid are: • Central carbon (alpha carbon) bonded to 4 groups • Amino group • Carboxyl group • Hydrogen atom • Side chain (R group)…which gives each amino acid its own particular characteristics. 2 5

  11. Dehydration Synthesis Cells link amino acids together to make proteins by taking out a water molecule. Dehydration Synthesis Peptide bonds form to hold the amino acids together Peptide Bond

  12. Dehydration Synthesis • Dehydration Synthesis is used to link amino acids together to form proteins. • Also used to put together carbs, lipids, and nucleic acids

  13. ___Hydrolysis___

  14. Protein shape determines function (which is determined by amino acid order) • Protein function is determined by 3-D shape • Shape is determined by folding • Folding is determined by what order the amino acids are arranged in. • Amino Acid order is determined by DNA

  15. ά - helix β-pleated sheet

  16. Proteins • Proteins are responsible for virtually all the structures of your body. • Hemoglobin carries oxygen in your blood. • Melanin shields your skin from devastating U.V. rays. • Myosin & Actin proteins make up your muscles. • Collagen allows your skin to be elastic. • Keratin helps keep your skin, hair, and nails waterproof. As Wilson does his bicep curls (above), the myosin and actin protein filaments in his muscles slide over each other to contract.

  17. Chiral Isomers • The two isomers are designated “L” or “D” form, from the Latin words for left and right • “levo”= left • “dextro”= right • The “handedness” of the molecule is also known as its “chirality”

  18. Chiral Isomers • Often times, one isomer is biologically active while the other is inert. • In living organisms, only L-form amino acids can be used to build proteins, but only D-form sugars can be utilized for energy!

  19. Homochirality • When all the isomers utilized in a molecule are the same “handedness” they are said to be homochiral. • All proteins and sugars utilized for life are homochiral.

  20. Enzymes

  21. Enzymes • Enzymes are specially shaped proteins that cells use to speed up chemical reactions. • They accomplish this by lowering the amount of energy needed to get a reaction started. Substances that can get reactions started are called catalysts.

  22. Enzymes • Enzymes act on specific substances called substrates during a chemical reaction. • The place on the enzyme where the chemical reaction occurs is called the active site.

  23. Enzymes • Usually an enzyme’s name will also give you a clue as to what substrate it works on.Ex.- Protease (proteins), Lipase (lipids), Sucrase (sucrose sugar), Amylase (amylose starch)

  24. Enzyme Inhibitors • Inhibitors can compete with substrates and slow down enzyme activity by blocking the active site. (They bind to the active site)

  25. Carbohydrates

  26. Carbohydrates • “Monosaccharides” are singlesugars. • They are the simplest carbohydrates, and thus taste very sweet. Glucose (Blood sugar) C6H12O6 Fructose (Fruit sugar) ALSO C6H12O6

  27. Carbohydrates • “Disaccharides” are doublesugars made from linking two monomers (single sugars) together. Here are a few common disaccharides. Lactose (milk sugar) β-bond Sucrose (table sugar) Maltose (malt sugar)

  28. Carbohydrates • “Polysaccharides” are long chains of sugars, such as starches. Sometimes they are called “complex carbohydrates”. StarchGlycogen

  29. Carbohydrates • Some polysaccharides are built with beta-bonds. This makes them tough and durable. CelluloseChitin

  30. Biochem Phone Flash-Cards Functional Groups, Proteins, Enzymes, Carbohydrates

  31. Label the functional groups below: O C H H O P O H O

  32. Label the functional groups below: H O H N C H O

  33. Label the functional groups below: H C O O

  34. The functional group below is a “hydroxyl group”. It is biochemically important because when added onto a molecule it will: (What is it’s function?) H O

  35. The functional group below is a “hydroxyl group”. It is biochemically important because when added onto a molecule it will: turn the molecule into an alcohol and make it polar…being polar also allows it to dissolve in water H O

  36. Name the 5 parts of an amino acid:

  37. The 5 parts of an amino acid are: • Central carbon (alpha carbon) bonded to 4 groups • Amino group • Carboxyl group • Hydrogen atom • Side chain (R group)…which gives each amino acid its own particular characteristics.

  38. Which ones are Amino Acids? 1 2 3 4 6 5

  39. 1 2 3 Propionic Acid (NO) L-Glutamine (YES) L-Tryptophan (YES) L-Cysteine (YES) Acetic Acid (NO) D-Alanine (YES) 4 6 5

  40. Identify (list) the four levels of protein structure:

  41. ά - helix β-pleated sheet

  42. Identify the proteins below with their correct functions • Used for tough, durable, waterproof protection of sensitive areas. ______________ • Major component of muscles. ____________ • Responsible for the color of skin and hair; blocks harmful UV. __________________ • Flexible and tough protein that gives skin its elasticity. ______________________ • Covers red blood cells; Used to transport oxygen. __________________

  43. Identify the proteins below with their correct functions • Used for tough, durable, waterproof protection of sensitive areas. Keratin • Major component of muscles. Actin & Myosin • Responsible for the color of skin and hair; blocks harmful UV. Melanin • Flexible and tough protein that gives skin its elasticity. Collagen • Covers red blood cells; Used to transport oxygen. Hemoglobin

  44. Name these molecules & tell how you know what they are. A B C

  45. Name these molecules & tell how you know what they are. A Starch - It is long and unbranching, made of ALL alpha-bonds (All point same direction) B Cellulose - It is long and unbranching, made of ALL beta-bonds (alternating up/down) C Glycogen - It is long and branching, made of ALL alpha-bonds (All point same direction)

  46. Name this polysaccharide and tell what it is used for N group N group N group N group

  47. Name this polysaccharide and tell what it is used for Chitin - It is long, uses beta-bonds, and has an N-group coming off in alternating directions It is found in insect and arthropod exoskeletons, used for protection

  48. Name the molecules. 1 2 3

  49. Name the molecules. Maltose (malt sugar) – Two six-sided rings joined by an alpha –bond Sucrose (table sugar) – One six-sided ring joined to one five-sided ring by an alpha bond Lactose (milk sugar) – Two six-sided rings joined by a beta-bond

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