4_Nutrients_cal_dig_10

4_Nutrients_cal_dig_10 - BIOL 103 Human Biology Testing...

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BIOL 103 Human Biology
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Testing your knowledge of the concepts: Page 18 (Ch. 1): Questions: 13-17 Pages 63-60 (Ch. 3): Questions: 13-17, 22-24, 26, 27 Page 42 (Ch. 2): Questions: 20-25 Pages 89 & 90 (Ch. 4): Questions: 12-20 Pages 183-184 (Ch. 8) Questions: 9-21, 27, 29 Answers: Pages A-2 & A-4
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Supplemental Instruction Sessions Tuesday 7-8, Milne 105, Joanne Thursday 7-8, Milne 105, Gauri Sunday 6-7, Milne 109, Office Hours M&F 2:00-3:00, Blake C 211, Gauri T&R 10:00-11:00, Blake C 210, Joanne
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68% 77% 78% 83%
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70% 74% 77% 82%
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W, February 10, 2010 6:30 pm, Newton 202 Bulimia Please consider attending Ms. Mary Egger's talk on her experience with bulimia if you or someone you know has symptoms or you have concerns. Mary is a nurse, mother, triathlete and an athletic coach. She is also available to speak with directly after the seminar or you may contact her via email with questions/concerns. Sponsored by the Biology Department.
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Proteins
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Proteins Location in the body collagen = most abundant, even in bone muscle , hair, nails, etc. cell membranes (globular) form enzymes -- “catalysts that facilitate chemical reactions without being used up or becoming part of the product” play a regulatory role some hormones insulin (lowers blood glucose) glucagon (raises blood glucose)
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friends enemies you you
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structure of proteins 20 amino acids (building blocks) -- see RER adults can make 12 the remaining 8 are essential , i.e., we must obtain them from food general structure of amino acids amino group (body needs water for deamination) -- with nitrogen carboxyl group (-COOH) -- acid group -OH = hydroxyl radical group (R = rest of molecule)
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General structure of amino acid R = radical group (carboxyl)
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Radical groups
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Specific levels of protein structure primary = sequence of amino acids (up to 3,000) -- human muscle contains string of 27,000 amino acids peptide bonds and polypeptides condensation reaction: carboxyl to amino group dictates final structure and chemical behavior secondary = coiling of the amino acid chain (hydrogen bonds hold coils in place) tertiary = folding of the amino acid coils (hydrogen bonds, covalent and ionic bonds hold folds in place) quaternary = separate protein molecules clumped together, e.g., hemoglobin
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peptide bond carboxyl +l amino dehydration
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+ amino acid + amino acid + amino acid +
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sequence coiling folding of coils e.g., hemoglobin 1 2 3 4
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folding of coils S-S 1 2
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(bond)
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e.g., tendon in RBC
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Proteins (cont.) Note: secondary and tertiary levels easily denature (loss of native shape) e.g., egg white (albumin) is altered with heat (also quaternary level easily denatured if present) weak hydrogen bonds sensitive to increases or decreases in temperature and pH
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cooked egg, skin, etc. X
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4_Nutrients_cal_dig_10 - BIOL 103 Human Biology Testing...

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