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Human Systems

Human Systems. 8.1 Essential Nutrients . Essential Nutrients. Living things composed of non-living components - Carbohydrates - Lipids - Proteins - vitamins/minerals - nucleic acids Nutrients: in food eaten ( carbs , proteins, fats)

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Human Systems

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  1. Human Systems 8.1 Essential Nutrients

  2. Essential Nutrients • Living things composed of non-living components- Carbohydrates- Lipids- Proteins- vitamins/minerals- nucleic acids • Nutrients: in food eaten (carbs, proteins, fats) • Vitamins/Minerals: in food eaten but needed in smaller amounts • Water: essential for life but not a nutrient

  3. Carbohydrates • Energy nutrients- fast source- majority of diet (in excess stored as fat) • Body not able to make carbohydrates- eat plants that synthesize carbs through photosynthesis (glucose) • Composed of single sugar units or polymers (many)- C, H, O in 1:2:1 ratio- triose sugars C3H6O3 • End in ‘ose’ suffix

  4. Carbohydrates • Classified by number of sugar units contained • Monosaccharides: single sugar unit Ex) Same chemical formula- different structural arrangements gives differentchemical properties

  5. Carbohydrates • Disaccharides: two monosaccharides togetherex) sucrose: glucose and fructose together • Formed by DEHYDRATION SYNTHESIS (dehydrolysis)- water molecule is formed from 2 monosaccharides • Opposite reaction is hydrolysis – water used to break disaccharide bond

  6. Dehydration Synthesis Dehydration Synthesis Animation

  7. Carbohydrates • Polysaccharides: union of many monosaccharides • Starch – plants store energy in starch bonds- two forms: amylose and amylopectin • Glycogen – animals store carbs in glycogen bonds- similar form to amylopectin (just smaller) • Cellulose – plant cell walls- 50% all organic carbon in biosphere- tends not to form coiled structures like starch, instead in layers.

  8. Lipids • Non-polar – makes them insoluble in polar solvents (like water) • 2 structual units: GLYCEROL and FATTY ACIDS- combined through dehydration synthesis Can also get monoglycerides and diglycerides but triglycerides most common Lipid dehydration synthesis

  9. Lipids Functions: • Storage of energy- glycogen supply built up, excess stored as fat • Key components in cell membranes • Cushions for organs of body • Carriers for vitamins A, D, E, K • Raw materials for synthesis of hormones • Insulates body from cold

  10. Lipids • Triglycerides- solid at room temperature (fats); liquid at room temp (oils) • saturated fatty acids – single bonds between carbons- most animal fats are saturated – difficult to break down • Unsaturated fatty acids – double bonds between carbons- most plant fats unsaturated- more reactive – plant oils more easily broken down • Phospholipids – have a phosphate group bonded to glycerol- negative charged phosphate replaces one fatty acid - results in a polar end, which is soluble in water- non-polar end: insolubleex) cell membranes

  11. Proteins • Not primarily energy compounds • Form structural components of cells-damaged – proteins made-build new cells • Composed of amino acids- NH2 group (amino group)- COOH group (carboxyl group)- R group (differentiates amino acids from one another) • Ribosomes manufacture proteins according to DNA instructions

  12. Proteins • Composed of C, H, O • Also contain N and sometimes S • Array of proteins almost infinite- composed of 20 different amino acids- change in position of a single amino acid, changes the protein structure • Small proteins = a few amino acids • Large proteins = can have more than 250 000 amino acids • Order and number of amino acids determine type of protein.

  13. Proteins • Human eat protein to get amino acids. - digested (broken down) and absorbed- cells assemble amino acids depending on DNA instructions • Amino acids joined by dehydration synthesis- water removed- covalent bond forms between carboxyl group of one amino acid and the amino group of the otherPEPTIDE BOND! • Polypeptides: chains of amino acids • Body capable of making some amino acids: 8 essential amino acids must come from FOOD

  14. Proteins • Folded into 3-D shapes- shape (structure) determines function- structure determined by amino acid sequence • 4 levels of protein structure- PRIMARY – unique sequence of amino acids- SECONDARY – folds and coils of chain (helical shape)- TERTIARY – interactions between R groups result in additional folding- QUATERNARY – large, globular proteins formed from 2 of more polypeptide chains Ex) hemoglobin Protein Structure

  15. Proteins • Excess heat, radiation, or change in pH - alters shape and configuration of protein- DENATURATION: can assume its original shape after factor is removed • Permanent change in protein shape- COAGULATION- ex) boiling an egg

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