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FSU HUN 1201 - Chapter 6: Proteins

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Chapter 6: Proteins1. Large complex molecules found in all living things. 2. Synthesis controlled by our DNA (genetic material)3. Contains carbon, hydrogen, oxygen and nitrogen4. Made from 20 amino acids – 9 of which are essential (must be obtained from food)5. Nonessential – can be synthesized in sufficient quantities. We do not need to consume them in the diet. 6. Transamination – the transfer of an amine froup from an essential amino acid to a different acid group and side chain (r group) It is used to make nonessential amino acids.7. Conditionally essential amino acidea. Nonessential becomes essentialb. PKU – tyrosine becomes a conditionally essential amino acid that must be provided by the diet. Phenylalanine  tyrosine8. How are proteins made?a. Long chains of amino acids connected by peptide bondsb. Gene expression – when cells use genes to make proteinsi. Gene: segment of DNA that serves as a template for the synthesis (expression) of a particular protein (AT-CG)c. Transcription: messenger RNA copies the genetic information from DNAd. Translation: the genetic information in RNA is converted into the amino acid sequence of a protein. e. Transcription – copy; Translation – to translate from RNA to ribosome to create a proteinf. Protein turnover – existing proteins are degraded to provide the building blocks for new proteinsi. Amino acid pool includes amino acids from food and cellular breakdowng. Protein organization determines function – sequential order of the amino acidsi. Spiral shape from twist in amino acid chain9. Hemoglobin: red blood cells10. Protein denaturation – proteins uncoil and lose the shapea. Damaging substances: heat, acid, base, heavy metal, alcoholb. Protein function is losti. Denatured enzyme, high fever, blood pH out of normal range, during digestion11. Protein in the diet: for protein synthesis, all essential amino acids must be available to the cella. Limiting amino acidi. Essential amino acid that is missing or in the smallest supplyii. Slows down or halts protein synthesisb. Inadequate energy consumptioni. Limits protein synthesisc. Incomplete protein (low quality): insufficient essential amino acidsi. Derived from animal and soy proteinii. Soy protein sufficient for adults, not for infantsd. Mutual Supplementation: combine two or more incomplete protein sources to make a complete proteine. Complementary proteins: two or more foods are combines to supply all nine essential amino acids for a complete protein12. Protein digestion: begins in the stomach and continues in small intestinea. Hydrochloric acid denatures protein strands and activates pepsinb. Pepsin: enzymes breaks down proteins into short polypeptides and amino acidsc. Gastrin: hormone controls hydrochloric acid production and pepsin released. Pancreatic enzymes (proteases) complete protein digestionse. Special sites (small intestine) transport amino acids, dipeptides, tripeptidesf. High doses of individual amino acid supplements can lead to amino acid toxicity and deficiencies. 13. Protein qualitya. Methods:i. Chemical scoreii. Protein digestibility corrected amino acid score (PDCAAS)b. Animal protein and many soy products are highly digestible (90% absorption)14. Functions a. Cell growth, repair, maintenanceb. Enzymes and proteinsc. Fluid and electrolyte balanced. Acid-base balancee. Immune systemf. Energy sourceg. Nutrient transport and storage.15. Protein Adequacya. Nitrogen balance determines proteins needsi. Positive nitrogen balance; negative nitrogen balance, in nitrogen balance16. RDA for proteina. RDA: 0.8 g per kg of body weight per day.b. Recommended percentage of energy is 10-35% of total energy intake.c. Protein needs are higher during growth and development (children, adolescents and pregnant/lactating women)17. Too much protein can be harmfula. High cholesterol and heart disease – animal protein rich diets are associated with high blood cholesterol levels (saturated fat)b. Contributed to bone lossi. High protein diets increase calcium excretion and can lead to bone lossii. However, adequate protein intake is associated with decreased risk of osteoporosisc. Kidney diseasei. High protein  increased risk among susceptible individualsii. People with diabetes have higher rates of kidney disease and may benefit from a lower-protein dietiii. Max of 2g of protein per kilogram body weight each day is safe for healthy people18. Protein Sourcesa. Meats, milk-based products, soy products, legumes, whole rains, nuts, quorn19. Vegetarian Dietsa. Vegetarianism: restricting diet to foods of plant originb. People choose to be for healthy benefits, ecological reasons, religious reasons, ethical reasons, and concerns over food safety. c. Healthy benefits:i. Lower fat and total energy intakeii. Lower blood pressure, reduced risk of heart disease, fewer digestive problems, reduced risk of some cancers, reduced risk of kidney disease, kidney stones and gallstonesd. Challenges:i. Can be low in some nutrients, Associated with disordered eating, Varied and adequate diet planning, Soy and complementary proteins, Vegetarian food guide pyramid, Special attention to vitamins D, B12 and riboflavin (b2) and zinc and iron20. Protein energy malnutrition: caused by inadequate protein and energy intakea. Common forms: marasmus and kwashiorkor21. Marasmus – grossly inadequate energy and nutrition intakea. Consequences: wasting and weakening of muscle (heart), stunted brain development and learning, depressed metabolism, stunted physical growth, deterioration of the intestinal lining (anemia), severely weakened immune system, fluid and electrolyte imbalances22. Kwashiorkor – disease resulting from low protein intakea. Sympotoms: Some weight loss and muscle wasting, retarded growth and development, edema resulting in distention of the belly, fatty degeneration of the liver, loss of appetite, sadness, irritability, apathy and skin problems/hair loss.23. Genetic disorders – caused by defective DNAa. Phenylketonuria – inherited, cannot break down phenylalaninei. Phenylalanine and metabolic byproducts build up in tissues and can cause brain damageii. Should consume a diet low in phenylalanineb. Sickle cell anemia – inherited disorder of the RBCs in people who get the gene from bothparentsi. Cells become crescent shape causing them to become hard and sticky which restricts blood flow and damages organs (spleen)ii. Sickle cells have a shorter life span – anemiaiii.


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