Science of Human Nutrition Week 10 notes
Science of Human Nutrition Week 10 notes 23511
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This 3 page Class Notes was uploaded by Layne Henwood on Sunday April 3, 2016. The Class Notes belongs to 23511 at Kent State University taught by Carmen Blakely-Adams in Spring 2016. Since its upload, it has received 39 views. For similar materials see Science of Human Nutrition in Nutrition and Food Sciences at Kent State University.
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Date Created: 04/03/16
Proteins Major Functions of Protein in the Body Structure o Basic structure of tissues, bones, teeth and skin Catalysis o Enzymes Movement o Found in muscles, ligaments and tendons Transport o Movement of substances across cell membranes and within the circulatory system Communication o Protein hormones and cell-signaling proteins o Hormones made of proteins Protection o Skin proteins and immune protein o Can develop sores on skin Regulation of fluid balance o Regulate the distribution of fluid in the body Regulation of pH o Maintain the pH of the body Gluconeogenesis o Synthesis of glucose o Production of glucose form a non carbohydrate protein o Do not want this to occur Happens in malnutrition and starvation Getting protein from muscle mass Calculations All healthy people require .8 grams of protein per kilogram Healthy person o 200 lbs- what are protein needs? 200/2.2=91 91x.8=73 grams of protein o 85 kg- what are protein needs? 85x.8=68 grams of protein AMDR (acceptable macronutrient distribution ranges) for protein in 10-35% o How many grams of protein is needed? o 2000 kcals with 15% protein 2000*.15=300 300/4=75 o 1800 kcals with 30% protein 1800*.3=540 540/4=135 o 1200 kcals with 10% protein 1200*.1=120 120/4=30 What are Proteins Complex molecules o Amino acids Peptide bonds- how they are linked together Condensation reaction- how they are developed (water is released) o Nitrogen base o Classification Number of amino acids linked together Oligopeptides- smaller units between 2-12 amino acids linked together Polypeptides- greater than 12 amino acids linked together Amino acids o 3 common parts Central carbon bonded to a hydrogen R-group with determine the characteristic of the protein o Classifications Essential- 9 amino acids Coming from the diet Histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine Nonessential- 11 amino acids Body can make them Conditionally essential- 6 amino acids Normally they are nonessential but something has happened o Transamination Process of making nonessential amino acids How? Body will transfer an amino group (NH2) from one amino acid to another organic compound Organic compound will not have an amino group in it, compound is called a-keto acid A-keto acid Are All food proteins equal? Categorization of food proteins o Complete protein source Have all of the essential amino acids we require High in bioavailability, not only do they have it but our bodies can also absorb it Ex. Poultry, meat, eggs, nuts, beans, dairy products o Incomplete protein sources Missing one or more essential amino acids Ex. Plant foods, pasta, grains, fruits, vegetables, cereals o Protein complementation Having an incomplete matched with a complete protein o Protein quality High quality protein Meat, poultry, nuts, dairy products Low quality protein Pastas, breads, fruits, vegetables, cereals GMOs Change in the DNA to improve the quality of a food, especially protein How are proteins made? Step 1: cell signaling initiates protein synthesis o Up-regulation Signals cell to turn on the ability to start making protein o Down-regulation Signals cell to turn off the ability to start making protein Step 2: transcription transfers genetic info o Chromosomes and genes Genes determine what type of amino acids need to be made and their sequence o Messenger ribonucleic acid (mRNA) Decodes information given by genes, determines translation Combines with ribosomes Step 3: Translation produces new peptide o Ribosomes Translate the information o Transfer ribonucleic acid (tRNA) Transports information to cell to make the amino acid How do proteins get their shape? Primary structure o How many amino acids in each link and what is their sequence o Critical to function of protein Secondary structure o Shape o A-helix (alpha helix) Looks like a spiral staircase o B-pleated sheet (beta folded) Look like a folded fan Tertiary structure o Folding due to R-group interactions R-groups coil around each other Quaternary structure o Two or more peptide chains come together o In all of the protein there is a non protein element (called Heme) o Prosthetic groups
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