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Nutrition Notes Week 9

by: Alyssa Anderson

Nutrition Notes Week 9 NTRI 2000

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Alyssa Anderson

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These notes cover what we went over the 9th week of school. It is the start of the material for the next exam.
Nutrition and Health
Dr. Greene
Class Notes
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This 6 page Class Notes was uploaded by Alyssa Anderson on Wednesday March 9, 2016. The Class Notes belongs to NTRI 2000 at a university taught by Dr. Greene in Spring 2016. Since its upload, it has received 16 views.


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Date Created: 03/09/16
Nutrition Notes Week 9 Protein Overview A. The body is made up of thousands of proteins B. They contain nitrogen, carbon, hydrogen, & oxygen C. General functions 1. Regulates & maintains body functions 2. Provides essential form of nitrogen (in the form of amino acids) D. In the developed world: 1. Diet is typically rich in protein (is this an issue?) 2. Association between protein intake & mortality 3. Age 50-65 —> decrease in overall, cancer, & diabetes mortality 4. Ages 66+ —> increase in overall/cancer mortality, decrease in diabetes mortality E. In the developing world: 1. Protein deficiency is an issue 2. Important to focus on protein intake in diet planning 3. Aside from water, protein makes up the major part of the lean body tissue Protein structure A. Amino acids are the building blocks of proteins B. Contain nitrogen bonded to carbon C. Makes them unique from carbohydrates and fats D. The proteins in our bodies are made up of 20 different amino acids (actually 21, but standard science says 20) E. Nine are essential (Some are limiting, meaning they have very low amounts in particular foods) F. Eleven are nonessential G. New category 1. Conditionally or acquired indispensable 2. Infants or disease states H. Structure 1. Central carbon 2. Acid group 3. Amino group 4. Side group (Different for each amino acid - gives own characteristics) 5. Hydrogen 6. Peptide bond a. Amino acids are connected together by a peptide bond b. Two amino acids - dipeptide; three amino acids - tripeptide, etc c. Many amino acids - polypeptide d. Some proteins contain multiple polypeptide chains I. Sequence of amino acids is called the protein primary structure (coded in DNA) J. Primary structure leads to the protein higher order structure K. Higher order structure causes the protein to get into a specific shape (native conformation) L. Shape is necessary for the protein to work properly Disruption of normal structure A. Denaturation 1. Heat 2. Strong acids 3. Bases 4. Heavy metals B. Protein basically unfolds 1. Structure is important in proper functioning 2. Only have to change structure a little bit for it to not work properly Protein primary structure A. Determined by the genes (DNA) - kept in the cell’s nucleus 1. Info of the primary structure gets transcribed into messenger RNA (mRNA) 2. mRNA leaves the nucleus & goes tot the ribosome (rough ER) where the protein gets translated (made) B. Protein synthesis 1. DNA contains coded instructions 2. Copies of codes are transferred to the cytoplasm (via mRNA) 3. Amino acids added one at a time 4. With aid of transfer RNA (tRNA) 5. Requires energy Central dogma of biology A. DNA —><— RNA —> protein B. How to change protein structure 1. Genetic alterations 2. Can change the protein’s primary structure 3. Sometimes this isn't a big deal (silent mutation) 4. Sometimes causes significant change in amino acid, which can lead to genetic diseases, such as sickle cell anemia a. A single-base substitution: causes one amino acid to be changed in the polypeptide of the hemoglobin protein b. Alters the higher order structure of the protein c. Protein doesn't work as efficiently (as unaltered version) d. Hemoglobin binds oxygen in red blood cells (heme actually binds) e. RBC have sickle shapes instead of biconcave Digestion of proteins A. Pre-digestion: cooking (slicing the meat), heat denatures proteins, softens food B. Digestion begins in the stomach 1. Acid (HCl) denatures protein 2. Pepsin (enzyme) breaks down peptide bond of proteins resulting protein fragments C. What controls pepsin & stomach acid release? 1. Gastrin - hormone 2. Released in response to thinking about food and chewing and digesting food D. Partially digested proteins and other nutrients is called chyme E. Movement to small intestine once processed into chyme 1. Release of CCK (hormone) movement of chyme into small intestine stimulates cells to release CCK 2. CCK caused pancreas to release proteolytic enzymes (trypsin, chymotrypsin) (proteolytic: cleaving proteins) 3. Pepsin inactivation (elevated pH) F. Several peptidases are found in brush border 1. Small peptides (2-3 amino acid in length) & free amino acids are absorbed by active transport 2. Any intracellular peptides are digested by enzymes within cells 3. Taken up by capillaries and taken to the liver via the portal vein 4. Free amino acids used as building blocks for liver proteins are then broken down for energy, released into blood, and converted to nonessential amino acids, glucose or fat G. Sensitivity to proteins 1. Gluten / Gluten sensitivity (celiac disease) a. Protein found in grains like wheat, rye, and barely that gives backed goods their bought, elastic structure b. Incomplete gluten breakdown in small intestine leaving small peptides and amino acids c. Celiac disease-inflammatory response to small peptides/ amino acids d. Autoimmune response, genetic predisposition (immune system attacks “foreign” bodies; autoimmune: attacking self) e. Prevalence is 1 in 133 f. In people with related symptoms: 1 in 56 g. Blood test looks for antibodies which results in a biopsy of intestines h. If positive, remove all gluten from diet Function of protein in body A. Producing vital body structures 1. Body is in a state of constant protein turnover 2. Producing proteins & disassembling proteins B. What happens with protein inadequacy? 1. Muscles, blood proteins, & vital organs decrease in size 2. Brain resists breakdown C. Maintain fluid balance 1. Blood proteins attract fluids 2. Fluid shifts into tissues - edema D. Contributes to acid-base balance 1. Act as buffers - maintain pH within a narrow range 2. Keeps blood slightly alkaline E. Form hormones and enzymes 1. Hormones- communication between cells 2. Enzymes- Catalyzes reactions in cells F. Transport and signaling receptors 1. Transport- bring nutrients into the cell 2. Signaling receptors 3. Communication in the cell G. Immune function 1. Antibodies production (move DNA around to come up with new combinations) 2. What happens with protein inadequacy? Decrease in immune function H. Providing energy (direct) and indirect (glucose) I. Contribute to satiety Infant digestion of proteins A. Up to 4 fo 5 months of age B. The GI tract is somewhat permeable to small proteins (whole proteins can be absorbed) C. If breastfed, this allows antibodies to be passed from mother to baby (immune system is learning difference between self and foreign) D. Waiting until the infant is at least 6-12 months of age before introducing some foods than can cause allergies (introduce in a step-by-step manner)


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