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Lecture

Kin110_Chapter 6 Proteins.docx

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Department
Biomedical Physio & Kines
Course
BPK 110
Professor
Gina Whitaker
Semester
Summer

Description
Kin110 Chapter 6 Protein & Amino Acids Protein Sources-Animal High protein content; provide B vitamins and some minerals Higher in saturated fat and cholesterol; low in fiber One cup of milk provides 8g protein One egg provides 7g protein 3 ounces of meat provides over 20g protein Protein Sources-Plant Low in saturated fat and cholesterol; high in fiber, phytochemicals, and unsaturated fat 1 slice of bread provides about 2g protein ½ cup legumes (the starchy seed of a plant that provides bean pods; includes peas, peanuts, beans, soy beans, and lentils) provides about 6-10g protein ½ cup rice, pasta or cereal provides about 2-3g protein ½ cup of nuts or seeds provides 5-10 grams protein Amino Acids Amino acids-building blocks of proteins Carbon, hydrogen, amino group (contains nitrogen), acid group, and side chain 20 different side chains make 20 different amino acids Amino Acids → Peptides → Proteins Polypeptide chain-primary chain -not the final protein structure Most foods we eat are in their final protein structures however, cooking process may unravel these final protein structures Essential vs. non-essential amino acids Essential-cannot be synthesized by the body in sufficient amounts to meet its need and therefore must be included in the diet -if one is missing, body proteins such as muscle protein are broken down to make new proteins Non-essential-amino acids that can be synthesized by the body in sufficient amounts to meet needs Conditionally essential-amino acids that are essential in the diet only under certain conditions -non essential amino acids that cannot be made in adequate amounts -certain metabolic diseases Protein Denaturation-alteration of a protein’s three-dimensional structure Heat-cooking and processing Low pH-protein entering the stomach Neurodegenerative diseases-Alzheimer’s, Parkinson’s disease Protein can no longer function properly or at all Digestion of dietary protein In the mouth, chewing begins the mechanical breakdown of protein In the stomach, hydrochloric acid and the enzyme pepsin begin the chemical digestion of protein In the small intestine, protein digesting enzymes secreted from the pancreas, along with those in the microvilli break down polypeptides into amino acids, dipeptides and tripeptides A variety of transport proteins move the products of protein digestion into the mucosal cell. Some amino acids share the same transport system Dipeptides and tripeptides can enter the mucosal cell. Once inside, they are broken down into single amino acids Amino acids pass from the mucosal cell into the blood and travel to the liver, which regulates the distribution of amino acids to the rest of the body Little dietary protein is lost in the feces Amino acids in our body Amino acid pool-all the amino acids in body tissues and fluids available for use in the body Each cell in the body will have a limited pool Amino acids are not stored in a specific part of the body. They rebuild proteins in our bodies There is equilibrium between protein breakdown and synthesis Amino acid → Protein Our genes (in DNA) contain the instructions for making different proteins The first step in protein synthesis occurs inside the nucleus. It involves transferring or transcribing the blueprint or code for the protein from the DNA gene into a molecule of messenger RNA (mRNA). This process is called transcription The mRNA takes the genetic information from the nucleus of the cell to structures called ribosomes in the cell fluid where proteins are made Transfer RNA reads the genetic code and delivers the need amino acids to the ribosome to form a polypeptide chain. This process is called translation Limiting amino acids A shortage of a specific amino acid needed to make a certain protein will stop synthesis of that protein If it is a non-essential amino acid → transamination (the process by which an amino group from one amino acid is transferred to a carbon compo
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