Chapter 6 Flashcards
Describe how proteins differ from carbohydrates and fat.
Proteins contain nitrogen
Genetic material dictates the structure of each protein molecule
Describe the process of protein synthesis.
Proteins are long chains of amino acids. Amino acids bond to form a variety of peptides.
Amino acids join together by means of a peptide bond. The amine group of one amino acid binds to the acid group of another When amino acids join together, they form peptides. Dipeptide: 2 amino acids joined together Tripeptide: 3 amino acids joined together Oligopeptide: 4 to 9 amino acids joined together Polypeptide: 10 or more amino acids joined together Genes regulate amino acid bonding. The structure of each protein is dictated by the DNA of a gene. Gene expression: The process of using a gene to make a protein. Transcription: use of the genetic information in DNA to make RNA. mRNA copies (transcribes) information from DNA in nucleus and carries to ribosomes in cytoplasm Translation: conversion of genetic information in mRNA to the amino acids sequence of a protein. Information from the mRNA is translated into a growing strand of amino acids that bind together to form a specific protein. Protein turnover involves synthesis and degradation of body proteins.
What are the building blocks of protein?
Amino Acids
Identify the parts of an amino acid molecule.
- an alpha carbon, which is the central, asymmetric carbon
- a carboxyl group at the right end of the alpha carbon
- an amino group at the left end of the alpha carbon
- an R group
- a hydrogen atom
Which part of an individual amino acid distinguishes it from other amino acids?
The R Group/side chain
What is an essential amino acid and how many are there?
A complete protein contains all 9 essential amino acids.
The most complete protein food sources include meat, poultry, fish, egg whites, milk, and soybeans. These foods are considered to be “high quality protein” foods.
How many non-essential amino acids are there?
11, these can be made by the body
Discuss how proteins are digested and absorbed by our bodies.
Stomach acids and enzymes break proteins into short polypeptides.
Hydrochloric acid (HCl) in the stomach begins protein digestion by denaturing the protein. HCl also converts inactive pepsinogen to its active form, pepsin. Pepsin begins breaking the peptide bonds between amino acids.
Enzymes in the small intestine break polypeptides into single amino acids.
Proteases from the pancreas and small intestine continue the breakdown of polypeptides in the small intestine. Amino acids, dipeptides, and tripeptides are absorbed into the cells of the intestinal wall. Enzymes in the intestinal cells further break down dipeptides and tripeptides into single amino acids. Amino acids are transported into the bloodstream.
Protein digestibility affects protein quality.
Digestibility of a protein refers to how well our bodies can digest it. Animal protein sources are highly digestible.
Proteins contribute to cell growth, repair, and maintenance.
Cells are constantly being broken down, repaired, and replaced.
When proteins in the cells are broken down, the amino acids are recycled into new proteins.
Examples: skin cells, hair cells, burn recovery
Proteins act as enzymes and hormones.
Enzymes are compounds (usually proteins) that speed up chemical reactions, without being changed by the chemical reactions themselves.
Some hormones are made from amino acids.
Hormones are substances that act as chemical messengers in the body.
Examples: glucagon, insulin, thyroid hormone
Proteins help maintain fluid and electrolyte balance.
Proteins attract fluid.
When protein intake is deficient, it can cause edema (swelling).
Transport proteins in the cell membrane help to maintain the proper balance of sodium and potassium inside and outside the cell.
Proteins help maintain acid-base balance.
Proteins are excellent buffers and help to maintain a proper blood pH.
acidosis- blood becomes acidic; level of hydrogen (H+) in blood is excessive alkalosis - blood becomes basic (alkaline); level of H+ in blood is deficient buffers - proteins that help maintain proper acid-base balance by attaching to, or releasing H+ ions
Proteins help maintain a strong immune system.
Antibodies are proteins that defend the body against foreign substances.
Each antibody is designed to defend against a specific invader.
Proteins serve as an energy source.
In healthy people, protein contributes little to energy needs.
When proteins are needed for energy, they are taken form the blood and body tissues.
To use proteins for energy, deamination is required.
deamination - amine group is removed from amino acid and nitrogen is transported to the kidney for excretion, while carbon and other components are metabolized for energy
To protect our body tissues, it is important to eat an adequate amount of fat and carbohydrate.
Our body cannot store excess protein. Excess protein intake results in nitrogen excretion; remaining components are used for energy or converted to fat for later use.
Calculate the AMDR and the recommended dietary allowance for protein.
The RDA for sedentary people is 0.8 gram per kilogram of body weight per day.
Example: 150 pound sedentary adult / 2.2 = 68.2 kg
68.2 kg x 0.8 grams/kg = 55 grams protein per day
Protein needs depend on many factors including age, activity level, etc.
The recommended percentage of energy that should come from protein is 10 to 35% of total energy intake.
Protein needs are higher for some groups, such as children, adolescents, pregnant or lactating women, vegetarians, and athletes.