Chapter 6: Protein Flashcards
Acid-Base Balance
The process of achieving, or the state of, equilibrium between acidic and alkaline molecules.
Cell Signaling
Process of communication between cells by biological messengers to govern cellular function.
Organic Molecules
Chemical structures containing only carbon, hydrogen, oxygen, and/or nitrogen.
Amino Acids
The organic building blocks of proteins containing both a carboxyl and an amino group.
Essential Amino Acid (EAA)
Amino acids that are necessary for bodily functions but cannot be synthesized by the body and, therefore, must be obtained in the diet.
Branched Chain Amino Acid
The three essential amino acids (leucine, isoleucine, and valine) which are abundant in skeletal muscle tissue and named for their branch-like structure.
Conditionally Essential Amino Acids
Amino acids that are not typically essential, but can become essential during times of extreme dietary insufficiency, illness, or trauma.
Nonessential Amino Acids
Amino acids that can be synthesized by the body and do not, under normal circumstances, need to be obtained in the diet.
Gluconeogenesis
A metabolic pathway that results in the generation of glucose from non-carbohydrate carbon substrates such as lactate, glycerol, and glucogenic amino acids.
Protein Synthesis
Process of joining amino acids with peptide bonds to form proteins.
Dehydration Synthesis
The joining of two large molecules by removing one hydrogen from one molecule and a hydroxyl group (OH) from another molecule and then binding the two larger molecules together on the newly freed bonds.
Peptide Bond
The bond between two amino acids, occurring between the carboxyl group of one and the amino group of the other.
Hydrolysis
Breakdown of one large molecule into two smaller molecules via the donation of one hydrogen and one hydroxyl group from water to the smaller molecules, respectively.
Dipeptide
A chain of two amino acids.
Tripeptide
A chain of three amino acids.
Oligopeptide
A chain of four to nine amino acids.
Polypeptide
A chain of 10 or more amino acids.
What is the molecular component that makes each individual amino acid unique?
Side chain
Which protein is one of the largest polypeptides in the body and gives muscles their property of elasticity?
Titin
Denaturation
The process of changing a protein‘s shape.
Gastrin
A hormone released when food is ingested to stimulate release of digestive fluids.
Pepsinogen
A proenzyme secreted by the stomach as a precursor to pepsin.
Pepsin
An enzyme in the stomach that begins breaking peptide bonds.
Duodenum
It is the first section of the small intestine where some digestion occurs, and it is located immediately after the stomach and leads into the jejunum.
Secretin
A hormone that stimulates the liver and pancreas to produce bile and bicarbonate; inhibits gastrin release.
Cholecystokinin
A hormone secreted by the duodenum that causes release of enzymes and bile.
Protease Enzymes
Enzymes in the small intestine that break long peptide chains into shorter peptide chains.
Peptidase
An enzyme that breaks down small peptides.
Aminopeptidases
Enzymes that cleave individual amino acids from a peptide chain so they may be absorbed.
Hepatic Portal Vein
The vein that transports blood from the spleen, stomach, pancreas, and the intestinal tract to the liver.
Collagen
A protein formed of a triple-helix structure with great tensile strength, found primarily in skin, muscles/connective tissue, and bones.
Tensile Strength
Ability of a material to resist breaking under tension.
Elastin
A protein with high elasticity, found mainly in the skin.
Keratin
A protein found in hair and nails.
Sodium-Potassium Pump
A protein found on the cell membrane that transports sodium and potassium to create electrochemical gradients across the membrane.
Albumin
A protein found in the blood stream that helps draw water into the blood vessel from surrounding tissue.
Hemoglobin
An iron-containing protein found on red blood cells, binds oxygen and other molecules for transport in the blood.
What is the final step in protein digestion and absorption that occurs once all peptide chains have been broken down into their individual amino acids?
Absorbed into the portal vein and processed through the liver
Which protein has a triple helix molecular structure and works with calcium to form bones?
Collagen
Recommended Dietary Allowance (RDA)
Amount of nutrient needed to meet the needs of almost all individuals in an age-sex group.
Protein Quality
The quantity of essential amino acids found in, and the digestibility of, a protein.
Complete Protein
A protein that contains sufficient quantities of all essential amino acids.
Complementary Protein
Two incomplete proteins that, when comsumed together, mimic a complete protein by providing all essential amino acids.
According to the USDA My Plate, what percentage of one’s diet should come from high-protein sources?
20-25%
What is the recommended dietary allowance (RDA) for protein seeking to address for the population?
General intake needs to avoid adverse health effects
How much daily protein is recommended for someone who participates in regular moderate-intensity resistance training?
1.5-2.0 g/kgBW
True or False? Performing resistance training while consuming a high protein diet consisting of 1.8-2.2 g/kgBW daily protein can help maintain muscle mass during a calorie-restricted weight loss diet.
True
Which amino acid is responsible for signaling for muscle protein synthesis, and is the only amino acid independently capable of enhancing muscle anabolism?
Leucine
Which protein timing strategy has been shown through research to be the most optimal for continued muscle protein synthesis throughout the day?
4 meals with 20g protein each
What is dehydration synthesis?
Removal of 2 hydrogens and 1 oxygen from 2 different molecules when the 2 molecules are joined together
Which is most likely to impact longevity?
Calorie restriction may enhance longevity.
What are enzymes?
Protein-based structures which catalyze chemical reactions
Which of the following is the best protocol for fat loss while maintaining muscle mass?
A calorie-restricted, high-protein (1.8-2.2 g/kg body weight) diet & resistance training
What is the primary reason that plant proteins tend to make it more difficult to gain muscle compared to animal proteins?
Plant proteins do not have as many essential amino acids.
If a new client reveals they have kidney disease, what should the Nutrition Coach do?
Work with their registered dietitian or medical doctor for dietary guidance.
Can post-workout protein consumption increase muscle glycogen synthesis?
Yes, when consumed with carbohydrates.
Is post-workout protein consumption more important for novice or experienced weightlifters?
Experienced
Which of the following may be the most optimal protein distribution pattern for a 70kg client with a goal to build muscle?
4 meals, each with 21g protein
Ketogenic amino acids may become which 2 molecules that can be used to produce ATP?
Acetyl-CoA and acetoacetate
Protein is involved in forming which of the following?
Bones
A new client with goals to lose a little body fat and build a little bit of muscle describes their current eating pattern as normal, consisting of breakfast, lunch, dinner, and sometimes a snack or dessert. Should a Nutrition Coach recommend they eat more or less frequently to help them meet their goals?
No changes to meal frequency should be recommended.
Which of the following is true about high-protein snacks?
Protein-based snacks without excess fats or carbohydrates can enhance satiety and, therefore, weight loss.
In general, what sources are complete proteins?
Animal-based products
What are the essential amino acids?
Histidine, lysine, methionine, phenylalanine, threonine, tryptophan, leucine, isoleucine, valine
