Protein Flashcards
Acid–Base Balance
The process of achieving, or the state of, equilibrium between acidic and alkaline molecules.
Amino Acids
The organic building blocks of proteins containing both a carboxyl and an amino group.
second-most abundant molecule in fat-free bodily tissues
protein
role of protein
acid–base balance, energy production, cell signaling, and nutrient transport
what elements form the amino acids?
carbon (C), hydrogen (H), oxygen (O), and nitrogen (N)
how many amino acids are needed in the body?
20
five components of amino acid structure
a central carbon, a carboxyl group (organic acid – COOH), a hydrogen, an amino group (NH2), and a side chain (R 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 list
Alanine
Asparagine
Aspartic acid
Glutamic acid
Serine
conditionally essential amino acids list
Arginine
Cysteine
Glutamine
Glycine
Proline
Tyrosine
essential amino acids list
Histidine
Lysine
Methionine
Phenylalanine
Threonine
Tryptophan
branch chain amino acid list
Isoleucine
Leucine
Valine
Gluconeogenesis
A metabolic pathway that results in the generation of glucose from non-carbohydrate carbon substrates such as lactate, glycerol, and glucogenic amino acids.
Glucogenic amino acids
amino acids that can have their carbon backbone converted to glucose by the process of gluconeogenesis, or they can be converted to an intermediate compound that may enter the Krebs cycle directly
Ketogenic amino acids
amino acids that may become acetoacetate (a ketone body) or acetyl-CoA prior to entering the Krebs cycle for the generation of ATP.
Glucogenic amino acid list
Alanine
Asparagine
Aspartic acid
Cysteine
Valine
Glutamic acid
Glutamine
Glycine
Proline
Serine
Arginine
Histidine
Methionine
how many glucogenic amino acids are there?
13
ketogenic amino acid list
Leucine
Lysine
how many ketogenic amino acids are there?
2
Glucogenic or Ketogenic amino acid list
Tyrosine
Isoleucine
Tryptophan
Phenylalanine
Threonine
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.
How are nonessential amino acids made?
They’re made by breaking other amino acid or nitrogen-containing compounds apart, and then reusing the components.
In order to make tyrosine, you need to eat enough ______
Phenylalanine
Can your body store amino acids?
No
Proteins are part of every bodily fluid except……
Bile and urine
Plant sources of complete protein
Quinoa and soy
_______ and ________ help muscles contract to make your body move
Actin and myosin
What amino acid helps keep blood vessels open?
L-arginine
What amino acid is part of epinephrine and norepinephrine?
Tyrosine
What amino acid is needed for serotonin?
Tryptophan
______ is a protein that helps transport oxygen in blood to body cells
Hemoglobin
Kwashiorkor
A form of protein deficiency that results in muscle loss, failure to grow, lower immunity, increased risk for disease, and weakened respiratory and cardiovascular systems
Marasmus
A type of severe protein energy malnutrition that causes a debilitating amount of muscle loss and often death
What does the body do with excess protein?
It breaks down and converts into body fat or glycogen for energy storage. It’s nitrogen containing components are removed and excreted through urine by the kidneys
Which amino acids are more limited in plant foods?
Cysteine
Lysine
Methionine
Tryptophan
Beans are high in _______ but low in ________ and _________
Lysine, cysteine and methionine
Nuts, seeds and grains are high in ______ and ________ but limited in _________
Menthionine and cysteine, lysine
Rice is high in _________ but limited in _______
Methionine, lysine
Corn is high in _________ but is low in ______ and _______
Methionine, lysine and tryptophan
On labels, high protein =
10 g or more per serving
On labels, good source of protein =
5 to 9.9 g per serving
On a label, more/extra/plus protein =
At least 5 g *more per serving
On a label, fortified/enriched with protein =
At least 5g *more per serving
Sarcopenia
The progressive decline in muscle mass and strength that happens naturally with aging
50% of bone volume is ….
Protein
Soys’s two main isoflavones- _________ and _______, have weak estrogen like effects
Genistein and daidzein
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.
When proteins are consumed, they must first be broken down into ___________________by digestion to be absorbed in the ______________.
amino acids, intestines
after protein is absorbed, it can be transported to ________________ tissues and recombined to form new proteins such as ___________, __________, and ______________.
peripheral
collagen, myosin, hemoglobin
Bodily proteins are most often formed by at least _______ amino acids.
50
Oligopeptide
A chain of four to nine amino acids.
Polypeptide
A chain of 10 or more amino acids.
The three major muscle proteins are:
myosin, actin, titin
titin has about __________ amino acids
30,000 amino acids
myosin has about ________ amino acids
6,000 amino acids
actin has about ______ amino acids
400 amino acids
___________uses energy from ATP to grab ________ and flex in unison with many other myosin proteins to produce a muscle contraction.
myosin, actin
function of titin
helps provide a muscle’s elasticity so it can return to its resting length following muscle contractions.
which protein stretches over the entire muscle cell?
titin
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.
protein need for no activity
0.8 to 1.2 g/kg body weight
protein need for light to moderate cardiovascular activity
1.2 to 1.6 g/kg body weight
protein need for Light to Moderate resistance training
1.5 to 2.0 g/kg body weight
protein need for Moderate to Vigerous cardiovascular activity
1.5 to 2.0 g/kg body weight
protein need for Moderate to Vigerous resistance training
1.7 to 2.2 g/kg body weight
what is NH2?
the amino group
what is the organic acid of a carboxyl group?
COOH
What is the byproduct of dehydration synthesis?
water
what are the reactants in dehydration synthesis?
hydrogen from one amino acid and a hydroxyl group (OH) from a second amino acid
what bond joins the amino acid and the hydroxyl group in a dehydration synthesis?
peptide bond
what causes denaturation?
temperature, pH, and enzymes, cooking
Unlike with carbohydrates and fats, enzymes for protein in the __________ are relatively inactive and do little to aid in digestion.
saliva
chewing food causes the stomach wall to release _________ in anticipation of the digestion process
gastrin
gastrin causes the release of ____________________ and the hormone _____________ in the stomach.
hydrochloric acid and pepsinogen
When pepsinogen contacts the hydrochloric acid, it releases the active enzyme _________
pepsin
______________ acid denatures the protein and _______ begins breaking the very long polypeptide chains into smaller peptide chains (hydrolysis reaction).
hydrochloric acid, pepsin
the breaking of polypeptide chains into smaller peptide chains due to pepsin
hydrolysis reaction
As the food passes from the stomach into the duodenum of the small intestine, the intestinal cells release the hormones _______ and _____________
secretin, cholecystokinin
function of secretin
acts as a regulator of digestion, reducing acid release to help restore pH when eating ceases
Cholecystokinin causes the pancreas to release what enzymes into the small intestine?
the protease enzymes trypsin, chymotrypsin, carboxypeptidase, and elastase
which enzymes break peptides into single amino acids?
peptidases and aminopeptidases
what carries amino acids and dipeptides to the liver?
the hepatic portal vein
what percent of plant protein can be absorbed?
85%
what percent of animal protein can be absorbed?
95%
what amino acids form collagen?
glycine, proline, and hydroxyproline
collagen has a ____________ structure
triple helix
protein RDA for women
46 g
protein RDA for men
56 g
protein needs for no activity
0.8 to 1.2 g/kg body weight
protein needs for light/mid cardiovascular exercise
1.2 to 1.6 g/kg body weight
protein needs for light/mid resistance exercise
1.5 to 2.0 g/kg body weight
protein needs for mid-hard cardio
1.5 to 2.0 g/kg
protein needs for mid-hard resistance
1.7 to 2.2
Maintaining as much muscle mass as possible while dieting can be achieved with at least ______________ grams per kilogram of protein and regular resistance training
1.8 to 2.2 grams per kilogram
individuals 65 years of age and older consume at least _____ to ______ grams of protein per kilogram bodyweight
0.9 to 1.6
24-hour net muscle protein synthesis may be optimal if stimulated with dietary protein (containing leucine) every _______ hours
3 hours
Post-workout protein consumption with carbohydrates in a ______ or ______ ratio of carbohydrates to protein can accelerate the replenishment of muscle glycogen
3:1 or 4:1
PVT stands for
phenylalanine, valine,
