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Q:
Which reaction is characterized as anabolic? a. Pyruvate synthesis from glucose b. Acetyl CoA synthesis from cholesterol c. Carbon dioxide synthesis from citric acid d. Cholesterol synthesis from acetyl CoA molecules e. Hydrolysis of glycogen to glucose
Q:
The site of lipid synthesis in the cell is the ____. a. nucleus b. Golgi bodies c. mitochondria d. smooth endoplasmic reticulum e. exoplasm
Q:
Which reaction is characterized as catabolic? a. Glucose formation from glycerol b. Pyruvate formation from glucose c. Albumin formation from amino acids d. Palmitic acid formation from acetate e. Formation of triglycerides from glycerol and fatty acids
Q:
In the adult body, food energy not stored as fat or glycogen is lost as ____. a. heat b. photons c. carbon dioxide d. electromagnetic radiation e. methane
Q:
What is the approximate percent efficiency of conversion of food energy to ATP energy in the body? a. 30% b. 50% c. 70% d. 90% e. 99%
Q:
Which statement defines a coenzyme? a. A unit consisting of an enzyme bound to reactants plus ATP b. An organic molecule required for the functioning of an enzyme c. The small, active part of an enzyme that binds to the organic reactants d. An inactive enzyme that becomes functional upon contact with specific cofactors e. An enzyme precursor
Q:
Which metabolic reaction occurs when a cell uses energy? a. ATP gains a phosphate group and becomes ADP. b. ADP gains a phosphate group and becomes ATP. c. ATP releases a phosphate group and becomes ADP. d. ADP releases a phosphate group and becomes ATP. e. ADP and ATP cycle back and forth repeatedly.
Q:
Which process describes the sum of all chemical reactions that go on in living cells? a. Digestion b. Metabolism c. Absorption d. Catabolism e. Anabolism
Q:
What is the major energy carrier molecule in most cells? a. ATP b. Glucose c. Pyruvate d. A kcalorie e. Acetyl CoA
Q:
Describe the signs and symptoms of phenylketonuria. What is the cause and what is the treatment?
Q:
Provide examples of how the dietary habits of grandparents can influence the body's metabolism and susceptibility to disease in future generations.
Q:
Provide several examples of beneficial and adverse consequences of activating or silencing gene expression.
Q:
What are the assumptions made by the DRI Committee in setting the RDA for protein?
Q:
What are the hazards of consuming amino acid supplements?
Q:
Explain the proposed relationships between body homocysteine levels and heart disease.
Q:
What is a limiting amino acid? What are the four amino acids most likely to be limiting in protein nutrition?
Q:
Compare and contrast the quality of protein foods derived from animals versus plants.
Q:
What is meant by nitrogen balance? How does it differ among infants, adults, and those who are injured or on weight-loss diets?
Q:
What are the signs and symptoms of sickle-cell anemia and what causes it?
Q:
List and define 5 major roles of proteins in the body.
Q:
What are the differences between transcription and translation in the synthesis of proteins?
Q:
Explain the processes of protein digestion and absorption.
Q:
Define protein denaturation and provide an example of a denatured protein.
Q:
Explain the differences among amino acids that are classified as essential, nonessential, or conditionally essential.
Q:
Matching: a. Soy b. Urea c. Pepsin d. Lysine e. Gelatin f. Alanine g. Insulin h. Infection i. Tyrosine j. Collagen k. Denatured l. Ribosome m. Enzyme n. Kwashiorkor o. Pregnancy p. Edema q. Hemoglobin r. Hydrophobic s. Homocysteine t. Buffer 1>A dietary nonessential amino acid 2>A conditionally essential amino acid 3>A small protein 4>A large protein that carries oxygen 5>Substances repelled by water 6>Describes protein exposed to severe heat 7>An active protease 8>A cell structure where protein synthesis takes place 9>A connective tissue protein 10>A protein catalyst 11>Excessive fluid residing between cells 12>Substance that keeps the pH constant 13>A condition that favors positive nitrogen balance 14>A condition that favors negative nitrogen balance 15>A product of amino acid breakdown 16>A dietary protein lacking tryptophan 17>A good quality protein source 18>A typical limiting amino acid 19>A condition of protein malnutrition 20>An amino acid associated with heart disease
Q:
The term ____________________ is used to describe the condition that develops when the diet delivers too little protein, too little energy, or both.
Q:
____________________ provide enough of all the essential amino acids needed to support the body's work.
Q:
The supply of amino acids derived from either food proteins or body proteins that collect in the cells and circulating blood and stand ready to be incorporated in proteins and other compounds or used for energy is called the ____________________.
Q:
Breaking down reactions are called ____________________ and building up reactions are called ____________________.
Q:
____________________ is the process of messenger RNA directing the sequence of amino acids and synthesis of proteins.
Q:
____________________ is the process of messenger RNA being made from a template of DNA.
Q:
____________________ enzymes on the membrane surfaces of the intestinal cells split most of the dipeptides and tripeptides into single amino acids.
Q:
The ____________________ is determined by weak electrical attractions within the polypeptide chain.
Q:
The simplest amino acid, ____________________, has a hydrogen atom as its side group.
Q:
____________________ are composed of carbon, hydrogen, oxygen, and nitrogen atoms, arranged into amino acids linked in a chain.
Q:
The area of study that examines how environmental factors influence gene expression without changing the DNA is known as ____. a. genetics b. genomics c. nutritional genomics d. epigenetics e. nutrigenetics
Q:
A variation in a single nucleotide of a DNA strand is called a(n) ____. a. RNA switch b. thymine substitution c. environmental mutation d. single nucleotide polymorphism e. replication failure
Q:
Dietary restriction of phenylalanine combined with adequate tyrosine is the usual treatment for people born with the disorder ____. a. DNA b. ALC c. NLM d. PKU e. BHA
Q:
The study of how food interacts with genes is known as ____. a. nutritional genomics b. chromosomal nutrition c. nucleotide expression d. mutagenic expression e. personalized nutrition
Q:
The disease phenylketonuria is related chiefly to abnormal metabolism of ____. a. lactose b. omega-3 fats c. soy polysaccharides d. a specific amino acid e. glucose
Q:
What amino acid supplement has been advertised in the popular media for treating herpes infections? a. Lysine b. Arginine c. Tryptophan d. Phenylalanine e. Methionine
Q:
What amino acid has been linked to the development of the rare blood disorder eosinophilia-myalgia syndrome in people who took it as a supplement? a. Glycine b. Arginine c. Tryptophan d. Phenylalanine e. Proline
Q:
Which of the following is a feature of whey protein? a. It is a high-priced protein supplement. b. It is chemically extracted from gelatin. c. It is a waste product of cheese production. d. It enhances athletic performance when regularly consumed. e. It is no longer legal to use in over-the-counter products
Q:
Which of the following is an assumption made in the formulation of the RDA for protein? a. Dietary protein is of high quality only. b. Dietary protein is of animal origin only. c. Dietary carbohydrate and fat intakes are adequate. d. Dietary protein should represent 12% of total energy. e. Dietary protein needs are lower in infants and children.
Q:
What is a feature of the protein RDA? a. The recommendations are generous. b. The recommendations are highest proportionately for adult males. c. The recommendations are established at 8 grams per kilogram of ideal body weight. d. The recommendations assume that dietary protein is from animal sources only. e. The recommendations fail to consider the need to replace damaged tissues.
Q:
What would be the primary principle of wise diet planning as related to protein nutrition? a. Variety b. Moderation c. Nutrient density d. kCalorie control e. Balance
Q:
What is the actual ratio of calcium to protein intake (mg to g) for most U.S. women? a. 3:1 b. 9:1 c. 13:1 d. 21:1 e. 36:1
Q:
Which statement describes an association between protein intake and kidney function? a. Low-protein diets increase the risk for kidney stone formation. b. Restricting protein intake may slow the progression of kidney disease. c. High protein intakes over the long term represent a risk factor for kidney disease. d. Liberal protein intakes result in high urea production, which increases the long-term efficiency of the kidneys. e. High protein diets in childhood protect the kidneys from age- and illness-associated damage.
Q:
Which statement describe a relationship between protein/amino acids and heart disease? a. Substituting soy protein for animal protein raises blood cholesterol levels. b. High blood levels of the amino acid arginine are a risk factor for atherosclerosis. c. High levels of homocysteine in food promote elevation of blood low-density lipoproteins. d. Elevated blood homocysteine levels are associated with smoking cigarettes and drinking alcohol. e. High blood levels of phenylalanine dampen inflammatory responses, reducing risk of heart disease.
Q:
Which amino acid has been reported to lower blood pressure and reduce homocysteine levels? a. Arginine b. Cysteine c. Tryptophan d. Phenylalanine e. Methionine
Q:
Excessive amounts of homocysteine in the blood are thought to increase the risk for ____. a. cancer b. diabetes c. heart disease d. protein-energy malnutrition e. hypothyroidism
Q:
In general, the protein quality of legumes would be most improved by the addition of a plant protein rich in ____. a. lysine b. tyrosine c. methionine d. glutamic acid e. phenylalanine
Q:
In general, the protein quality in grains would be most improved by the addition of a plant protein rich in ____. a. lysine b. tryptophan c. phenylalanine d. glutamic acid e. methionine
Q:
Which statement characterizes the protein nutrition in vegetarians? a. Vegetarians in general must practice complementary protein nutrition. b. Most vegetarians should consume gelatin to ensure adequate tryptophan intake. c. Healthy vegetarians typically consume protein sources of very high digestibility. d. Most vegetarians eating a variety of foods need not balance essential amino acid intake at each meal. e. A significant majority of vegetarians experience clinically significant protein malnutrition.
Q:
What is a "limiting" amino acid in a protein? a. A nonessential amino acid present in high amounts, which inhibits protein synthesis b. An amino acid of the wrong structure to be utilized for protein synthesis efficiently c. An essential amino acid present in insufficient quantity for body protein synthesis to take place d. An amino acid that limits the absorption of other essential amino acids by competing with them for transport sites within the GI tract e. An amino acid that has the paradoxical effect of causing catabolism
Q:
If the diet is lacking an essential amino acid, what will be the likely course of action? a. Body cells will synthesize it. b. Protein synthesis will be limited. c. Health will not be affected as long as other nutrients are adequate. d. Proteins will be made but they will lack that particular amino acid. e. Massive muscle wasting will occur.
Q:
Which animal-derived protein is classified as a poor-quality protein? a. Fish b. Cheese c. Gelatin d. Turkey e. Fatty fish
Q:
Which of the following food proteins has the best assortment of essential amino acids for the human body? a. Egg b. Rice c. Corn d. Gelatin e. Soy
Q:
What is the percent digestibility of most animal proteins? a. 50-59 b. 60-69 c. 70-79 d. 80-89 e. 90-99
Q:
What is the percent digestibility of most plant proteins? a. 30-50 b. 50-60 c. 60-70 d. 70-90 e. 90-99
Q:
What is the most likely reason for having an abnormally high blood urea level? a. Liver dysfunction b. Kidney dysfunction c. Protein intake twice the RDA d. Protein intake one-tenth the RDA e. Hyperstimulation of the immune system
Q:
What is the most likely reason for a person to have abnormally high blood ammonia levels? a. Liver dysfunction b. Kidney dysfunction c. Protein intake twice the RDA d. Protein intake one-tenth the RDA e. Hyperstimulation of the immune system
Q:
In the metabolism of amino acids for energy, what is the fate of the amino group? a. Excreted as urea b. Burned for energy c. Stored in the liver d. Converted to glucose e. Recycled in the liver
Q:
What is the process whereby an amino group is combined with a keto acid to form an amino acid? a. Deamination b. Ureagenesis c. Transamination d. Ammoniogenesis e. Ketoacidosis
Q:
What is a consequence of excess protein intake? a. Decreased excretion of calcium b. Decreased size of the liver and kidneys c. Increased production and excretion of urea d. Increased protein storage by the liver and kidneys e. Improved renal functioning
Q:
What is the most likely side effect of a high-protein, low-carbohydrate diet? a. Diarrhea b. Increased thirst c. Nitrogen toxicity d. Increased water retention in the body e. Weight gain
Q:
Approximately how much urea (g) can be produced daily by the average adult? a. 5 g b. 50 g c. 100 g d. 250 g e. 500 g
Q:
Protein sparing in the body is best achieved when a person ingests ____. a. proteins of plant origin only b. proteins of animal origin only c. adequate levels of carbohydrate and fat d. mixed protein sources on alternate days e. consumes a very low fat diet
Q:
When amino acids are deaminated, the immediate products are ammonia and often a ____. a. uric acid b. keto acid c. folic acid d. gluco acid e. phyto acid
Q:
What is meant by protein turnover? a. Nitrogen equilibrium b. The antibody-antigen complex c. The synthesis and degradation of body proteins d. The secondary structure of proteins that initiates folding e. The failure of the body to form needed proteins
Q:
What amino acid is used to synthesize the neurotransmitter serotonin and the vitamin niacin? a. Glycine b. Tyrosine c. Methionine d. Tryptophan e. Valine
Q:
What is the usual state of nitrogen balance for healthy infants, children, and pregnant women? a. Equilibrium b. Metabolic c. Positive d. Negative e. Homeostatic
Q:
What is the amino acid pool? a. The total amino acid content derived from a 24-hour dietary intake b. A measure of the circulating essential amino acid levels available for protein synthesis c. The total amount of free amino acids in the circulation destined for deamination and excretion d. A mix of essential and nonessential amino acids derived from protein breakdown and dietary protein intake e. The essential and nonessential amino acids from dietary intake that are available for protein synthesis
Q:
When nitrogen taken into the body exceeds nitrogen losses, we say the person is in ____. a. a healthy state b. nitrogen equilibrium c. positive nitrogen balance d. negative nitrogen balance e. nitrogen homeostasis
Q:
Which of the following may be used to determine protein utilization? a. Calorimetry b. Nitrogen balance c. Amino acid pool d. Supplementary value e. Body mass index
Q:
Which substance is involved in the clotting of blood? a. Opsin b. Fibrin c. Collagen d. Transferrin e. Thyroxin
Q:
Which of the following describes the structure of an antibody? a. Tripeptide b. Small nucleic acid c. Huge protein molecule d. Large peptide molecule e. Location of carbons
Q:
What is opsin? a. An antigen b. An antibody c. A light-sensitive protein d. A blood transport protein e. A sterol
Q:
How do sodium and potassium travel into and out of cells? a. Antidiuretic hormone transports potassium and prodiuretic hormone carries sodium. b. Specific transport proteins in the blood deliver the minerals to the cell cytoplasm. c. The balance of insulin and glucagon determines the movement of these minerals into and out of cells. d. Transport proteins within the cell membrane pick up and release the minerals across the membrane. e. A negative feedback loop uses blood glucose levels for transfer.
Q:
What function does a buffer perform? a. It helps emulsify fats. b. It helps maintain a constant pH. c. It facilitates chemical reactions. d. It helps protect against plaque buildup. e. It prevents degradation of proteins.