Chapter 7
used for energy converted to other compounds, such as glucose
After deamination, the remaining carbon skeleton can be:
trypsin and chymotrypsin
After polypeptides enter the small intestine, the pancreas secretes protein-splitting enzymes:
peptide bond
Amino acids are chemically linked together via the acid group of one amino acid and the amino group of the next one, forming a:
amino acid pool to use for future protein synthesis
Amino acids not incorporated into proteins become part of an:
Seeds, tree nuts, legumes supply more Fruits or edible leaves, roots, flowers, and stems of vegetables provide less
Certain parts of plants provide more protein than other parts:
dipeptides, tripeptides, and individual amino acids
Enzymes released by absorptive cells break down shortened peptides into:
15%
Protein comprises about what percentage of the typical adult American's total energy intake?
Pregnancy, Breastfeeding, Periods of rapid growth, Recovery from serious illness, blood losses, burns
Protein needs increase during:
Can be used as a marker of protein intake Normal values are 12 to 20 g in a 24-hour urine sample
UUN:
deamination
Unnecessary amino acids undergo:
denaturation
When exposed to certain conditions, a protein undergoes unfolding in a process called:
tripe-tides
molecules that consist of three amino acids
amino acids
nitrogen-containing chemical units that constitute proteins
tyrosine
precursor for epinephrine
tryptophan
precursor for serotonin
carbon skeleton
remains of an amino acid following deamination
secondary structure
the coiling of a polypeptide chain
tertiary structure
the three dimensional, twisted structure of a polypeptide chain that includes interactions between various amino acid groups on the chain
endogenous
within the body
0.8 g/kg of healthy body weight
A healthy adult's RDA for protein is:
Travel to the liver via hepatic portal vein Liver keeps some amino acids and releases the rest into circulation
After absorption, the peptides are broken down into amino acids, and the amino acids enter the capillary of villus:
capillary of villus
After absorption, the peptides are broken down into amino acids, and the amino acids enter the:
denaturation
Altering a protein's natural shape and function by exposing it to conditions such as heat, acids, and physical agitation
Used to assess kidney function Normal values are 6 to 20 mg/dL
BUN:
nitrogen balance (equilibrium)
Balancing nitrogen intake with nitrogen losses
trypsin and chymotrypsin
Break down polypeptides into shorter peptides and amino acids
Hydrogen atom Amino or nitrogen-containing group R group (side chain) carboxylic acid group
Each amino acid has a carbon atom that anchors:
nitrogen balance (equilibrium)
In a healthy adult, the body maintains its protein content by maintaining:
ammonia
NH3, a potentially toxic waste product
amino acid derivatives
Nitrogen-containing compounds that are not proteins but have important physiological roles
R group (side chain)
Part of an amino acid that determines its physical and chemical properties
specific carrier systems
Short peptides and amino acids move into absorptive cells via:
nitrogen, providing about two-thirds of the amino acid supply The remaining one-third is from exogenous sources
The amino acid pool is an endogenous source of:
amino acid derivatives
The body uses amino acids as precursors to form:
peptide bond
The chemical attraction that connects two amino acids together
Absorbed directly by microvilli Further broken down into amino acids by enzymes within the microvilli
The dipeptides and tripeptides can be:
function
The shape of a protein is important because it determines its:
reversible
Transamination reactions are:
NH2 is transported to liver (as glutamate) where cells remove the NH2, forming ammonia Liver converts NH3 to urea Kidneys filter urea, ammonia, and creatinine
Unnecessary amino acids undergo deamination:
dietary protein intake and chronic disease
Urea levels in both blood and urine are used as markers of:
vitamin B-12 supplement
Vegan pregnant women should consult healthcare provider about the need of a:
creatinine
a nitrogen- containing waste produced by muscles
urea
a waste product of amino acid metabolism
conditionally essential amino acid
amino acids that are normally nonessential but became essential under a certain condition
essential amino acids
amino acids the body cannot make or cannot make enough of to meet its needs
protein turnover
cellular process of breaking down proteins and recycling their amino acids
mutation
change in the normal DNA sequence of a gene
complementary combinations
combining certain plant foods to provide all essential amino acids
high quality proteins
complete proteins that are well-digested, absorbed, and used by the body
nutrigenomics and nutrigenetics
components of nutritional genomics:
amines
compounds that include amino groups in their chemical structure
inborn errors of metabolism
conditions that occur when genes undergo mutations that disrupt metabolism of specific nutrients
peptides
contain two or more amino acids
vegan diet
diet based solely on plant foods, with complete elimination of animal foods and products
personalized nutrition
dietary recommendations based on individual response to food and nutrients
Creatine Melanin Regulatory amines such as serotonin, epinephrine, histamine
examples of amines:
complete protein
food source of protein that contains an adequate proportion of each of the nine essential amino acids
incomplete protein
food source of protein that contains inadequate amounts of one or more of the essential amino acids
marasmus
form of undernutrition that results from starvation; diet lacks energy and nutrients
Kwashiorkor
form of undernutrition that results from consuming adequate energy and insufficient high-quality protein
marasmic kwashiorkor
form of undernutrition that results in a child with kwashiorkor who then starts to not consume enough energy; characterized by edema and wasting
dipeptide
forms when two amino acids bond, and a water molecule is released
20
how many different amino acids are found in the proteins of the human body?
undernutrition
inadequate consumption of nutritious food
low quality proteins
incomplete and generally less digestible, making their amino acids less bioavailable than high-quality proteins
proteins
large, complex organic molecules made up of amino acids
protein-energy malnutrition (PEM)
malnutrition that occurs when the diet lacks sufficient protein and energy
blood urea nitrogen (BUN)
measure of the concentration of urea in blood
urine urea nitrogen (UUN)
measure of the concentration of urea in urine
dipeptides
molecules that consist of two amino acids
complete proteins exceptions are quinoa and soy protein
most plant foods are not sources of:
During starvation, serious illness, and as a result of severe injury Recovery from the illness or injury involves replacing the protein that was lost (refeeding), resulting in positive nitrogen balance until nitrogen equilibrium is restored
negative nitrogen balance:
Exogenous
outside the body (dietary or other external source)
vegetarian diet
plant-based eating pattern that may or may not include some animal foods
legumes
plants that produce pods with a single row of seeds
gene
portion of DNA that codes for a protein
During periods of rapid growth, such as pregnancy, infancy, and puberty When people are recovering from illness or injury When performing weight (resistance) training
positive nitrogen balance:
High: Vitamins C , vitamin E, and folate Phytonutrients Fiber Magnesium and potassium Low: Saturated fatty acids
possible advantages for plant based diets:
Low: Vitamin B-12, vitamin D, and riboflavin Zinc, iron, and calcium Omega-3 fatty acids Certain essential amino acids Energy
possible disadvantages for plant based diets:
stomach
protein digestion begins in the:
polypeptides
proteins comprised of 50 or more amino acids
carbon, hydrogen, oxygen, and nitrogen
proteins contain:
high protein diet
provides an amount of protein greater than the RDA, usually 20 to 35% of calories
deamination
removal of the nitrogen-containing group from an amino acid
negative nitrogen balance
state in which the body loses more nitrogen than it retains
positive nitrogen balance
state in which the body retains more nitrogen than it loses
hydrochloric acid (Hal)
denatures food proteins and converts inactive pepsinogen to active pepsin
To build new cells and many functional components of cells As a component of hardened structures, such as hair and nails As enzymes to speed chemical reactions As lubricants to ease movement In clotting compounds in blood To build antibodies that fight disease organisms As compounds that help maintain fluid and pH balance As transporters To make certain hormones As an energy source (as a last resort, only under certain conditions)
functions of proteins:
nonessential amino acids
group of amino acids that the body can make
nutrigenetics
study of how inherited genetic variations influence the body's responses to specific nutrients and nutrient combinations
nutrigenomics
study of how nutrients affect the expression of a person's genome
nutritional genomics
study of nutrigenomics and nutrigenetics
primary structure
the basic structure of protein; a linear chain of amino acids linked by peptide bonds
limiting amino acid
the essential amino acid found in the lowest concentration in an incomplete protein
wasting
the loss of organ and muscle proteins as the body breaks down these tissues to obtain amino acids for energy metabolism
amino or nitrogen-containing group
the portion of an amino acid that contains nitrogen
carbon skeleton
the remains of an amino acid following removal of the nitrogen-containing component (amino group) of the amino acid
quaternary structure
the structure of protein that is comprised of two or more polypeptide chains arranged together in a complex matter
transamination
transfer of the nitrogen-containing group from an unneeded amino acid to a carbon skeleton to form an amino acid
Walnuts Cashews Almonds
tree nuts include:
urinary elimination of urea and creatinine
what accounts for most the lost nitrogen:
10-35%
what is the AMDR percentage of energy from protein?