Human Nutrition - Chapter Seven
Chemical structure of a protein
a carbon atom that anchors a hydrogen atom and three different groups of atoms: the amino or nitrogen containing group, the R group, and the carboxylic acid group
albumin
a protein in blood that helps to maintain the proper distribution of fluids in the blood and body tissues
edema
accumulatio of fluid in tissues - can happen during starvation when the level of protein in the blood decreases and some water then leaks out of the bloodstream
celiac disease
autoimmune disorder in which a person's immune system reacts to gluten resulting in damage to intestine and poor absorption
nitrogen balance
balancing nitrogen intake and protein turnover with losses
blood urea nitrogen
blood test used to assess kidney function; elevated level occurs when kidneys cannot filter urea from the blood properly
Functions of proteins
build new cells and many functional components of cells, component of hardened structures such as hair and nails, as enzymes, lubricants, clotting components, antibodies, compounds that help maintain fluid and pH balance, transporters, hormones, energy source as a last resort
carboxylic acid group
carboxylic acid portion of a compound
Phenylketonuria
cells are unable to produce active phenylalanine hydroxylase enzyme so phenylalanine and its toxic by products build up in tissues and damage cells
inborn error of metabolism
change in the normal DNA sequence of a gene
secondary structure
coiling of the polypeptide chain due to chemical attractions between certain components of the amino acids
amino
portion of an amino acid that contains nitrogen
food provocation test
prior, the patient eliminates the food from their diet for 3 weeks, then the provoking food is given and symptoms are noted
How do proteins act as a buffer?
protein molecules bind to H+ or to OH-
susceptibility to food allergies is influenced by
timing and does of initial allergen exposure, gut microbial dysbiosis, vitamin D status, omega 3 fatty acid intake, and antiacid use
food allergies effect ___% of the population
10
How much protein in a typical adult?
10-35% of energy from protein; 0.8 g/kg body weight
nonessential amino acids
11 of the 20 amino acids that a healthy human body can make
The human body contains about ____ of its amino acid supply from endogenous sources and the remainder from exogenous (dietary) sources
2/3
the human body contains proteins made from __ different amino acids
20
high protein diet
20-35% of total calories
in general, most plant foods provide less than ___ of protein per ounce
3g
essential amino acids
9 of the 20 amino acids that must be supplied by foods because the body cannot synthesize them or make enought to meet its needs
high quality proteins
complete proteins that are well digested, absorbed, and used by the body
proteins
complex organic molecules that contain carbon, hydrogen, and oxygen atoms like lipids and carbohydrates. They also contain nitrogen
common reasons for elevated Blood urea nitrogen
congestive heart failure, high protein intake, GI bleeding, heart attack, kidney disease, shock
peptide bond
connection between two amino acids; between the acid group of one amino acid and the amino group of another that release a water molecule when bonded
polypeptides
contain two or more amino acids
complete protein
contains all essential amino acids in the proper proportions that promote the deposition of protein in muscles and other tissues; primarily animal foods
incomplete protein
contains inadequate amounts of one or more of the essential amino acids
amino acid derivates
creatine, melanin, and regulatory amines - serotonin, epinephrine, and histamine
Effects of protein energy deficiency in children
do not grow well, weak, irritable, dehydration, infections, stunted growth, lower integlligence
protein complementation
eating combinations of certain plant food protein sources that together contain a proportion of amino acids similar to complete proteins from animal sources
marasmic kwashiorkor
edema and wasting
non celiac gluten sensitivity
emerging disorder - an intolerance to gluten containing foods in the absence of celiac disease or wheat allergy - causes IBS like symptoms
limiting amino acids
essential amino acids that are in relatively low amounts
tertiary structure
final three dimensional form of the protein
sickle cell anemia
genetic condition characterized by abnormal red blood cells - wrong amino acid is added to two of the polypeptide chains in hemoglobin; impairs hemoglobin's oxygen carrying ability
Where does protein digestion start?
in the stomach when HCl denatures proteins and converts inactive pepsinogen to pepsin
FODMAP intolerance
inability to digest the long chains of fructose
undernutrition
inadequate consumption of nutritious food
low quality proteins
incomplete and generally less digestible making their amino acids are less bioavailable
Where does the body get the info to make proteins
information coded in DNA
a food can be labeled as gluten free if
it contains less than 20 ppm
Risks with high protein diets
kidney damage in susceptible individuals, higher risk for CVD due to increase saturated fat diet, red meat and colon cancer are linked, osteoporosis
primary structure
linear chain of amino acids linked by peptide bonds
common reasons for low BUN
liver failure, inadequate protein, malnutrition, overhydration
negative nitrogen balance
loses more nitrogen than it retains; occurs during starvation, illness, and severe injury
protein energy malnutrition
malnutrition that occurs when the diet lacks sufficient protein and energy - children are susceptible
urine urea nitrogen
marker of protein intake
top food allergens in US
milk, eggs, fish, crustacean shelfish, tree nuts, peanuts, wheat, soybeans
antibodies
molecules that tag invading organisms for destruction by the immune system
transamination
nitrogen containing group is transferred to another substance to make a nonessential amino acid
creatinine
nitrogen containing waste produced by muscles
kwashiorkor
occurs where mothers breastfeed infants until they give birth to another child who is abruptly weaned to make way for the younger sibling - have stunted growth, unnaturally blond hair, swollen cheeks, arms, legs, and bellies
R group
part of an amino acid that determines its physical and chemical properties
after short peptides and amino acids enter absorptive cells,
peptides are broken down into amino acids and then travel to the liver via the hepatic portal vein; the liver keeps some amino acids and releases the rest into general circulation
amino acids
proteins are composed of smaller chemical units called amino acids
sources of complete proteins from plants
quinoa and soy
health advantages of high protein diet
reduce caloric intake, help retain lean muscle during weight loss, keep people full even when eating limited calories, enhance blood sugar regulation, improve blood lipid levels, and reduce blood pressure
carbon skeleton
remains of an amino acid following the removal of the amino group
deamination
removing the nitrogen containing group from an unneeded amino acid to make a carbon skeleton
positive nitrogen balance
retains more nitrogen than it loses as proteins are being added to tissues; pregnancy, infancy, and puberty, recovery from illness or injury, insulin, growth hormone, testosterone, weight training
What plant parts contain most protein?
seeds, tree nuts, legumes, and pods
conditionally essential
several nonessential amino acids that can become essential under certain conditions
marasmus
severe PEM; starvation - weakness and loss of body tissue mass
the shape of a protein is important because
structure determines function in the body
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
protein turnover
the process of breaking down old or unneeded proteins into their component amino acids and recycling them to make new proteins, occurs continuously within cells
protein splitting enzymes that come from the pancreas into the small intestine
trypsin and chymotrypsin
quaternary structure
two or more polypeptide chains associating with each other to form large complexes
What happens if a person consumes more protein than they need?
undergo deamination and some of the excess NH2 goes to the liver as glutamate which is converted to ammonia which is converted to urea and exits the body as urine
denaturation
unfolding of protein - happens when protein is cooked
food intolerances
unpleasant physical reactions after consumin nonprotein foods