Nutrition 1020: Chapter 7

tertiary structure

refers to the three dimensional, twisted structure of a polypeptide that includes interactions between various amino acid groups on the chain

carbon skeleton

remains of an amino acid following deamination and removal of the nitrogen containing component of the amino acid

deamination

removal of the nitrogen containing group from an amino acid

what plants are exceptions to the fact that plant foods are not sources of high quality protein?

soy bean and quinoa

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

buffer

substances that can protect the pH of a solution

nutrigenetics

the study of how inherited genetic variations influence the body's responses to specific nutrients and nutrient combinations

nutrigenomics

the study of how nutrients affect the expression of a persons genome

what are the essential amino acids?

threonine, tryptophan, histidine, isoleucine, leucine, lysine, methionine, valine, phenylalanine ( TT HILL MVP)

transamination

transfer of the nitrogen containing group form an unneeded amino acids to a carbon skeleton to form an amino acid

amino acid absorption

transported to aborptive cells and into capillary of the villus

gluten

type of protein found in many grains; provides texture and shape to baked products

gluten sensitivity

uncomfortable symptoms following consumption of gluten, but the individual does not have damage to small intestine

food intolerances

unpleasant physical reactions including headaches and intestinal discomfort following consumption of certain foods

limiting amino acids

essential amino acid found in the lowest concentration in a protein source

kwashiorkor

form of under nutrition that results from consuming adequate energy and insufficient high-quality protein

marasmus

form of undernutrition that results from starvation; diet lacks energy and nutrients

phenylketonuria

genetic metabolic disorder characterized by the inability to convert the amino acids phenylalanine to tyrosine, resulting in accumulation of phenylalanine

nonessential amino acids

group of amino acids the body can make

amino acids

nitrogen containing chemicals that comprise proteins

creatine

nitrogen-containg waste product by muscles

what is a way to remember amino acids that are not essential?

no essential amino acids start with A or G

lactovegetarian

obtains animal protein from milk and milk products (no eggs)

protein-energy malnutrition

occurs when the diet lacks sufficient protein and energy

R group (side chain)

part of an amino acid that determines the molecules physical and chemical properties

legumes

plants that produce pods with a single row of seeds

gene

portion of DNA

amino or nitrogen containing group

portion of an amino acid that contains nitrogen

chymotrypsin

protein splitting enzyme secreted from pancreas

high quality (complete) protein

protein that contains all essential amino acids in amounts that support the deposition of protein in tissues and the growth of a young person

trypsin

protein-splitting enzyme secreted form pancreas

polypeptides

proteins composed of 50 or more amino acids

low quality (incomplete) protein

proteins that lack or has inadequate amounts of one or more of the essential amino acids

primary structure

refers to the basic structure of a protein; a linear chain of amino acids linked by peptide bonds

secondary structure

refers to the coiling of a polypeptide chain

quaternary structure

refers to the structure of protein that is comprised of two or more polypeptide chains arranged together in a unique manner

semivegetarian

usually avoid red meat but consumes other animal foods

urea

waste product of amino acid metabolism

RDA for protein

0.8g/kg body weight

describe protein synthesis

1) information on DNA transcribed onto mRNA so that a ribosome can attach to the mRNA and "read the instructions" 2) ribosome reads the mRNA 3 at a time and a tRNA attaches the requested amino acids; this goes until the protein is completed

protein AMDR

10 to 35%

how many essential amino acids are there?

9

what are the major functions of proteins

build new cells, hair/nail growth, enzymes, maintain fluid and pH, transporters, energy

edema

accumulation of fluids in tissues; "swelling"

what type of protein helps maintain the proper distribution of fluids in the blood and body tissue

albumin

denaturation

altering a protein's natural shape and function by exposing it to conditions such as heat, acids, and physical agitation

conditionally essential amino acids

amino acids that are normally nonessential but become essential under certain conditions

essential amino acids

amino acids the body cannot make or cannot make enough of to meets its needs

nitrogen balance (equilibrium)

balancing nitrogen intake with nitrogen losses

protein digestion

begin in stomach with HCl and pepsin; in pancreas trypsin, chymotrypsin break polypeptide into shorter components; these are then broken into dipeptides and tripeptides; microvilli break these into amino acids

what issues come with too much protein in ones diet?

cancer, high calcium losses, dehydration

carboxylic acid group

carboxylic acid portion of a compound

peptide bind

chemical attraction that connects 2 amino acids together

tripeptides

compounds that consist of 3 amino acids

dipeptides

compounds that consist of two amino acids

lactoovovegatarian

consumes milk and eggs

peptide

contain two or more amino acids

what are the two key factors in determining the quality of protein?

digestibility and amino acid composition

ovovegetarian

eats eggs but not milk

what is the reference protein most commonly?

egg white protein (albumin)

the amino acid pool is ___________ and ________________

endogenous; exogenous

DNA

hereditary material that provides info for making proteins

caesin

high quality protein found in milk

food allergy

inflammatory response that results when the boys immune system reacts inappropriately to one or more harmless substances in food

celiac disease

inherited condition in which the protein gluten cannot be absorbed; results in damage to small intestine and poor absorption of nutrients

sickle cell anemia

inherited form of anemia

undernutrition

lack of food

proteins

large, complex organic molecules made up of amino acids

acid-base balance

maintaining the proper pH of body fluids

personalized nutrition

making dietary choices based on ones genetic makeup

protein digestibility correct amino acid score

measure of protein quality based on amino acid composition score and digestibility of a protein food

biological value

measure of protein quality based on how well and quickly the body converts food protein into body tissue protein

protein efficiency ratio

measure of protein quality based on the ability of a protein to support weight gain in a laboratory animal

blood urea nitrogen

measure of the concentration of urea in blood (used to access kidney function)

complementary combination

mixtures of certain plant foods that provide all essential amino acids without adding animal proteins