Nutrition 303 - Chapter 6

how many different amino acids are there?

20

proteins are made of strings of

amino acids

what groups make up an amino acid?

amino, acid, hydrogen, side

what is the amino group in an amino acid made of?

hydrogen and nitrogen

what part of the amino acid gives the aa its unique identity?

the side group

the three groups of amino acids

essential, nonessential, conditionally essential

amino acids are linked together by

peptide bonds

two amino acids are called a

dipeptide

three amino acids are called a

tripeptide

many amino acids linked together are called a

polypeptide

the reaction that occurs to join amino acids together, losing a water molecule is:

condensation

denaturation

the uncoiling of a protein

what can cause denaturation?

heat, pH, oxidation, agitation

the protein structure

a chain of amino acids linked by peptide bonds

the sequence of amino acids determines the protein's

shape

a protein's shape determines its

function

what is a peptide bond?

a bond between 2 amino acids formed when a carboxyl group (COOH-) of one amino acid joins an amino group (NH2) of another amine acid, releasing water in the process

complete protein

has all 20 amino acids present

incomplete protein

has some of the 20 amino acids missing

what part of the amino acid is measurable in the body/?

nitrogen

proteins are denatured in the stomach by

HCL

protein digestion in the stomach

pepsinogen and pepsin start to break polypeptides apart

pepsinogen

an inactive form of protein enzyme released in the presence of HCL

pepsin

an active form of an enzyme that cleaves the proteins into smaller polypeptides

protein digestion in the small intestine

enzymes from the pancreas and intestines (proteases and peptidases) complete digestion

protease

enzyme that hydrolyzes protein into short peptides called oligopeptides

oligopeptides

peptides made of 4-9 amino acids

peptidases

enzymes that split proteins into amino acids

what happens to the amino acids once peptidase breaks them down from proteins?

they can be absorbed into the bloodstream and brought to the liver

does the body handle broken down or whole proteins better?

whole

protein synthesis

mrna goes into a cell's nucleus, copies the dna, takes it out to a ribosome and waits for a trna to bring the correct assortment of amino acids to form the necessary protein

why does the sequence of amino acids matter?

sequence determines shape which then impacts function, so by changing the sequence you change the function

the 8 roles of protein

growth, enzymes, hormones, regulation of fluid balance, acid-base regulation, transport proteins, antibodies, source of energy and glucose

how do proteins regulate fluid balance?

plasma proteins attract water, they prevent edema

how do proteins regulate acid-base levels?

proteins act as buffers, accepting or donating H+ ions into the blood to keep blood at a certain pH

acidosis

proteins release H+

alkalosis

proteins accept H+

transport proteins act as ____ in cell membranes

pumps

protein turnover

proteins are constantly being broken down for use and regenerated

amino acid pool

the supply of aa available for protein synthesis

zero nitrogen balance

the amount of nitrogen consumed equals the amount excreted

positive nitrogen balance

the amount of nitrogen consumed is greater than the amount excreted

negative nitrogen balance

the amount of nitrogen consumed is less than the amount excreted

PEM stands for

protein energy malnutrition

PEm

inadequate calories and/or protein

two types of PEM

kwashiorkor, marasmus

kwashiorkor

severe dietary protein deficiency

marasmus

severe caloric deficiency

the health effects of too much protein

heart disease, osteoporosis, obesity, cancer

conditionally essential amino acids

nonessential amino acids that are made from essential amino acids; when the body doesn't get enough of the essential, it can't make the nonessential, making it conditionally essential

protein absorption

carriers transport amino acids into intestinal cells to be used for energy or to synthesize needed compounds before unused ones are transported to the the liver

high quality protein

dietary proteins containing all the essential amino acids in relatively the same amounts that human beings require

reference protein

a standard against which to measure the quality of other proteins

complementary proteins

two or more dietary proteins whose amino acid assortments complement each other in such a way that the essential amino acids missing from one are supplied by the other

signs of kwashiorkor

edema, muscle loss, skin rashes, hair changes, water and electrolyte imbalances

signs of marasmus

emaciation, lack of growth, loss of fat stores

what is the RDA for protein?

.8g/kg weight

what is the AMDR for protein?

10-35%