• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/100

Click to flip

Use LEFT and RIGHT arrow keys to navigate between flashcards;

Use UP and DOWN arrow keys to flip the card;

H to show hint;

A reads text to speech;

100 Cards in this Set

  • Front
  • Back

large complex molecules found in cells of all living things


- muscle mass, bones, skin, blood


- metabolism,immunity, gluid balance, nutrient transport, can provide energy

proteins

human body is able to syntethsize

proteins



difference betweeen carbs, lipids, and proteins

= they are made according to instructions provided by dna


= proteins contain nitrogen that our bodies can readily use

proteins made from

amino acids


- central caroon with 4 groups, amine group, acid group, atm, side chain

amine means

nitrogen containing

bodies syntehsize estimated

10k to 50k unique proteins

20

amino acids in our bodies


- 9 are essential

esential amino acid

bodies cannot produce at all or in sufficient amount to meet our physiologic needs


- must obtain from food


- wo this we lose ability to make proteins and nitrogen compounds

we make nonessential amino acids by

transferring amine group from other amino acid to different acid group and side chain


= called transamination



acid groups and side chains can be

- can be donated or brokedown from carbs and fats

conditionally essential amino acid

- nonessential to essential


- arginine, cysteine, glutamine

essential amino acids

histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, valine

unique chemical bond where amine group of one amino acid binds to acid group of another in order to manufacture dipeptides and all larger pdptide moelcules


- water molecule is released


- amine + acid of two amino acids

peptide bonds

oligopeptide

4-9 amino acids

10 or more

polypeptide

process by which cells use genes to make proteins

gene expression

proteins actually manufacture at site of

ribosomes in the cells cytoplasm

molecule to copy/transcribe infor fromdna and carry it to ribosomes

messenger rna


- during transcription mrna copies dna and brings to ribosomes in cytoplasm and translation occurs DNA TO AMINO ACIDS


- at ribosome mrna binds with rrna and genetic infor distributed to trna


- trna roams cytoplasm for amino acid

beta cells

pancrease express insulin

skin cells live form

30 days

amino acids from food and breakdown fo cells creates

amino acid pool

levels of protein structure

1. primary


2. secondary


3. tertiary


4. quarternary

primary structure

sequential order of amino acids

secondary structure

twisting or folding of amino acid chain

tertiary structure

folding in 3d


- bonds between h atoms and s atoms maintin shapeand function

quartanary structure

2 or more polypeptides interact forming larger protein


- actin


- may be globular or fibrous

process by which proteins uncoil and lose their shape and function when they are exposed to heat,a cids, bases, heavy metals, alcohol

denaturation

essential amino acid that is missing or in smallest supply in the amino acid pool and is thus responsible for slowing or halting protein synthesis

limiting amino acid

protein or foods that does not contain all of essential amino acids in suficient quantities to support growth and health

incomplete protein

foods that do contai all 9 essential amino acids

complete proteins/ high quality

most complete protein sources

animals: egg whites, meat, oultry, fish, ilk


plant: soybeans, quinoa

process of combining two or more incomplete protein sources to make complete protein


- complementary foods are involved which have complementary proteins

mutual supplementation

2 or more foods that together contain all 9 essentail amino acids necessary for complete protein


- not necessary to eat complementary proteins at same meal

complementary proteins

consume complementary protein foods

same day bc partially not stored

rbc

live for 3/4 months

cells lining intestinal tract replaced

3/6 days

phosphofructokinase

- drive rate of break down glucose and use for energy during exercise


- wb we wouldnt be able to generate energy fast enough to be physically active

most hormones made from

amino acids

electrically charged atoms ions that assist in maintaing luid balance


- na and k

electrolytes

disorder in which fluids build up in the tissue spaces of the bodym causing fluid imbalances and a swollen appearance

edema

na k pump of transport proteins

na pumped outside and k inside

low protein intake

-nerve signals and contractions of muscles


- rythym of heart


- muscle weakness


- muscle spasms


- kidney failure

acids has

more hydrogen ion s tha pure water

acids and bases transported in blood and excreted through

kidneys and lungs

acidosis

when blood becomes too acidic, level of hydrogen in blood is excessive


- can be caused by respiratory or metabolic problems

alkalosis

blood becomes to alkalic


- level of hydrogen in blood is deficient


- can be caused by respiratory or metabolic problems

proteins that help maintain proper acid-base balance by attaching to or releasing hydrogen ions as condition change in the body

buffers

defenseive proteins of the immune system


- production is promoted by presence of bacteria, viruses, toxins, allergens

antibodies

proteins are good buffers bc

side chains have negative charges that can bind hydrogen ions when blood becomes acidic and neutralize

adequate protein necessary to support

increased production of antibdies that occurs in response to cold, flu or allergic reaction

to use proteins for energy

liver removes amine group from amino acid in deamination


- nitrogen bonds with hydrogen breating ammonia


- kidney converts ammonia to urea


-- amino acids can be converted to glucose bia gluconeogensis

eating too much protein results in

removal and excretion of nitrogen in urine

lipoproteins

- lipids bound to proteins


- allow transport of hydrophobic lipids

transferring

- iron in blood


- storage protein where iron is stored in liver

chemicals that transmit messages from one nerve cell to another


- epinephrine and norepinephrine

neurotransmitters

process by which an amine group is removed from an amino acid. nitrogen is then transported to kidneys for excretion in urine, while carbona nd other components are metabolized for energy or used to make other compounds

deamination

an enzyme in the stomach that begins the brekdown of proteins into shorter o=polpeptide chains and single amino acids

pepsin

when proteins reach stomach, hydrochloric acid denatues protein strands and converts pepsinogen into pepsin a protein digesting enzyme

ya

enzymes that continue breakdown of polypeptides int he small intestine

ya

quality of protein

- amount of essential amino acids


- diestibility

animal protein are highly digestive and soy

more than 90%

legumes digestibility

70-80% high

grains and vegetable proteins less digestible

60-90%

positive nitrogen balance

consume more than excreted


- states that body is retaining or adding protein


- occurs during periods of growth, pregnancy, or recovery form illness, or protein deficiency

healthy adults who are not pregnant are in

nitrogen balance

rda for sedentary people is

.8 g per kg body weight per day of protein

recommended percentage of energy from protein is

10-35%


- higher for children, adolescents, and pregnant/lactating women bc more proeing needed for gorwth, active, and vegetarians

negative nitrogen balance

results from starvation, low energy diet, illness, infection, serious burns, injuries

health risks with high protein intkes

1. heart disease - animal cholesterol


2. bone loss - blood acidic and pulls cacium to buffer


3. kidney disease - increase in protein consumption increases protein metabolisma nd urea production

good sources of protein include

meats, eggs, dairy, legumes, nuts, quorn, certain ancient grains like quinoa

of 4 % of americans that are vegetarians

25% are vegans

vegetarians should eat 2-3 servings of beans nuts seeds eggs or meat substitutes


- vitamin d , riboflavin b2, zinc and iron

vegetarians

protein energy malnutrition diseases

marasmus and kwashiorkor

form of protein energy malnutrition that rsults form grossly inadequate intake of enrgy and protein and nutrients


- characterizzed by extreme tissue wasting and stunted growth and development


- weakening of muscles, stunted brain development and learning impariment, depresed metabolism, little insulation, deterioration of intestinal lining, anemia, weak immune system

marasmus

form of protein energy malnutrition that is typically seen in infants and toddlers


- wasting, edema


- less severe than marasmus


- loss of appetite


- sores


- dry brittle hair

kwashiorkor

genetic disorder that causes red blood cells to be shaped like a sickle or rescent, impeding their transport to body tissues

sickle cell anemia

genetic disorder causes alteration in chloride transport, leading to production of thick, sticky mucus that causes life threatening repsiratory and digestive problems

cystic fibrosis

organic compounds that regulate a wide range of body processes


- can syntehsize small amounts of d and k


- we must consume all in our diet

vitamins

fat soluble vitamins

adek


- found in fatty portions of food

consuming nutrients in amounts that are ten or more times higher than recommended levels

megadosing

water soluble vitamins

c (ascorbic acid) and b vitamins (riboflaving, niacin, b6,b12,folate, pantothenic acid, biotin, thiamin)


- excreted in urine

cobalamin

b12

b6

include pyridoxal,pyridoxine, pyridoxamine

vitamin d

include cholecalciferol and ergocalciferol

vitamin k includes

phylloquinone and menanaquinone

bitamin a includes

retinol, retinal, retinoic acid

vitamine e includes

tocopherols, alpha tocopherol

naturally occuring inorganic substances


- calcium, iron, zinc


- solid


- crystalline substances that do not contain carbon


- do not break down during digestion or absorption


- assist in regulating body processes

minerals

- all elements


minerals that must be consumed in amounts of 100mg/day or more and that are present in body at level of 5g or more

majorminerals

minerals that must be consumed in amounts of less than 100mg/day and present in body less than 5g


- selenium, fluoride, iodine, chromium, manganese, iron, zinc, copper

trace minerals

micronutients digestibility

3-10%

dietary iron

heme iron - meats


non heme iron= plants and animal foods

alcoholics more susceptible to toxic effects of

vitmin a supplements

vitamin d has lowered disease risk for

colon cancer

vitamin e has lowered disease risk for

diabetes

vitamin k has lowered disease risk for

osteoporosis

calcium has lowered disease risk for

high blood pressure (hypertension)

chromium has lowered disease risk for

type 2 diabetes in older adults

magnesium has lowered disease risk for

muscle wasting (sacropenia) in older adults

selenium has lowered disease risk for

certain types of cancer