Nutrition 11 Ch. 6

Front 1

Large, complex molecules made up of amino acids and found as essential components of all living cells.

Back 1

proteins

Front 2

Nitrogen-containing molecules that combine to form proteins.

Back 2

amino acids

Front 3

Amino acids not produced by the body that must be obtained from food.

Back 3

essential amino acids

Front 4

Amino acids that can be manufactured by the body in sufficient quantities and therefore do not need to be consumed regularly.

Back 4

non-essential amino acids

Front 5

The process of transferring the amine group from one amino acid to another in order to manufacture a new amino acid.

Back 5

transamination

Front 6

Unique types of chemical bonds in which the amine group of one amino acid binds to the acid group of another in order to manufacture dipeptides and all larger peptide molecules.

Back 6

peptide bonds

Front 7

The process of using a gene to make a protein.

Back 7

gene expression

Front 8

The process through which messenger RNA copies genetic information from DNA in the nucleus

Back 8

transcription

Front 9

The process that occurs when the genetic information carried by messenger RNA is used to synthesize a chain of amino acids by a ribosome.

Back 9

translation

Front 10

The process by which proteins uncoil and lose their shape and function when they are exposed to heat, acids, bases, heavy metals, alcohol, and other damaging substances.

Back 10

denaturation

Front 11

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

Back 11

limiting amino acid

Front 12

Foods that do not contain all of the essential amino acids in sufficient amounts to support growth and health.

Back 12

incomplete proteins

Front 13

Foods that contain all nine essential amino acids.

Back 13

complete proteins

Front 14

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

Back 14

mutual supplementation

Front 15

Two or more foods that together contain all nine essential amino acids necessary for a complete protein.

Back 15

complementary proteins.
(It is not necessary to eat complementary proteins at the same meal.)

Front 16

Legumes are limited in these amino acids:

Back 16

methionine & cysteine

Front 17

Grains are limited in these amino acids:

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lysine

Front 18

Vegetables are limited in these amino acids:

Back 18

methionine, cysteine, & lysine

Front 19

Nuts & seeds are limited in these amino acids:

Back 19

isoleucine & lysine

Front 20

Stands for percentage of hydrogen. It is a measure of the acidity-or level of hydrogen-of any solution, including human blood.

Back 20

pH

Front 21

A disorder in which fluids build up in the tissue spaces of the body, causing fluid imbalances and a swollen appearance.

Back 21

edema

Front 22

Protein molecules that help transport substances throughout the body and across cell membranes

Back 22

transport proteins

Front 23

A disorder in which the blood becomes acidic; that is, the level of hydrogen in the blood is excessive. It can be caused by respiratory or metabolic problems.

Back 23

acidosis

Front 24

A disorder in which the blood becomes basic; that is, the level of hydrogen in the blood is deficient. It can be caused by respiratory or metabolic problems.

Back 24

alkalosis

Front 25

Proteins that help maintain proper acid-base balance by attaching to, or releasing hydrogen ions as conditions change in the body.

Back 25

buffers

Front 26

Defensive proteins of the immune system. Their production is prompted by the presence of bacteria, viruses, toxins, allergens, etc.

Back 26

antibodies

Front 27

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

Back 27

deamination

Front 28

An enzyme in the stomach that begins the breakdown of proteins into shorter polypeptide chains and single amino acids.

Back 28

pepsin

Front 29

Enzymes that continue the breakdown of polypeptides in the small intestine.

Back 29

proteases

Front 30

The practice of restricting the diet to food substances of plant origin, including vegetables, fruits, grains, and nuts.

Back 30

vegetarianism

Front 31

cancer causing agents, such as certain pesticides, industrial chemicals, and pollutants.

Back 31

carcinogens

Front 32

A disorder caused by inadequate consumption of proteins. It is characterized by severe wasting.

Back 32

protein-energy malnutrition

Front 33

A form of protein-energy malnutrition that results from grossly inadequate intakes of protein, energy, and other nutrients.

Back 33

marasmus

Front 34

A form of protein-energy malnutrition that is typically seen in developing countries in infants and toddlers who are weaned early because of the birth of a subsequent child. Denied breast milk, they are fed a cereal diet that provides adequeate energy but inadequate protein.

Back 34

kwashiokor

Front 35

What is a side group or side chain?

Back 35

the side chain is the portion that varies from one amino acid to the next.

Front 36

what are the 9 essential amino acids?

Back 36

P- Phenylalanine
V- Valine
T.- Threonine
T- Tryptophan
I- Isoleucine
M- Methionine
H- Histidine
A- Arginine
L- Leucine
L- Lysine

Front 37

What is a peptide bond?

Back 37

when two amino acids join together; the amine group of one binds to the acid group of another. (NH2 + COOH)

Front 38

2 amino acids form a:
3 amino acids form a:
A string of 4-9 amino acids amino acids form a:
10 or more amino acids form a:

Back 38

-dipeptide
-tripeptide
-oligopeptide
-polypeptide

Front 39

what are the four levels of protein structure:

Back 39

-primary structure
-secondary structure
-tertiary structure
-quaternary structure

Front 40

which structure determines the proteins function in the body?

Back 40

the tertiary structure

Front 41

how is protein quality measured?

Back 41

The quantity of essential amino acids in a protein determines its quality: proteins that contain higher quantities of essential amino acids are considered high-quality.

Front 42

describe how the body uses protein for energy?
Can protein be stored?

Back 42

To use proteins for energy, the liver removes the amine group from the amino acids (deamination). Nitrogen binds with hydrogen creating ammonia, which is quickly converted to urea. Urea is then transported to the kidneys, where it is excreted as urine. The remainder of the amino acid (carbon, hydrogen, oxygen), is used to make glucose (gluconeogenesis)

Protein cannot be stored in the body like fats and carbs can.

Front 43

protein quality is also measured by:

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digestibility:

Front 44

name the digestibility % of these: protein sources:
-animal & soy:
-legumes:
-grains & vegetables:

Back 44

-animal & soy: 90%
-legumes: 70-80%
-grains & vegetables: 60-90%

Front 45

what is the RDA for protein?
Are athlete's protein needs higher?
RDA for athletes?

Back 45

0.8g of protein/Kg of body weight

athlete's protein needs are higher.
RDA for athletes = 1.2- 1.8g of protein/Kg of body weight

Front 46

Nutrients of concern in a vegan diet are:

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-vit. B12
-vit. B2 (Riboflavin)
-Zinc
-vit. D
-Iron
-Calcium

Front 47

semivegetarian (partial vegetarian or flexitarian)

Back 47

excludes or limits red meat; may also avoid other meats

Front 48

Pescovegetarian

Back 48

Fish is the only animal source of protein in this diet

Front 49

lacto-ovo vegetarian

Back 49

only eats dairy and eggs for protein

Front 50

lacto-vegetarian

Back 50

only eats milk and cheese for protein

Front 51

Ovovegetarian

Back 51

only eats eggs for protein

Front 52

Vegan

Back 52

only plant based foods for protein

Front 53

Macrobiotic diet

Back 53

vegan type diet; becomes progressively more strict

Front 54

Fruitarian

Back 54

only fruit, seeds, nuts, honey and vegetable oil.

Front 55

excessive dietary protein can lead to these three conditions:

Back 55

heart disease, bone loss, and kidney disease

Front 56

marasmus =

Back 56

STARVING TO DEATH!

Front 57

what is the differences between marasmus and kwashiorkor?

Back 57

marasmus is starvation, it is slow and prolonged. kwashiorkor is not starvation but a protein deficiency with a sudden onset after child is weened suddenly.