Vnhs Biology Ch 5

Front 1

the four main classes of biological molecules

Back 1

lipids, fats, carbs, and proteins

Front 2

macromolecule

Back 2

molecules that have thousands of covalently bonded atoms to them with a mass of over 100,000 daltons

Front 3

polymer

Back 3

a long molecule consisting of many similar or identical building blocks linked by covalent bonds

Front 4

monomers

Back 4

the repeating units that serve as the building blocks of a polymer that are small molecules

Front 5

How are monomers linked to each other?

Back 5

condensation reaction

Front 6

condensation reaction

Back 6

two molecules are covalently bonded to each other through the loss of a water molecule

Front 7

What is the more specific name for a condensation reaction?

Back 7

dehydration reaction

Front 8

How do the monomers connect to each other?

Back 8

One donates the hydroxyl group (-OH) while the other donates the hydrogen(H)

Front 9

hydrolysis

Back 9

water is added to break the bonds of the monomers and to break the polymer

Front 10

What attributes to the differences in siblings?

Back 10

the different polymers

Front 11

carbohydrates

Back 11

the class that has sugars and the polymers of sugars

Front 12

Monosaccharides

Back 12

single sugar

Front 13

Monosaccharides are often made up of multiples of the unit ____.

Back 13

CH2O

Front 14

What is a common monosaccharide?

Back 14

Glucose(C6H12O6)

Front 15

What are some of the trademarks of sugars?

Back 15

a carbonyl group ( ), multiple hydroxyl groups (-OH), depending on the location of the carbonyl group the sugar is either an aldose or a ketose

Front 16

List the different carbon skeletons in the sugars.

Back 16

Triose, Pentose, and Hexose

Front 17

disaccharide

Back 17

two monosaccharides joined together by a glycosidic linkage

Front 18

glycosidic linkage

Back 18

a convalent bond formed between two monosaccharides by a dehydration reaction

Front 19

maltose

Back 19

disaccharide formed by the linking of two molecules of glucose

Front 20

sucrose

Back 20

table sugar, two monomers are fructose and glucose

Front 21

Lactose

Back 21

glucose is joined with galactose

Front 22

Polysaccharides

Back 22

macromolecules, polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages

Front 23

Starch

Back 23

a storage polysaccharide of plants, is a polymer consisting entirely of glucose monomers

Front 24

Simplest form of starch

Back 24

amblyose,is an unbranched polymer

Front 25

How do plants store starches?

Back 25

in granules withing cell structures called plastids

Front 26

glycogen

Back 26

a polymer of glucose that animals store

Front 27

What would hydrolysis of glycogen produce?

Back 27

glucose for the animal to use

Front 28

cellulose

Back 28

structural polysaccharide that is a major component of the tough walls that enclose plant cells

Front 29

What is the most abundant organic compound on Earth?

Back 29

cellulose

Front 30

insoluble fiber refers to ______.

Back 30

cellulose

Front 31

How many ring forms are there for glucose?

Back 31

two, alpha and beta

Front 32

chitin

Back 32

the carbohydrate used by arthopods to build their exoskeletons

Front 33

lipids

Back 33

do not consist of polymers, they have little or no affinity for water

Front 34

What do lipids mainly consist of?

Back 34

hydrocarbons

Front 35

fat

Back 35

constructed from two two kinds of smaller molecules: gycerol and fatty acids

Front 36

glycerol

Back 36

alcohol with three carbons, each bearing a hydroxyl group

Front 37

fatty acid

Back 37

has a long carbon skeleton, usually 16 to 18 carbon atoms in length. At one end of the fatty acids is a carboxyl group which is attached to a long hydrocarbon chain

Front 38

triacylglycerol or triglyceride

Back 38

three fatty acids joined together

Front 39

saturated fatty acid

Back 39

there are no double bonds so there are as many hydrogens as possible

Front 40

unsaturated fatty acid

Back 40

has one or more double bonds formed by the removal of hydrogen bonds from the carbon skeleton, they will have a kink in its hydrocarbon chain

Front 41

saturated fat

Back 41

a fat made from saturated fatty acids

Front 42

unsaturated fat

Back 42

a fat made from unsaturated fatty acids

Front 43

room temperature solid fat

Back 43

saturated, as there are no kinks so they stack nicely on top of each other

Front 44

room temperature liquid fat

Back 44

unsaturated as they don't stack nicely because they have kinks in the cis side

Front 45

hydrogenated

Back 45

unsaturated fat artificially synthesized with hydrogens

Front 46

fat that causes cardiovascular diseases and why?

Back 46

saturated fats, deposits called plaques develop within the walls of blood vessels which impede the blood flow

Front 47

hydrogenation produces both saturated and unsaturated fats called _____ fats.

Back 47

trans fat, which have trans double bond

Front 48

major function of fat

Back 48

energy storage

Front 49

phospholipid

Back 49

two fatty acids attached to glycerol, the thrid hydroxyl group is joined to a phosphate group which has a negative electrical charge

Front 50

cause of phospholipid ambivalent behavior toward water

Back 50

hydrocarbon tails are hydrophobic, bur phosphate group that is attached to the tail has affinity to water

Front 51

How do phospholipids arrange themselves?

Back 51

in bilayers, with heads facing outwards and tails inward

Front 52

steroids

Back 52

lipids characterized by a carbon skeleton consisting of four fused rings

Front 53

cholesterol

Back 53

common component of animal cell membranes and is also the precursor from which other steroids are synthesized

Front 54

Protein

Back 54

speed up chemical reactions, while others play a role in structural support, storage, transportation, cellular communications, mvmt, and defense against foreign substances

Front 55

enzymes

Back 55

regulate metabolism by acting as catalysts

Front 56

catalysts

Back 56

chemical agents that selectively speed up chemical reactions in the cell without being consumed by the reaction

Front 57

Can enzymes be reused?

Back 57

yes

Front 58

polypeptides

Back 58

polymers of amino acids

Front 59

how many different amino acids are there?

Back 59

20

Front 60

protein

Back 60

consists of one or more polypeptides folded and coiled into specific conformations

Front 61

amino acid

Back 61

organic molecules possessing both carboxyl and amino groups

Front 62

components of an amino acid

Back 62

an alpha carbon, hydrogen atom, carboxyl group, and an R group which is a side chain that differs with each amino acid

Front 63

basic amino acids

Back 63

side chains are usually positive in charge

Front 64

acidic amino acids

Back 64

side chains are usually negative in charge

Front 65

peptide bond

Back 65

the covalent bond amino acids form through a dehydration reaction to form polymers

Front 66

primary structure

Back 66

unique sequence of amino acids

Front 67

secondary structure

Back 67

polypeptide chains repeatedly folded or coiled

Front 68

alpha helix

Back 68

delicate coil held together by hydrogen bonding between every fourth amino acid

Front 69

beta pleated sheet

Back 69

two or more regions of polypeptide chains that are lying next to each other are connected by hydrogen bonds between parts of the two parallel polypeptide backbones

Front 70

tertiary structure

Back 70

a shape resulting from the polypeptide chains and the R side chains

Front 71

hydrophobic interactions

Back 71

as the polypeptide folds into its conformation, the amino acids with hydrophobic side chains usually end up clustered at the core of the protein

Front 72

disulfide bridges

Back 72

form where 2 cysteine monomers, amino acids with sulfhydryl groups on their side chains, are brought together by the folding of the protein

Front 73

quaternary structure

Back 73

aggregation of polypeptide subunits

Front 74

sickle-cell Anemia

Back 74

caused by a single substitution with Valine replacing Glutamic acid, causes sickle shaped cells

Front 75

denaturation

Back 75

protein may unravel and lose its conformation when the environment of its location is not right

Front 76

chaperonins

Back 76

protein molecules that assist the proper folding of other proteins

Front 77

X-Ray Crystallography

Back 77

a method used to determine a protein's 3-D structure

Front 78

two types of nucleic acid

Back 78

DNA and RNA

Front 79

DNA

Back 79

provides directions for its own replication, and RNA replication

Front 80

RNA

Back 80

controls protein synthesis

Front 81

polynucleotides

Back 81

nucleic acids are macromolecules that exist as polymers

Front 82

nucleotides

Back 82

each polynucleotide consists of monomers

Front 83

components of a nucleotide

Back 83

nitrogenous base, a pentose, and a phosphate

Front 84

the nucleotide without the phosphate group

Back 84

nucleoside

Front 85

Pyrimidines

Back 85

a six-membered ring of carbon and nitrogen atoms, cytosine, thymine and uracil

Front 86

Purines

Back 86

larger, six-membered rings of carbon paired with five-membered ring, adenine and guanine

Front 87

ribose

Back 87

a pentose connected to a nitrogenous base, nucleotides of RNA

Front 88

deoxyribose

Back 88

in DNA

Front 89

difference between ribose and deoxyribose

Back 89

deoxyribose lacks an oxygen atom on the second carbon in the ring

Front 90

double helix

Back 90

cellular DNA molecules have two polynucleotides that spiral around an imaginary axis

Front 91

antiparallel

Back 91

the sugar-phosphate backbones run opposite directions to each other