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o chem Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

dehydration

A

to make bonds you create water. two monomers are joined by removing one molecule of water

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2
Q

hydrolysis

A

to break bonds use water with enzymes. water is added to split large molecules

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3
Q

hydrocarbons

A

consist of carbon, hydrogen, and oxygen only

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4
Q

isomers

A

molecules that have the same molecular formula but differ in their arrangement of these atoms

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5
Q

functioning group

A

attached to carbon skeleton have diverse properties. the behavior of organic molecules is dependent on the identity of their functioning groups

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6
Q

polymers

A

long chain molecules made of repeating subunits called monomers

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7
Q

carbohydrates

A

refers to all types of sugars simple and complex

CHO in 1:2:1 ratio

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8
Q

monosaccharides

A

all CH2O (C6H12O6) isomers

hexoses: 6 sided - glucose and galactose
pentoses: 5 sided - deoxyribose, ribose, and fructose

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9
Q

disaccharides

A

C12H22O11 (ratio off from dehydration reaction)

sucrose, maltose, lactose

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10
Q

glucose + fructose

A

sucrose (cane sugar)

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11
Q

glucose + galactose

A

lactose (milk sugar)

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12
Q

glucose + glucose

A

maltose (malt sugar)

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13
Q

glycosidic bond

A

dehydration forms this bond between monosaccharides - O atom forms bridge between 2 C atoms

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14
Q

polysaccharides

A

comprised of hundreds of glucose molecules (C6H10O5)n

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15
Q

glycogen

A

energy storage polysaccharide found in animals, vertebrate muscle cells, and liver cells; branched

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16
Q

starch

A

energy storage polysaccharide found in plants; helical

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17
Q

chitin

A

structural support polysaccharide found in exoskeleton of arthropods like insects and crustaceans. (contains N but is primarily glucose, so it’s categorized as a carb)

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18
Q

cellulose

A

structural support polysaccharide in cell wall of plants

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19
Q

glycoproteins

A

short sugar chains (oligosaccharides) bound to one of more proteins - they are receptors

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20
Q

excess carbs

A

turn into glycogen, and if your glycogen stores are axed out then it turns into fat

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21
Q

nucleic acids

A

4 nitrogenous bases (adenine, thymine, cytosine, guanine, and uracil in RNA)
DNA, RNA, ATP

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22
Q

purines

A

2 rings - AG

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23
Q

pyrimidines

A

1 ring - CUT

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24
Q

ATP

A

molecule with stored energy between phosphate groups - nucleic acid

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25
Q

nucleotides

A

made up of nitrogenous base, pentose, phosphate group

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26
Q

bonds in nitrogenous bases

A

covalent between nucleotides and hydrogen between nitrogenous bases

27
Q

lipids

A

CHO only and O is only in small amounts. most are hydrophobic and won’t dissolve. fatty acids are the monomers. lipids aren’t polymers

28
Q

amphipathic

A

having both hydrophilic and hydrophobic ends - triglycerides and phospholipids

29
Q

fats

A

glycerol and fatty acids, solids at room temp, animals

30
Q

oils

A

liquid fat, plants

31
Q

lipids chemical composition

A

H:O is variable in fats, very small amounts of oxygen.

lipids are huge molecules and generally linear

32
Q

saturated fat

A

carbon backbone has no double bonds and is full of H

33
Q

unsaturated fat

A

some H atoms are missing and replaced by double bonds (easier to break down and therefore healthier)

34
Q

monounsaturated fat

A

1 double bond, healthier than saturated fat because a kink at the double bind prevents packing of molecules (easier to break down)

35
Q

polyunsaturated fat

A

fatty acid with many double bonds - the healthiest type of fat

36
Q

hydrogenated fats

A

unsaturated fats are purposefully saturated to produce solids - also creates trans fat

37
Q

glycerol

A

important for building lipids; glycerol is needed to make a triglyceride and a phospholipid (its the hydrophobic head of phospholipid)

38
Q

triglycerides

A

when lipids are in excess transported through blood stream for storage as a triglyceride - from food or can be made by the liver

39
Q

phospholipid

A

used to make the phospholipid bilayer of the cell membrane - 1 phosphate and 2 fatty acids

40
Q

steroids

A

identifiable by four rings.

cholesterol -> progesterone -> testosterone -> estrogen

41
Q

anabolic steroids

A

to build up - synthetic testosterone used to build up dz muscles, testosterone increases bone/muscle mass

42
Q

too much anabolic steroids

A

in males: violent mood swings, depression, liver damage, cancer, heart problems, shrink testicles, decreased sex drive, infertility, and breast enlargement
in females: masculine characteristics, disrupts menstruation, stunts bone growth

43
Q

proteins

A

polymers made up of amino acid monomers

44
Q

amino acid

A

contain central carbon bonded to a carboxyl group, an amino group, a hydrogen an R group

45
Q

categories of amino acids

A

nonpolar, hydrophobic; polar, hydrophilic; hydrophillic: acidic - negatively charged (R group has carboxyl); and basic - positively charged (R has amino)

46
Q

peptide bond

A

link amino acids, formed by dehydration synthesis

47
Q

polypeptide

A

short chain of amino acids

48
Q

functioning protein

A

1 or more proteins precisely twisted folded or coiled into unique 3D shape

49
Q

collagen

A

structural protein - tendons, ligaments, cartilage

50
Q

keratin

A

structural protein - wool, hair, nails, skin

51
Q

hemoglobin

A

transport protein

52
Q

immunoglobulin

A

defense protein

53
Q

globular proteins

A

glob or round

54
Q

fibrous

A

long thin or filamentous

55
Q

primary structure

A

the unique sequence of amino acids are joined in

56
Q

secondary structure

A

refers to one of the two 3D shapes that are the result of hydrogen bonding

57
Q

alpha helix

A

a possible secondary structure. coiled shape

58
Q

beta pleated sheet

A

a secondary structure, accordion shape

59
Q

tertiary structure

A

complex globular shape, due to interactions between R groups such as hydrophobic interactions, van der Waals interactions, hydrogen bonds, disulfide bridges

60
Q

quaternary structure

A

the association of 2+ polypeptide chains into one large protein (ex: collagen and hemoglobin)

61
Q

protein function is dependent on

A

shape and folding, ability to recognize and bind to some other molecule

62
Q

native

A

natural 3D folding has occurred

63
Q

denatured

A

a protein that has lost its 3D shape which usually kills or changes its function

ap bio (24 decks)

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