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AP Bio > Molecules of Life > Flashcards

Molecules of Life Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Organic Chemistry

A

deals with organic compounds

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2
Q

Cell composition

A

70 – 95% water, the rest is carbon based compounds

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3
Q

Major elements in living things:

A

C, O, H, N, S, P

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4
Q

Organic compounds-

A

compounds containing

carbon bonded to carbon–only formed within living things (usually also has H)

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5
Q

Inorganic compounds-

A

compounds that do not contain

carbon bonded to carbon–found in living + non living world

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6
Q

Carbon

A

4 valence electrons. Most likely to share electrons in covalent bonds- can form four directions of bonds

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7
Q

What different shapes can carbon compounds can take on?

A

straight (chain), branched, closed rings

Assume H are bonded to the extra Cs

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8
Q

Hydrocarbons-

A

contain only
C and H. Major component of
fossil fuels. Store large amounts of
organic compounds

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9
Q

Isomers-

A

compounds that have the same molecular formula but

different structural formulas

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10
Q

Structural isomers-

A

differ in arrangement of atoms

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11
Q

Geometric isomers

A

same arrangement, but

subtle differences in shape or in spatial arrangement

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12
Q

Stereoisomers

A

mirror images- one is

active and inactive

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13
Q

Functional Groups

A

Groups of atoms attached to
carbon skeletons; Most commonly involved in
chemical reaction; Each gives unique properties to the molecule

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14
Q

Polymer-

A

large molecule consisting of many identical or similar subunits strung together

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15
Q

monomer

A

each individual subunit

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16
Q

one nucleotide/monomer of a dna molecule

A

sugar+phosphate+base

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17
Q

Condensation/ dehydration synthesis-

A

links monomers together
by removing one
water molecule for each monomer added

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18
Q

synthesis

A

build up

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19
Q

how does condensation work

A

One molecule contributes the

H and the other contributes the OH. Each monomer bonds each other covalently. Requires energy.

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20
Q

Hydrolysis

A

reverse of above- breaking bonds in a
polymer by adding water. H from water attaches to one molecule
OH from water attaches to adjacent molecule
releases energy

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21
Q

Carbohydrates (sugars, starches) shape

A

rings

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22
Q

Monosaccharides

A

carbohydrate sugars; singular; have formula of
CH2O in multiples.
- If these monosaccharides are not used immediately, they can form larger sugars for long term storage (humans–be stored in the liver as glycogen)

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23
Q

Monosaccharides ex

A

Glucose (C6H12O6) Major nutrient for cells. During cellular respiration-cells release energy stored in glucose molecules

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24
Q

Disaccharides:

A

double sugar consisting of 2 monosaccharides joined by a covalent bond

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25
Q

Polysaccharides

A

macromolecules- polymers in which

a few 100 to a few 1000 monosaccharides are linked together

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26
Q

molecules of life

A

carbs, lipids, nucleic acids, proteins

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27
Q

Storage polysaccharides

A

starch, glycogen

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28
Q

Starch-

A

polymer of only glucose. Storage unit synthesized in plants; helical shape; major source of starch-potatoes, grains

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29
Q

Glycogen-

A

polymer of only glucose. Stored in
liver and muscle cells of animals; very branched; Depleted in about
a day if not replenished by food

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30
Q

Structural polysaccharides:

A

cellulose, chitin

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31
Q

cellulose

A

major component of cell walls of plants; Parallel cellulose molecules are held together by hydrogen bonds- arranged in units called microfibrils, eventually form super coiled fibrils

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32
Q

wood main ingredient

A

cellulose

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33
Q

digestion of cellulose

A

Few organisms can digest cellulose- important roughage in the human diet,
moves everything along, and stimulates the digestive tract to secrete mucus. Some bacteria and microorganisms can digest it- cow has this bacteria inside a pouch called a rumen connected to the stomach and gets energy from the grass

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34
Q

Chitin

A

Found in exoskeletons of
arthropods (insects, lobsters…)Also found in
fungi

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35
Q

lipids

A

have little or no affinity for water

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36
Q

types of lipids

A

triglycerides, phospholipids, steroids

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37
Q

Triglycerides (fats): composition

A

3 fatty acids + 1 glycerol

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38
Q

fatty acids

A

Long carbon skeleton
o At one end- head consisting of a carboxyl group
o Attached to head is long hydrocarbon tail

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39
Q

how does glycerol attach to fatty acid

A

attaches to fatty acid by covalent bonds

40
Q

Saturated Fats:

A

No double bonds between carbon atoms composing the tail of the fatty acids; As many hydrogen atoms as possible are bonded to the carbon skeleton

41
Q

ex and dangers of saturated fats

A

animal fats–butter, lard. Can contribute to atherosclerosis because deposits called
plaque develop on internal lining of blood vessels arteries get more narrow
blocking blood flow

42
Q

Unsaturated Fats:

A

Contains one or more double bond in the tail, formed by the removal of H atoms from the carbon skeleton. Has “kink” in shape wherever the double bond occurs. Prevents molecules from packing together close enough to solidify.
o Liquid at room temp

43
Q

ex unsaturated fats

A

oil

44
Q

function of triglycerides

A

energy storage– Gram of fat stores more than–g of fats more than 2x energy of g of polysaccharides (1 g of fat is 9kcal and 1 g of ps is 4 kcal)
o Humans store fat in adipose cells- can
swell and shrink depending on how much fat is stored in the cells

45
Q

phospholipids

A

Have two fatty acids and a
negatively charged phosphate group attached to the glycerol. Hydrocarbon tail is
hydrophobic. Phosphate group is
hydrophilic bc it’s charged so water attracted

46
Q

function phospholipids

A

major components of cell membranes. Arranged in bilayer, Hydrophilic heads are on outside in contact with water, hydrophobic tails are sandwiched in the interior away from water

47
Q

steroids + ex

A

Lipids characterized by four interconnected rings (no fatty acids), Component of
membranes of animal cells, Precursor from which most other steroids are synthesized (like sex hormones)
ex: cholesterol

48
Q

Carotenoids:

A

Orange-yellow pigment found in plants, - Plays role in photosynthesis

49
Q

Proteins

A

Account for more than 50% of nonwater part of cells
- Used for structure, storage, transport, signaling, movement,
defense
- Most structurally sophisticated- each has
a unique 3d shape

50
Q

Amino Acids:

A

Contain both a carboxyl group and an amino group; - Each amino acid has one carbon in center, bonded to a H atom, carboxyl group, amino group, variable chain represented by R
20 kinds of amino acids make up proteins

51
Q

acidic v basic in ionic bonds

A

proton donor–acidic

proton receiver–basic

52
Q

R group

A

side chain/variable that makes each amino acid different

53
Q

Examples of R group variations

A

Nonpolar side chains (hydrophobic)
o Polar side chains (hydrophilic)
o Acidic amino acids
o Basic amino acids

54
Q

acidic amino acids

A

side chains that are negative in charge

55
Q

Basic amino acids-

A

side chains that are positive in charge

56
Q

Polypeptide chains:

A

Amino acids join one another by dehydration synthesis, forming a
covalent bond called peptide bond. - Backbone is composed of
central Carbon, carboxyl group, amino group, side chains stick out

57
Q

Polypeptide chain-

A

polymer of many amino acids linked by peptide bonds

58
Q

Protein Conformation:

A

Protein consists of one or more polypeptide chain twisted, wound,
and folded upon itself to form a
macromolecule with a 3d shape, or conformation(shape). Protein’s function depends on conformation.

59
Q

Globular v fibrous proteins

A

Globular proteins–glob shaped; ex–enzymes
Fibrous proteins–used for structure
ex–keratin

60
Q

conformation proteins process

A

they form based on bonds
if two both have hydrophobic or hydrophilic side chains they might bond and then the entire proteins folds into a shape based on all those bonds. if one is replaced the protein folds the wrong way.

61
Q

Primary structure proteins

A

Sequence of amino acids. Even slight change in primary structure can affect
the protein’s ability to function

62
Q

ex of primary structure issue

A

sickle cell anemia, one amino acid is substituted for another in the primary structure of hemoglobin, preventing hemoglobin from forming properly

63
Q

Secondary structure proteins

A

Segments of polypeptide chains are repeatedly coiled or
folded in patterns due to
hydrogen bonds along the back bone. Weak positive charge of H attached to N has an attraction to
the weak negative of an O on a nearby carboxyl group

64
Q

two possible shapes–secondary structure proteins

A

alpha helix and beta pleated sheet

65
Q

alpha helix and beta pleated sheet

A

two shapes that can emerge (don’t have to, can coexist)

66
Q

Alpha helix-

A

coiled shape
ex–
all alpha helix example–hair. Proteins with these are more
elastic bc the H bonds can break and reform

67
Q

beta pleated sheet

A

chain folds back and forth, and
two regions of the chain lie parallel to one another. Found in fibrous proteins-fibroin (found in silk). proteins with these are stronger.

68
Q
  • Tertiary structure
A

Irregular contortions from bonding between
the side chains of the amino acids due to hydrophobic interaction. Amino acids with
hydrophobic side chains congregate at the core of the protein to avoid contact with water. Also due to H bonds and ionic bonds
reinforced by disulfide bonds.

69
Q

Disulfide bonds

A

help reinforce the conformation- form

where two amino acids with sulfhydryl groups bond to each other

70
Q

Quaternary structure

A

Two or more subunits join together into one functional macromolecule;

71
Q

subunit

A

each polypeptide chain in quaternary structures

72
Q

ex quaternary structure

A

Ex- collagen- helical subunits supercoiled into a larger triple
helix, giving it great strength; Hemoglobin consists of
2 kinds of polypeptide chains w 2 of each

73
Q

Factors determining conformation:

A

Conformations occur spontaneously as
the protein is being synthesized in the cell; If pH, salt, temp, or other environmental aspects are changed, the
protein may denature.
Protein can sometimes re-form its original shape when
returned to its normal environment

74
Q

denature

A

protein unravels and becomes inactive

75
Q

factors that disrupt conformation

A

Organic solvents (ether, chloroform) turn proteins inside out
o Chemicals can disrupt bonds
o Heat can disrupt conformations

76
Q

ex of heat disrupting conformation

A

(ex-

cooking an egg denatures proteins in egg whites and makes it solidify

77
Q

Nucleic Acids (+ex)

A

nucleotides are connected, forming a chain

ex–DNA, RNA

78
Q

Nucleotides

A

monomers that compose the polymers of nucleic acids

79
Q

parts to nucleotide

A

nitrogenous base
5 carbon sugar
phosphate group

80
Q

what kind of polymer is a nucleic acid?

A

polynucleotide

81
Q

polynucleotide

A

Nucleotides are joined by covalent bonds called phosphodiester
linkages between
the phosphate of one nucleotide and sugar of next, resulting in repeating sugar-phosphate-sugar-phosphate

82
Q

DNA (deoxyribonucleic acid)

A

Contains deoxyribose sugar (missing a ribose group)
Genetic material that organisms
inherit from their parents

Very long, consisting of
thousands of genes

Sequence of the bases in DNA
encode instructions for all cell activities

83
Q

RNA (ribonucleic acid)

A

o Contains a ribose sugar. Acts as messenger by bringing the genetic info found in the DNA in the nucleus to the ribosome where proteins are made. There, proteins are formed, from the encoded instructions in the RNA.

84
Q

Bases:

A

pyrimidines, purines, form H bonds w one another

85
Q

pyrimidines

A

a single ring–Cytosine, Thymine, Uracil

86
Q

purines

A

double ring–Adenine, Guanine

87
Q

James Watson and Francis Crick

A

discovered the shape of DNA molecule, double helix

88
Q

double helix

A

Consists of two polynucleotide chains that
spiral around an imaginary axis
- Phosphate and sugar are on
outside of the helix and the bases form the rungs
- Two strands are held together by
H bonds between the paired bases

89
Q

bases that always bond

A

Adenine always bonds thymine, guanine pairs with

cytosine.

90
Q

uracil

A

uracil only found in RNA and thymine only found in DNA

Uracil is the RNA replacement for Thymine

91
Q

nucleotides that don’t form polynucleotides

A

ATP, coenzymes, Chemical messengers between cells

92
Q

ATP

A

(adenosine triphosphate)
o Made up of sugar, base, 3 phosphate groups ; can transfer a phosphate group to another molecule thereby giving off energy–energy currency in cells

93
Q

coenzymes/enzyme helpers +ex

A

o Accepts hydrogen atoms and electrons from one molecule
and transfers them to different sites
(ex–NAD+, FAD)

94
Q

ex of Chemical messengers between cells

A

Ex- cyclic AMP, or cAMP- called a second messenger- can

activate proteins within the cell

95
Q

polarity rules for r groups

A

polarity: O > N > C = H.

AP Bio (35 decks)

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