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BIOL I > CHAPTER 3 > Flashcards

CHAPTER 3 Flashcards

1
Q

What are the molecules that make up organism?

A

proteins, carbohydrates, lipids, and nucleic acids

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2
Q

polymers

A

macromolecules

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3
Q

monomers

A

smaller molecules that create polymers

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4
Q

macromolecules

A

polymers containing thousands or more atoms

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5
Q

functional groups

A

group that has specific properties for macromolecules

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6
Q

hydroxyl

A

R-O-H; polar; hydrogen bonds with water to help dissolve molecules; enables linkages to other molecules by condensation

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7
Q

aldehyde

A

O=C-H; polar; C=O group is very reactive; important in building molecules and energy-releasing reactions

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8
Q

keto

A

O=C; polar; C=O group is important in carbohydrates and energy reactions

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9
Q

carboxyl

A

O=C-OH; charged; acidic; ionizes in living tissues to form COO- and H+; enters into condensation reactions by giving up OH-; important in energy-releasing reactions

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10
Q

amino

A

H-N-H; charged; basic; accepts H+ in living tissues to form NH3+; enters into condensation reactions by giving up H+

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11
Q

phosphate

A

O=P-O3; charged; acidic; enters into condensation reactions by giving up OH-; when bonded to another phosphate, hydrolysis releases much energy

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12
Q

sulfhydryl

A

by giving up H+, two SH groups can react to form a disulfide bridge, thus stabilizing protein structure

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13
Q

methyl

A

C-H3; nonpolar; important in interacting with other nonpolar molecules and in energy transfer

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14
Q

isomers

A

molecules with the same chemical formula, but the atoms are arranged differently
(STRUCTURAL - differ in how atoms are joined
CIS-TRANS - different orientation around a double bond
OPTICAL - mirror images)

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15
Q

condensation reactions

A

energy is used to make covalent bonds between monomers to make a polymer; a water molecule is removed

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16
Q

hydrolysis reactions

A

polymers are broken down into monomers; energy is released and water is consumed

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17
Q

polypeptide chains

A

single, unbranched chains of amino acids folded into specific 3-D shapes as defined by the sequence of amino acids

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18
Q

enzymes

A

catalyze (speed up) biochemical reactions

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19
Q

structural proteins

A

provide physical stability and movement

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20
Q

defensive proteins

A

recognize and respond to nonself substances (e.g., antibodies)

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21
Q

signaling proteins

A

control physiological processes (e.g., hormones)

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22
Q

receptor proteins

A

receive and respond to chemical signals

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23
Q

membrane transporters

A

regulate passage of substances across cellular membranes

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24
Q

storage proteins

A

store amino acids for later use

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25
Q

transport proteins

A

bind and carry substances within the organism

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26
Q

gene regulatory proteins

A

determine the rate of expression of genes

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27
Q

motor proteins

A

cause movement of structures in the cell

28
Q

amino acids

A

carboxyl and amino groups; function as both acid and base

29
Q

side chains (R-groups)

A

have functional groups and determine where amino acids are grouped; determine how the protein can twist and fold; determine secondary and tertiary structure

30
Q

oligopeptides (peptides)

A

short polymers of 20 or fewer amino acids

31
Q

polypeptides

A

longer polymers

32
Q

peptide linkages (peptide bonds)

A

condensation reaction that covalently bonds amino acids together

33
Q

primary structure

A

sequence of amino acids

34
Q

secondary structure

A

ALPHA helix - right-handed coil resulting from hydrogen bonding between N-H groups and C=O groups
BETA pleated sheet - two or more polypeptide chains are aligned; hydrogen bonds form between the chains

35
Q

tertiary structure

A

folding results in the specific 3-D shape; determined by interactions between R-groups; outer surfaces present functional groups that can interact with other molecules

36
Q

denatured protein

A

protein that has been heated and has its secondary and tertiary structure broken down; when cooled it can return to normal because of the primary structure information and instructions

37
Q

quaternary structure

A

results from interaction of subunits by all reactions

38
Q

How do proteins bind with specific molecules?

A

SHAPE - there must be a general “fit” between the protein and the other molecule
CHEMISTRY - surface R-groups interact with other molecules via ionic, hydrophobic, or hydrogen bonds

39
Q

What conditions affect secondary and tertiary structure?

A

HIGH temperature
pH CHANGES
HIGH concentrations of POLAR molecules
NONPOLAR substances, via HYDROPHOBIC interactions

40
Q

How can protein shape change?

A

INTERACTIONS WITH OTHER MOLECULES - enzyme changes shape when it comes into contact with reactant
COVALENT MODIFICATION - addition of a chemical group, such as a phosphate, to an amino acid

41
Q

chaperones

A

proteins that prevent other proteins from binding to the wrong molecules after denaturation or when they are newly made and still unfolded; heat shock proteins surround a denatured protein and allow it to refold

42
Q

carbohydrates (C1H2O1)n

A

-sources of stored energy
-used to transport energy
-carbon skeleton for many other molecules
-form extracellular structures such as cell walls

43
Q

saccharides

A

mono - simple sugars
di - two simple sugars linked by covalent bonds
oligo - 3 to 20 monosaccharides
poly - hundreds or thousand of monosaccharides

44
Q

glucose

A

energy source; exists as a straight chain or ring form (alpha OH down or beta OH up and can interconvert)

45
Q

pentoses

A

five-carbon sugars (ribose and deoxyribose for RNA and DNA)

46
Q

hexoses

A

six-carbon sugars; some are structural isomers

47
Q

glycosidic bonds

A

condensation reactions that bind monosaccharides together to form disaccharides and so on

48
Q

polysaccharides

A

large polymers of monosaccharides connected by glycosidic bonds; some are branches
(STARCH - storage of glucose in plants
GLYCOGEN - storage of glucose in animals
CELLULOSE - very stable, good for structural components)

49
Q

How can carbohydrates be modified?

A

addition of functional groups to form
-Sugar phosphates
-Amino sugars
-Chitin

50
Q

lipids

A

nonpolar hydrocarbons; insoluble in water; if close together, weak but additive van der Waals forces hold them together in aggregates

51
Q

What are types of lipids?

A

-FATS and OILS which store energy
- PHOSPHOLIPIDS which have a structural role in cell membranes
-CAROTENOIDS and CHLOROPHYLLS which capture light energy in plants
-STEROIDS and MODIFIED FATTY ACIDS which are hormones and vitamins
-ANIMAL FAT which give thermal insulation
-LIPID COATING which is around nerves and provides electrical insulation
-OIL and WAX which is on skin, fur, and feathers, repels water, and slows evaporation

52
Q

triglycerides

A

three fatty acids + glycerol (e.g., fats and oils)

53
Q

fatty acid

A

nonpolar hydrocarbon chain with a polar carboxyl group

54
Q

ester linkages

A

condensation reactions which bond carboxyls with hydroxyls of glycerol

55
Q

saturated fatty acid

A

no double bonds between carbons; saturated with H atoms (animal fats; solid at room temperature)

56
Q

unsaturated fatty acid

A

one or more double bonds in the carbon chain results in kinks that prevent packing (plant oils; liquid at room temperature)

57
Q

cis fats

A

H atoms are on the same side

58
Q

trans fats

A

H atoms are on opposite sides of the C=C bond; result from hydrogenation of vegetable oils to produce a saturated fat (e.g. for margarine), but some of the cis bonds convert to trans; may contribute to heart disease and stroke

59
Q

omega-3 fatty acids

A

protect against heart disease and stroke; first C=C bond is at position 3 in the fatty acid chain

60
Q

phospholipids

A

fatty acids bound to glycerol; a phosphate group replaces one fatty acid; they are amphipathic

61
Q

amphipathic

A

“HEAD” - phosphate group which is hydrophilic
“TAILS” - fatty acid chains which are hydrophobic

62
Q

bilayer

A

in water, phospholipids line up with the hydrophobic tails together and the phosphate head facing outward (in biological membranes there is a phospholipid bilayer structure)

63
Q

phospholipids + proteins =

A

lipoproteins (which transport lipids such as cholesterol in the blood)

64
Q

carotenoids

A

light-absorbing pigments (e.g., beta carotene traps light energy for photosynthesis; in humans, beta carotene breaks down into Vitamin A)

65
Q

steroids

A

multiple rings share carbons; cholesterol is important in membranes; others are hormones

66
Q

waxes

A

long-chain alcohol bound to an unsaturated fatty acid

BIOL I (12 decks)

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