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BIO 101 EXAM 1 > CHAPTER 3 > Flashcards

CHAPTER 3 Flashcards

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1
Q

what are the molecules that make up organisms?

A

-proteins
-carbohydrates
-lipids
-nucleic acids
all but lipids are polymers of smaller molecules called monomers

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2
Q

define monomers. define polymers

A

-monomers: A small molecule, two or more of which can be combined to form polymers
-polymers: A large molecule made up of similar or identical subunits called monomers.

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3
Q

define macromolecules

A

-polymers containing thousands of more atoms. (large lipids are also treated as macromolecules)
-macromolecules function depends on the properties of functional groups; each group has a specific property (like polarity)
-a single macromolecule may contain many different functional groups

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4
Q

define functional groups

A
  • A characteristic combination of atoms that contributes specific properties when attached to larger molecules. A group of species that function in similar ways, whether or not they use the same resources.
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5
Q

define isomers and name the three types

A

-molecules with the same chemical formula, but the atoms are arranged differently
-structural isomers , cis-trans isomer , and optical isomers

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6
Q

define structural isomers

A

-differ in how atoms are joined

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7
Q

define cis-trans isomers

A

-centered around a double bond with a toms on either side in different orientations with respect to each other
-cis:
-trans:

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8
Q

define optical isomers

A

-mirror images

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9
Q

define condensation reactions

A

-energy is used to make covalent bonds between monomers to make a polymer; a water molecule is removed
-also known as dehydration reaction

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10
Q

define hydrolysis reactions

A

-polymers are broken down into monomers; energy is realized and water is consumed (added)

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11
Q

what chains do proteins consist of? how are the chains folded?

A

-they consist of one or more polypeptide chains
-the chains are folded into specific 3D shapes as defined by the sequence of amino acids
-proteins have diverse functions

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12
Q

define polypeptide chains

A

a single, unbranched chain of amino acids

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13
Q

what are the 10 types if proteins?

A

-enzymes
-structural proteins
-defensive proteins
-signaling proteins
-receptor proteins
-membrane transporters
-storage proteins
-transport proteins
-gene regulatory proteins
-motor proteins

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14
Q

enzymes function

A

catalyze (speed up) biochemical reactions

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15
Q

structural proteins function

A

provide physical stability and movement

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16
Q

defensive proteins function

A

recognize and respond to non self substances (ex: antibodies)

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17
Q

signaling proteins function

A

control physiological processes (ex: hormones)

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18
Q

receptor proteins function

A

receive and respond to chemical signals

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19
Q

membrane transporters function

A

regulate passage of substances across cellular membranes

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20
Q

storage proteins function

A

store amino acids for alter use

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21
Q

transport proteins function

A

bind and carry substances within the organism

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22
Q

gene regulatory proteins function

A

determine the rate of expression of a gene

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23
Q

motor proteins function

A

causes movement of structures in the cell

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24
Q

amino acids

A

-they have carboxyl and amino groups which allows them to function both as an acid and base
-amino acids are grouped based on the side chains
-the alpha carbon (central atom) is asymmetrical
-amino acids can be optical isomers: D-amino and L-amino acids

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25
Q

define side chains and R-groups

A

The distinguishing group of atoms of a particular amino acid. Also called a side chain.

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26
Q

amino acids with electrically charged hydrophilic side chains

A

positive charge: arginine (Arg; R), histidine (His; H), lysine (Lys; K)

negative charge: aspartic acid (Asp; D), glutamic acid (Glucose; E)

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27
Q

amino acids with polar but uncharged side chains (hydrophilic)

A

serine (Ser; S)
threonine (Thr; T)
asparagine (Asn; N)
glutamine (Gln; Q)
tyrosine (Tyr; Y)

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28
Q

special cases of amino acids

A

cysteine (Cys; C)
glycine (Gly; G)
proline (Pro; P)

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29
Q

amino acids with non polar hydrophobic side chains

A

alanine (Ala; A)
isoleucine (Ile; I)
leucine (Leu; L)
methionine (Met; M)
phenylalanine (Phe; F)
tryptophan (Trp; W)
valine (Val; V)

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30
Q

disulfide bridge

A

the cysteine amino acid
-SH group can react with another cysteine side chain to form a disulfide bridge, or disulfide bond (-s-s-) in this reaction the 2 H atoms are taken out
-these are important in protein folding but most cysteines in a protein are not involved in disulfide bridges

31
Q

oligopeptides, or peptides

A

short polymers of 20 or fewer amino acids

32
Q

polypeptide

A

longer polymer

33
Q

peptide linkages/ bonds

A

amino acids bond together covalently in a condensation reaction (water being taken out) and are linked together with peptide bonds

34
Q

the four levels of protein structures

A

-primary
-secondary
-tertiary
-quaternary

35
Q

primary structure of a protein

A

-the sequence of amino acids
-the properties of side chain functional groups determine h ow the protein can twist and fold which determines the secondary and tertiary structure

36
Q

secondary structure

A

α helix: right-handed coil resulting from hydrogen bonding between N-H groups and C=O groups

β pleated sheet: two or more polypeptide chains are aligned; hydrogen bonds form between the chains

37
Q

tertiary structure

A

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

38
Q

denatured

A

-if a protein is heated, secondary and tertiary structures break and the protein is said to be denatured

-when cooled some proteins return to normal tertiary structures; which means information to specify protein shape is in the primary structure

39
Q

quaternary structure

A

these results from interaction of subunits by hydrophobic interactions, van Der Waals forces, ionic attractions and hydrogen bonds
-each subunit has its own unique tertiary structure

40
Q

proteins bind non-covalently with specific molecules, the specificity is determined by?

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

41
Q

conditions that affect secondary and tertiary structures

A

-high temperatures
-pH changes
-high concentrations of polar molecules
-non-polar substances, via hydrophobic interactions

42
Q

protein shape can change as a result of?

A

-interaction with other molecules (EX: an enzyme changes shape when it comes into contact with a reactant )
-covalent modification: addition of a chemical group, such as a phosphate, to an amino acid

43
Q

Chaperones

A

proteins can bind to the wrong molecules after denaturation or when they are newly made and still unfolding; chaperones are proteins that help prevent this by surround a denatured protein and allowing it to refold

44
Q

carbohydrates

A

(C1H2O1)n
-sources of stored energy
-used to transport stored energy
-carbon skeletons for many other molecules
-form extracellular structures such as cell walls

45
Q

monosaccharide? disaccharide? oligosaccharide? polysaccharide?

A

-simple sugar (just one)
-two simple sugars linked by covalent bonds
-3 to 20 monosaccharides
-hundreds or thousands of monosaccharides

46
Q

glucose

A

-all cells use glucose as an energy source
-exists as a straight chain or ing form
-ring is more stable if there dis a ring there are two different types of glucose ( α- or β-glucose), that can interconvert

47
Q

types of monosaccharides

A

-pentoses
-hexoses

48
Q

pentoses

A

five-carbon sugars; includes ribose (RNA; has an oxygen) and deoxyribose (DNA; takes away oxygen)

49
Q

hexoses

A

six-carbon sugars; some are structural isomers
α-mannose, α-glucose, fructose

50
Q

glycosidic bonds

A

monosaccharides bind together in condensation reaction to form glycosidic bonds to form disaccharides

51
Q

oligosaccharides

A

several monosaccharides linked by glycosidic bonds; often covalently bonded to proteins and lipids on cell surfaces, where they serve as recognition signals

52
Q

examples of glycosidic bonds

A

sucrose
maltose
cellobiose

53
Q

polysaccharides

A

large polymers of monosaccharides connected by glycosidic bonds; some are branched.

54
Q

what are the 3 types of polysaccharides

A

-starch: storage of glucose in plants
-glycogen: storage of glucose in animals
-cellulose: very stable, good for structural components; only found in plant; often make up cell walls in plants (humans cannot digest)

55
Q

carbohydrates can be modified by the addition of functional groups to form?

A

-sugar phospahtes
-amino sugars
-chitin

56
Q

lipids

A

non-polar hydrocarbons; insoluble in water; if close together, weak but additive van Der Waals forces hold them together in aggregates

57
Q

types of lipids?

A

-fats and oils: store energy
-phospholipids: structural role in cell membranes
-carotenoids and chlorophylls: capture light energy in plants
-steroids and modified fatty acids: hormones and vitamins
-animal fat: thermal insulation
-lipid coating around nerves: provides electrical insulation
-oil and wax on skin, fur, and feathers: repel water and slows evaporation

58
Q

triglycerides

A

fats and oils made of three fatty acids and a glycerol

59
Q

fatty acid

A

non polar hydrocarbon chain with a polar carboxyl group

60
Q

ester linkages

A

carboxyl bond with hydroxyls in glycerol through ester linkages; from condensation reactions

61
Q

saturated fatty acid

A

no double bonds between carbons: it is matured with H atoms so they tightly pack together (animal fats; solid at rom temperature)

62
Q

unsaturated fatty acid

A

-one or more double bonds in the carbon chain result in kinks that prevent packing (plant oils; liquid at room temperature)
-double bonds in naturally occurring unsaturated fats are sis (H atoms are on the same side)

63
Q

trans fats

A

-H atoms are on opposite sides of the C=C bond (trans)
-may contribute to heart disease and stroke

64
Q

hydrogenation

A

-the process by which hydrogen atoms are added to unsaturated fats and oils.
-trans fats result from hydrogenation of vegetable oils to produce a saturated fat (EX margerine), but some of the cis bonds convert to trans

65
Q

omega-3 fatty acids

A

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

66
Q

phospholipids

A

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

67
Q

phospholipids are amphipathic which means?

A

-“head” is a phosphate group which is hydrophilic
-“tails” are fatty acid chains which is hydrophobic

68
Q

bilayer

A

in water, phospholipids line up with the hydrophobic tails together and the phosphate heads facing outwards

69
Q

phospholipid bilayer

A

biological membranes have this kind of structure

70
Q

lipoproteins

A

in animals, phospholipids and proteins form lipoproteins which transport lipids such as cholesterol in the blood

71
Q

carotenoids

A

light-absorbing pigment EX:β-carotene traps light energy for photosynthesis and in humans it breaks down into vitamin A

72
Q

steroids

A

multiple rings share carbons. cholesterol is important in membranes; other steroids are hormones

73
Q

waxes

A

long-chain alcohol bound to an unsaturated fatty acid

74
Q
A

BIO 101 EXAM 1 (5 decks)

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