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Bio 110 > Bio 110 Chapter 3 (3.8-3.16) > Flashcards

Bio 110 Chapter 3 (3.8-3.16) Flashcards

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1
Q

lipids are

A

water insoluble
hydrophobic
contain twice as much energy as a polysaccharide

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2
Q

lipids are important in

A

long-term energy storage

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3
Q

lipids consist mainly of

A

carbon and hydrogen atoms linked by nonpolar covalent bonds.

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4
Q

lipids differ from carbohydrates, proteins and nucleic acids because

A

they are not macromolecules, not built from similar monomers.

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5
Q

lipids vary a great deal in

A

structure and function

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6
Q

3 types of lipids

A

fats, phospholipids, and steroids.

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7
Q

a large lipid made from glycerol and 3 fatty acids

A

fat

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8
Q

glycerol is

A

an alcohol with 3 carbons that each have an -OH

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9
Q

a fatty acid is

A

a carboxyl group and a hydrocarbon chain 16 or 18 carbon atoms in length.

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10
Q

synonym for fat

A

triglyceride

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11
Q

a fatty acid can link to a glycerol by a

A

dehydration reaction

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12
Q

fatty acids containing one or more double bonds are

A

unsaturated fatty acids

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13
Q

double bonds in fatty acids cause

A

kinks or bends in the chain
prevent them from packing together tightly and solidifying at room temperature.
fewer hydrogen atoms because of the double bond.

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14
Q

fats with the max number of hydrogens are called

A

saturated fatty acids

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15
Q

unsaturated fats include

A

corn and olive oils

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16
Q

unsaturated fats include

A

most animal fats

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17
Q

hydrogenated vegetable oils are unsaturated fats that have been

A

converted to saturated fats by adding hydrogen (margarine)

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18
Q

hydrogenation creates

A

trans fats associated with health risks.

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19
Q

phospholipids are

A

structurally similar to fats and the major component of all cell membranes.

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20
Q

phospholipids are structurally similar to fats in that:

A

phospholipids contain 2 fatty acids instead of 3 attached to glycerol, but a phosphate group is attached to glycerol’s 3rd carbon.

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21
Q

hydrophilic and hydrophobic ends of multiple molecules assemble in a

A

bilayer of phospholipids to form a membrane.

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22
Q

The phospholipid bilayer is formed by

A

the hydrophobic tails of the fatty acids clustering in the center and the hydrophilic phosphate heads facing the watery environment on either side of the membrane.

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23
Q

lipids in which the carbon skeleton contains 4 fused rings

A

steroids

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24
Q

a common component in animal cell membranes and starting material for making other steroids, including sex hormones

A

cholesterol.

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25
Q

too much cholesterol can contribute to

A

atherosclerosis

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26
Q

anabolic steroids

A

synthetic variants of testosterone
can cause a buildup of muscle and bone mass
often prescribed to treat anemia and diseases that destroy body muscle.

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27
Q

abuse of anabolic steroids include

A

mood swings, depression, liver damage, cancer, high cholesterol and HBP.

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28
Q

proteins are

A

involved in nearly every dynamic function in your body and are very diverse

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29
Q

a protein is

A

composed of differing arrangements of a common set of 20 amino acid monomers, and is a polymer of amino acids.

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30
Q

amino acids have

A

an amino group and a carboxyl group (which makes it an acid.)

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31
Q

bonded to the alpha carbon in an amino acid is:

A

an amino group
a carboxyl group
a hydrogen atom
and R group

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32
Q

an R group is

A

the side chain,differs with each amino acid and determines the specific properties of each of the 20 amino acids found in proteins.

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33
Q

amino acids are classified as

A

hydrophobic (nonpolar)

hydrophilic (polar)

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34
Q

amino acid monomers are linked together to form

A

polymers by dehydration reactions.

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35
Q

the dehydration reaction in amino acids

A

joins the carboxyl group of one amino acid to the amino group of the next with a peptide bond.

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36
Q

peptide bond

A

covalent bond between amino acids

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37
Q

a chain of 3 or more amino acids is called a

A

polypeptide.

38
Q

most polypeptides are at least

A

100 amino acids in length; some are 1000 or more.

39
Q

functioning proteins are

A

1 or more polypeptide chains coiled, twisted and folded into a 3D shape.

40
Q

A polypeptide is not the same as a

A

protein.

41
Q

probably the most important role for proteins is as

A

enzymes

42
Q

Enzymes serve as

A

metabolic catalysts, and increase the rate of a chemical reaction without undergoing any permanent chemical change itself, regulate chemical reactions within cells

43
Q

provide associations between body parts

A

structural proteins

44
Q

found within muscles

A

contractile proteins (movement)

45
Q

include antibodies of the immune system

A

defensive proteins

46
Q

coordinate body activities through cell communication

A

signal proteins (hormones and other chemical messengers)

47
Q

transmit signals into cells, may be built into cell membranes

A

receptor proteins

48
Q

proteins that carry oxygen

A

transport proteins (hemoglobin)

49
Q

serve as a source of amino acids for developing embryos

A

storage proteins

50
Q

determines the protein’s specific function

A

the shape of the protein like a lock and key

51
Q

if a protein’s shape is altered, it

A

can no longer function.

52
Q

the process where a polypeptide chain unravels or loses it’s shape and therefore function is

A

denaturation

53
Q

can cause denaturation of proteins:

A

change in salt concentration, pH or high heat.

54
Q

4 levels of structure in a protein

A

primary
secondary
tertiary
quaternary

55
Q

the primary structure is

A

its unique sequence of amino acids

56
Q

the unique sequence of amino acids is determined by

A

the cell’s genetic information (genes)

57
Q

slightest change in amino acids in a protein can result in

A

changes in the protein’s ability to function

58
Q

sickle cell results from

A

change to hemoglobin’s primary structure

59
Q

secondary structure results from

A

coiling or folding of the polypeptide.

60
Q

coiling of a protein results in

A

an alpha helix

61
Q

folding of a protein results in a

A

beta pleated sheet (in spider webs)

62
Q

coiling and folding are maintained by

A

regularly spaced hydrogen bonds between H atoms and O atoms along the backbone of the polypeptide chain, giving strength.

63
Q

beta pleated sheets make

A

the core of globular and fibrous proteins

64
Q

proteins can have various combos of

A

alpha helix and beta pleated sheets.

65
Q

tertiary structure is

A

the overall 3D shape of a polypeptide.

66
Q

tertiary structure results from

A

interactions between R groups

67
Q

disulfide bridges (covalent bonds) may further

A

strengthen the protein’s shape.

68
Q

quaternary structure

A

when 2 or more polypeptide chains (subunits) associate.

69
Q

when proteins fold incorrectly

A

disease can result.

70
Q

collagen has 3 helices giving

A

strength.

71
Q

collagen makes up

A

40% of protein in the human body.

72
Q

the amino acid sequence of a polypeptide is programmed by

A

a discrete unit of inheritance known as a gene

73
Q

Genes consist of

A

DNA-a type of nucleic acid

74
Q

DNA provides

A

directions for its own replication and genetics are passed on to each daughter cell.

75
Q

DNA programs a cell’s activities by

A

directing the synthesis of proteins.

76
Q

DNA does not

A

build proteins directly

77
Q

RNA

A

transcribes DNA, and is translated into proteins.

78
Q

functions of proteins

A 
structure
movement
storage
defense
transport
hormones
receptors
enzymes
79
Q

RNA is translated in the

A

nucleus of eukaryotic cells and the cytoplasm of prokaryotic cells

80
Q

DNA and RNA are composed of

A

monomers called nucleotides

81
Q

nucleotides have

A

3 parts

82
Q

3 parts of a nucleotide

A

a 5 carbon sugar (ribose in RNA and deoxyribose in DNA)
a phosphate group
a nitrogenous base

83
Q

DNA nitrogenous bases are

A

adenine
thymine
cytosine
guanine

84
Q

RNA has

A

uracil instead of thymine

85
Q

a nucleic acid polymer is

A

a polynucleotide

86
Q

a polynucleotide forms

A

from nucleotide monomers when the phosphate of one nucleotide bonds to the sugar of the next by dehydration reactions, resulting in a repeating sugar-phosphate backbone with protruding nitrogenous bases.

87
Q

2 polynucleotide strands wrap around each other to

A

form a DNA double helix

88
Q

Base pairs

A

A and T C and G

89
Q

most people stop producing

A

lactase early in childhood, and can’t digest the milk sugar in lactose.

90
Q

researchers identified 3 mutations that

A

keep the lactase gene permanently turned on.

91
Q

Lactase gene mutations appear to have occurred

A

7,000 years ago at the same time domestication of cattle appeared in regions where dairy was available year round.

Bio 110 (3 decks)

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