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DAT Biology > Chapter 1 - Molecules and Fundamentals of Biology > Flashcards

Chapter 1 - Molecules and Fundamentals of Biology Flashcards

1
Q

Organic molecules contain what elements?

A

carbon, hydrogen, nitrogen, oxygen

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2
Q

Starch is a ____ polysaccharide in ____

A

storage; plants

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3
Q

Linear plant starch is called ____ and contains ____ bonds

A

amylose; alpha-1,4 glycosidic bonds

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4
Q

___ is a critical storage polysaccharide found in humans

A

glycogen

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5
Q

___ is the branched form of plant starch and forms ____ bonds

A

amylopectin; alpha 1,4 and alpha-1,6 glycosidic bonds

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6
Q

glycogen is mainly stores in:

A

liver and muscle cells

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7
Q

structural polysaccharide found in plant cell walls:

A

cellulose

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8
Q

cellulose contains what kind of bonds? what kind of structure results?

A

beta-1,4 bonds; linear strands that pack together in parallel, adjacent strands held together by H bonding

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9
Q

True or false: humans can digest cellulose

A

false: cannot digest cellulose, it passes through our digestive tracts as fiber

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10
Q

chitin is a _____ polysaccharide found in ____ cell walls and _____

A

structural; fungi cell walls; exoskeleton of insects

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11
Q

what kind of bonds does chitin have?

A

Beta-1,4 glycosidic bonds; however is a polymer of N-acetylglucosamine

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12
Q

True or false: chitin is a polymer of glucose molecules

A

false: made of N-acetylglucosamine molecules

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13
Q

proteome

A

all the proteins expressed in a cell under one set of conditions

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14
Q

at physiological pH, amino group in an amino acid is ____ and the carboxyl group is ____

A

protonated; deprotonated

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15
Q

unique enzymes called ____ ____ help peptide bond formation

A

peptidyl transferases (belong to broader class of enzymes called aminoacyl transferases)

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16
Q

primary structure

A

specific order of a peptide which is determined by DNA genes

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17
Q

secondary structure

A

folds that occur in polypeptide chain due to intermolecular interactions between atoms of the polypeptide backbone (not R group atoms)

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18
Q

two of the most common secondary protein structures

A

alpha helices; beta-pleated sheets

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19
Q

tertiary structure

A

3D structure of larger polypeptide chains which occurs due to R-group interactions

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20
Q

what R-group interactions can occur in tertiary structure?

A
  1. ionic bonding
  2. hydrogen bonding
  3. dipole-dipole interactions
  4. London dispersion forces
  5. hydrophobic interactions
  6. disulfide bonds between cysteines
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21
Q

True or false: tertiary structure interactions are usually not covalent

A

true; disulfide bonds are an exception to this

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22
Q

quaternary structure1

A

refers to large proteins that have multiple subunits which come together by the same general interactions used in creating tertiary structure

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23
Q

protein denaturation can occur by:

A

excess temperature, chemicals, pH changes, radiation

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24
Q

True or false: denatured proteins cannot fold back into their functional shapes

A

false: some can, which tells us that all of the information necessary for the folding of those proteins is contained directly within the amino acid sequence.

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25
Q

enzymes are:

A

globular (usually) protein catalysts that speed up specific forward and reverse reactions by lowering their activation energies

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26
Q

enzymes change the energy of:

A

the transition state

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27
Q

enzymes catalyze reactions by:

A

binding to reactant molecules called substrates

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28
Q

active site

A

location on enzymes where the substrate binds to

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29
Q

Because most enzymes are proteins, amino acids give the active site unique properties and ____ ___

A

substrate specificity

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30
Q

specificity constant

A

measures how efficient an enzyme is in converting substrate to product (high specificity constant means high efficiency)

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31
Q

true or false: some enzymes are not proteins

A

true: one example is ribozymes (RNA molecule capable of acting as enzyme)

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32
Q

cofactor

A

non-protein molecules that assist enzymes in the reactions they manipulate

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33
Q

coenzymes

A

organic cofactors (usually include things like vitamins)

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34
Q

inorganic cofactors

A

tend to be metal ions like Fe2+ or Mg2+

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35
Q

Holoenzymes

A

refer to enzymes that are bound to their cofactor

36
Q

apoenzyme

A

enzyme not bound to its cofactor

37
Q

prosthetic groups

A

cofactors that tightly/covalently bind to their enzyme in a holoenzyme

38
Q

competitive inhibition

A

inhibitors compete with substrates for active sites

39
Q

true or false: we can outcompete a competitive inhibitor

A

true: as we increase the amount of substrate, there is a higher chance that the substrate can bind to the active site

40
Q

true or false: adding more substrate will continuously increase the speed of catalysis

A

false: this only occurs until all active sites are occupied (enzyme saturation). then catalysis plateaus

41
Q

noncompetitive inhibition:

A

when an inhibitor binds to the allosteric site of an enzyme (dif location that is not the active site)

42
Q

true or false: we can outcompete noncompetitive inhibitors

A

false: rate of enzyme catalysis is unaffected by increasing the substrate concentration

43
Q

velocity (V)

A

rate at which reaction is occurring

44
Q

Vmax

A

maximum reaction velocity

45
Q

Michaelis constant (Km)

A

the substrate conc at which Vmax is at 50%

46
Q

Small Km implies:

A

we only need a little bit of substrate bc enzyme ability/function is high

47
Q

Large Km implies:

A

that we need many substrates for reaction progression because enzyme availability/function is low

48
Q

If we add a competitive inhibitor:

A

Km increases while Vmax stays the same

49
Q

If we add a noncompetitive inhibitor:

A

Km stays the same while Vmax decreases

50
Q

Fat is also called

A

triacylglycerol or triglyceride

51
Q

triglycerides are found in:

A

adipocytes

52
Q

fats have __ unique parts which are:

A

2; glycerol backbone and 3 fatty acids

53
Q

glycerol structure

A

3 carbons and 3 hydroxyl groups

54
Q

fatty acid

A

long hydrocarbon tail attached to a carboxylic acid

55
Q

fats are produced by ____ reactions

A

dehydration/condensation (just like for carbs and proteins)

56
Q

fats have what kind of linkages?

A

ester

57
Q

true or false: many fats contains fatty acids that are of different lengths and degrees of unsaturation

A

true

58
Q

phospholipid structure

A

3-carbon glycerol backbone, 1 phosphate group, 2 fatty acid tails

59
Q

glycolipid

A

looks virtually the same as a phospholipid, however these contain a carbohydrate molecule in place of the phosphate group

60
Q

cholesterol makes up around __-__% of a eukaryotic cell membrane

A

30-50%

61
Q

cholesterol contains _ hydrocarbon rings

A

4

62
Q

true or false: cholesterol is hydrophobic

A

false: amphipathic

63
Q

which organ makes cholesterol?

A

liver (but we can also get it from the diet)

64
Q

Cholesterol is a starting material for:

A

steroid, vitamin D, bile acids

65
Q

how do lipids travel through blood?

A

in lipoproteins

66
Q

lipoproteins contain:

A

coat of phospholipids, cholesterol, proteins and a lipid core

67
Q

LDL

A

considered to be unhealthy because they deliver cholesterol to peripheral tissues via the bloodstream. (bad cholesterol)

68
Q

HDL

A

high density of proteins. They are generally considered to be healthy because they take cholesterol away from peripheral tissues and deliver it to the liver.

69
Q

Other lipid derivatives (3)

A
  1. waxes
  2. carotenoids
  3. sphingolipids
70
Q

Waxes

A

contain long fatty acids that are connected to monohydroxy alcohols by ester linkages., serve as hydrophobic protective coating

71
Q

carotenoids

A

long carbon chains that have conjugated double bonds and six-membered rings at each end, function as pigments that provide color to plants and animals

72
Q

carotenoid examples

A

carotenes and xanthophylls

73
Q

sphingolipids

A

have a sphingoid base backbone composed of a set of aliphatic (non-aromatic) amino alcohols. They serve as structural integrity, signal transduction and cell recognition

74
Q

sphingolipids examples

A

ceramides, sphingomyelin

75
Q

purines

A

adenine and guanine

76
Q

pyrimidines

A

cytosine, thymine, uracil

77
Q

purines have _ rings

A

2

78
Q

pyrimidine have how many rings?

A

1

79
Q

A-T has how many H bonds?

A

2

80
Q

G-C has how many H bonds?

A

3

81
Q

modern cell theory statements:

A
  1. all life is composed of one or more cells, where cells are the basic structural, functional, and organizational unit of life
  2. all cells come from pre-existing, living cells via cell division
  3. genetic information (stored within cells) to pass onto new cells
  4. organism’s activity is dependent on the activity of its independent cells
  5. metabolism and biochemistry (energy flow) occur within cells, where all cells have the same chemical composition.
82
Q

true or false: cell theory does not apply to viruses

A

true - viruses are not living cells

83
Q

central dogma

A

dna–> rna –> protein

84
Q

main implication of central dogma:

A

information cannot travel from protein to protein, or from proteins to nucleic acids

85
Q

true or false: information cannot travel from rna to dna

A

false: they can

86
Q

prions

A

example where info can travel from protein to protein. they are misfolded proteins that cause other proteins to misfold as well, destroying their function in the process

87
Q

RNA world hypothesis

A

Earth’s “primordial soup” had a lot of RNA nucleoside triphosphates, which made phosphodiester bonds with each other to create short strands of RNAs. As the strands grew longer and longer, they became more and more stable. continued to evolve until they could replicate

DAT Biology (27 decks)

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