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Molecular Cell Biology Jessica > Chapter 2 > Flashcards

Chapter 2 Flashcards

1
Q

Water is polar or nonpolar?

A

polar

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2
Q

Ion and polar molecules are insoluble or soluble in water?

A

soluble. (they are hydrophillic) and water is polar so remember, like dissolves like

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3
Q

Do nonpolar molecules interact with water?

A

no they do not. they are poorly soluble because water is polar and nonpolar molecules are not easily dissolve/interact with water. Also nonpolar molecules are hydrophobic

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4
Q

What are some inorganic ions

A

Na^+, K^+, Mg^+2, Ca^+2, HPO4^2-,Cl^-,HCO3^- (ions)

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5
Q

What are the four classes of molecules?

A

carbohydrates, lipids, proteins, nucleic acids

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6
Q

what is a glycosidic bond?

A

this bond allows monosaccharides to be joined together by dehydration reactions (loss of water) and linkage of sugars

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7
Q

name two common polysaccharides that are composed entirely of glucose and molecules in alpha configuration

A

glycogen=storage of glucose in animal cells

starch= storage in plant cells

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8
Q

glycogen and amylopectin also contain alpha(1-6) bonds and they serve as____________

A

branch points

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9
Q

cellulose is the main structural component of what?

A

plant cell walls

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10
Q

what is cellulose composed of and in what configuration?

A

glucose molecules, B configuration

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11
Q

why does cellulose have B(1-4)linkages?

A

This linkage allows the chains to pack more tightly. This allows the cellulose to form long extended chains that pack side by side to form fibers of great mechanical strength

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12
Q

What are the 3 main rules of lipids?

A
  • energy storage
  • major component of cell membranes
  • important in cell signaling as steroid hormones and messenger molecules
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13
Q

define fatty acid

A

are long hydrocarbon chains (16-18 carbons) with a carboxyl group (COO-) at one end

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14
Q

define unsaturated fatty acids

A

have one or more double bonds. therefore it can not bond to as many hydrogens.

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15
Q

define saturated fatty acids

A

HAVE NO DOUBLE BONDS.

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16
Q

the hydrocarbon chain of a fatty acid is? hydrophobic or hydrophillic?

A

hydrophobic

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17
Q

name a saturated fatty acid

A

palmitate or stearate

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18
Q

name a unsaturated fatty acid

A

oleate

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19
Q

what are fatty acids stored as?

A

triacylglycerols

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20
Q

what is a triacylglycerol?

A

it is three fatty acids linked to a glycerol molecule

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21
Q

are triacylglycerol insoluble or soluble in water?

A

they are insoluble in water. this is why they can accumulate as fat droplets in the cytoplasm

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22
Q

why are fats more efficient energy storage than carbohydrates?

A

fats yield more than twice as much energy per weight of the material broken down

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23
Q

what is the principle component of the cell membranes?

A

phospholipids

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24
Q

what are phospholipids composed of?

A

2 fatty acids, joined to a polar head

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25
Q

When talking about the phospholipid.

The Hydrophobic tails are?
The Hydrophillic head is?

A

hydrophobic tails=hydrocarbon chains

hydrophillic head: phosphate group and polar attachment

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26
Q

What do you call a molecule that is part water-soluble and part water insoluble? give a example of such a molecule.

A

amphipathic molecules….

phospholipids are an example

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27
Q

glycerol phopholipids are composed of?

A

2 fatty acids bound to glycerol. bound to phophate group. which is bonded to another small polar molecule (choline, serine, inositol, ethanolamine)

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28
Q

how is sphingomyelin different then other phospholipids?

A

it is the only nonglycerol phospholipid. meaning the polar head group is formed from serine instead of glycerol

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29
Q

what is a glycolipid composed of?

A

two hydrocarbon chains and a carbohydrate polar head group

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30
Q

what is cholesterol composed of

A

four hydrophobic hydrocarbon rings and a polar hydroxyl (OH) group

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31
Q

the steriod hormones are derivatives of __________; that act as chemical messengers

A

cholesterol

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32
Q

what does DNA stand for?

A

deoxyribonucleic acid

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33
Q

what does RNA stand for?

A

ribonucleic acid

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34
Q

what does messenger RNA do?

A

carries information from DNA to the ribosomes

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35
Q

what does ribosomal RNA and transfer RNA do?

A

they are involve in protein synthesis.

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36
Q

still other _______ are involved in the regulation of gene expression and processing and transport of RNAs and protiens

A

other RNAS

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37
Q

DNA and RNA are polymers of ________ which consists of ___________- and _________ bases linked to a phosphorylated sugars

A

nucleotides
purine
pyrimidine

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38
Q

DNA has what two purines?

A

adenine and guanine

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39
Q

DNA has what two pyrimidines?

A

cytosine and thymine

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40
Q

RNA has what two purines?

A

adenine and guanine

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41
Q

RNA has what two pyrimidines?

A

cytosine and uracil

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42
Q

What do you call the sugar component in RNA?

A

ribose

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43
Q

what do you call the sugar component in DNA?

A

2’-deoxyribose

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44
Q

nucleoside + _____________= nucelotide

A

phosphate group

45
Q

a nucleoside is composed of what?

A

it is composed of a base, and a sugar……

addition of phosphate group turns nucleoside to nucleotide

46
Q

in nucleotides which carbon does the phosphate group link to

A

the 5th carbon of sugars

47
Q

what is a phosphodiester bond?

A

joins nucleotides

it is between the 5’ phospate of one nucleotide and the 3’ hydroxyl of another

48
Q

define oligonucleotides

A

are polymers of only a few nucleotides

49
Q

RNA and DNA are _________ and may contain thousands or even millions of nucleotides

A

polynucleotides

50
Q

what is connected to the 5’ carbon of the polynucleotide?

what is connected to the 3’ carbon of the polynucleotide?

A

phosphate group, hydroxyl group

51
Q

polynucleotides are always synthesized in what direction?

A

5’ to 3’ direction

52
Q

DNA is made up of two polynucleotide chains. how are the bases on the inside joined

A

hydrogen bonds

53
Q

what bases pair with the following:
Guanine
adenine

A

cytosine

thymine

54
Q

what are the most diverse of all molecules

A

protiens

55
Q

name five functions of protiens

A

structural components

transport and storage of small molecules

transmit information between cells (protein hormones)

defense against infection (antibodies)

enzymes

56
Q

proteins are polymers of how many amino acids

A

20

57
Q

when talking about an amino acid. what is connected to the alpha carbon?

A

side chain, amino group, carboxyl group, and hydrogen

58
Q

what are some basic amino acids

A

lysine, arginine, histidine

59
Q

what are some acidic amino acids

A

aspartic acid, glutamic acid

60
Q

amino acids are grouped based on characteristics of the side chains including properties such as (4)?

A

nonpolar side chains

polar side chains

side chains with charged basic groups

acidic side chains terminating in carboxyl groups

61
Q

amino acids are joined by what bonds?

A

peptide bonds

62
Q

define peptide bond

A

its how amino acids are joined

63
Q

define polypeptide

A

chains of amino acids, hundreds or thousands of amino acids in length

64
Q

one end of a polypeptide terminates in a ____ (N terminus) and the other in an ____________ (C terminus)

A

alpha amino group

alpha carboxyl group

65
Q

insulin consist of two

A

polypeptide chains

66
Q

the side chains of three pairs of cysteine residue are joined by ?

A

disulfide bonds

67
Q

the sequence of amino acids in a protein is determined by

A

order of nucleotides bases in a gene

68
Q

proteins also have distinct _____________________________ that are critical to their function

A

3- dimensional (3-d) conformations

69
Q

the shape and function of proteins is determined by their____________

A

amino acid sequences

70
Q

who demonstrated the importance of proteins 3- structure?

A

Christian Anfinsen

71
Q

Christian Anfinsen disrupted proteins by treatments such as heating, which breaks ______________

A

non-covalent bonds (denaturation)

72
Q

protein structure has what four levels

A

primary

secondary= alpha helix and beta sheet

tertiary

quaternary

73
Q

when talking about the secondary structure of a protein, both the alpha helix and beta sheet are held together by _________ between the ____________ groups of _________

A

hydrogen bonds

CO and NH

peptide bonds

74
Q

hemoglobin is composed of

A

four polypeptide chains

75
Q

what is the basic unit of a teritary structure (protien wise)

A

domains

76
Q

what is the fundamental properties of an enzyme?

A

increase rate of chemical reactions WITHOUT THEMSELVES BEING CONSUMED or permanently altered

increase reaction rates without altering the CHEMICAL EQUILIBRIUM between reactants and products

77
Q

When a _________ is converted to a __________ the chemical equilibrium between S and P is determined by the laws of thermodynamics

A

a substrate

a product

78
Q

equilibrium is determined by the

A

final energy states of S and P

79
Q

The substrate must be first converted to a higher energy state called?

A

transition state

80
Q

the energy required to reach transition state=

A

activation energy

81
Q

a fundamental rule of proteins is to __________

A

act as enzymes

82
Q

what are enzymes

A

they are catalysts that increase the rate of all chemical reactions in cells

83
Q

enxymes must bind to their substrate to form an?

A

enzyme-substrate complex (ES)

84
Q

define active site

A

this is where a substrate binds to a specific region of an enzyme

85
Q

specific side chains in the ____________ and form bonds with reaction intermediates

A

active site may react with the substrate

86
Q

chymotrypsin digest protiens by?

A

catalyzing the hydrolysis of peptide bonds

87
Q

chymotrypsin is a _______: these enzymes cleave peptide bonds adjacent to specific types of amine acids

A

a serine protease

88
Q

chymotrypsin

A

digests bonds adjacent to hydrophobic amino acids

89
Q

trypsin

A

digest bonds next to basic amino acids

90
Q

what are active sites

A

these are clefts or grooves on the surface of an enzyme formed by the tertiary structures

91
Q

substrates originally bond by

A

hydrogen bonds, ionic bonds, and hydrophobic interactions

92
Q

trypsin

A

digests bonds next to basic amino acids

93
Q

the active sites of serine proteases contain _____, _______, ______

A

serine,

histidine

aspartate

94
Q

substrates bind by insertion of the _________ adjacent to the cleavage site into a pocket at the active site

A

amino acid

95
Q

define lock and key model

A

the substrate fits precisely into the active site

96
Q

define induce fit (for enzyme related )

A

conformation of both enzyme and substrate is modified

97
Q

define coenzymes

A

small organic molecules that work together with enzymes to enhance reaction rates

THESE ARE NOT ALTERED BY REACTION

98
Q

what is nicotinamide adenine dinucleotide (NAD)

A

it is a coenzyme that carries electrons in oxidation-reduction reactions

99
Q

NAD can accept ______ and __ electrons from one substrate, forming NADH

A

H+ and two electrons

100
Q

NADH can then donate the _________ to a second substrate, re-forming NAD

A

electrons

101
Q

define prosthetic groups

A

small molecules bound to protiens that have critical functional roles

102
Q

feedback inhibition is a type of ?

A

allosteric regulation

103
Q

define allosteric regulation

A

enzyme activity is controlled by the binding of small molecules regulatory sites on an enzyme

104
Q

many coenzymes are closely realted to vitamins, which?

A

contribute part or all of the structure of the coenzyme

105
Q

phosphate groups are added to the side chain OH groups of ??????

A

serine, threonine, or tyrosine residues

106
Q

in feedback inhibition what happens?

A

the product of a metabolic pathway inhibits an enzyme involved in it synthesis

107
Q

if delta G <0, this reaction will proceed?

A

in the forward direction

108
Q

if delta G >0, this reaction will proceed?

A

in the reverse direction; B will be converted to A

Molecular Cell Biology Jessica (33 decks)

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