Molecular Biology Flashcards

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1
Q

polymer

macromolecule

A

large organic compound

contains repeating atom groups

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2
Q

4 types of polymers found in living organisms

A

carbohydrates

lipids

proteins

nucleic acids

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3
Q

monomer

A

small and repeating organic groups that covalently bond together

building blocks of polymers

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4
Q

defining characteristic of lipids

A

insolubility in water

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5
Q

structure of carbohydrates

A

contains carbonyl group

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6
Q

structure of fatty acid

A

contains carboxyl group

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7
Q

structure of amino acids

A

contains amino group and carboxyl group

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8
Q

structure of nucleotide

A

contains nitrogenous base, phosphate group, and pentose sugar

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9
Q

elements in carbohydrates

A

carbon

hydrogen

oxygen

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10
Q

elements in lipids

A

carbon

hydrogen

oxygen

sometimes phosphorus

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11
Q

elements in proteins

A

carbon

hydrogen

oxygen

nitrogen

sometimes sulfur

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12
Q

elements in nucleic acids

A

carbon

hydrogen

oxygen

nitrogen

phosphorus

sometimes sulfur

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13
Q

monomer of carbohydrates

A

saccharide

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14
Q

monomer of lipids

A

fatty acid

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15
Q

monomer of proteins

A

amino acid

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16
Q

monomer of nucleic acids

A

nucleotide

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17
Q

bond between monomers in carbohydrates

A

glucosidic link

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18
Q

bond between monomers in lipids

A

unnamed covalent bond

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19
Q

bond between monomers in nucleic acids

A

crosslink by 2 or 3 hydrogen bonds

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20
Q

process of formation of carbohydrates

A

condensation reaction between monosaccharides

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21
Q

process of formation of lipids

A

condensation reaction between fatty acids and glycerol

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22
Q

process of formation of proteins

A

condensation reaction between amino acids

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23
Q

process of separation of carbohydrates

A

hydrolysis reaction

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24
Q

process of separation of lipids

A

hydrolysis reaction

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25
Q

process of separation of proteins

A

hydrolysis reaction

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26
Q

condensation reaction

A

chemical reaction which forms water in process of combining 2 smaller molecules to form 1 larger molecule

used in formation of carbohydrates, lipids, and proteins

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27
Q

hydrolysis reaction

A

chemical reaction which uses water molecule to split 1 large molecule into smaller molecules

used in separation of carbohydrates, lipids, and proteins

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28
Q

metabolism

A

chemical reactions inside cells to release energy

sum of all reactions that occur in an organism

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29
Q

parts of metabolism

A

anabolism

catabolism

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30
Q

anabolism

A

reactions which build up larger molecules from smaller ones

requires energy (usually in form of ATP)

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31
Q

catabolism

A

reactions which break down larger molecules into smaller ones

releases energy (usually in form of ATP)

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32
Q

functions of carbohydrates

A

main fuel source for bodily functions

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33
Q

monosaccharide

A

simplest form of sugar

most basic unit of carbohydrate

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34
Q

disaccharide

A

carbohydrate composed of 2 monosaccharides bound together by glycosidic link

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35
Q

oligosaccharide

A

carbohydrate composed of​ relatively low number of monosaccharides bound together by glycosidic links

typically contains around 3 to 10 monosaccharides

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36
Q

polysaccharide

A

carbohydrate composed of more than 1 monosaccharide bound together by glycosidic links

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37
Q

α-glucose

alpha glucose

A

glucose molecule with downward-pointing hydroxide group

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38
Q

β-glucose

beta glucose

A

glucose molecule with upward-pointing hydroxide group

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39
Q

cellulose (and its structure)

A

polysaccharide formed by β-glucose molecules with alternating orientation

linked by first carbon atom to fourth carbon atom on separate β-glucose molecules

forms straight and unbranched chain

used to provide strength to cell walls of plants

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40
Q

starch (and its structure)

A

polysaccharide formed by α-glucose molecules with matching orientation

forms curved chain that can be branched or unbranched

used to store glucose in plants

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41
Q

glycogen (and its structure)

A

polysaccharide formed by α-glucose molecules with matching orientation

forms curved and branched chain

used to store glucose in humans

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42
Q

comparison of glucose and fructose

A
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43
Q

2 main types of lipids (and their differences)

A

fats (solid at room temperature)

oils (liquid at room temperature)

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44
Q

trygylceride

A

lipid composed of 3 fatty acids linked to 1 glycerol by an ester bond

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45
Q

length of hydrocarbon chain of fatty acids found in living organisms

A

usually between 14 and 20 carbon atoms

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46
Q

saturated fatty acid

A

fatty acid with single bonds between all carbon atoms

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47
Q

unsaturated fatty acid

A

fatty acid with at least 1 double bond in between its carbon atoms

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48
Q

monounsaturated fatty acid

A

fatty acid with 1 double bond in between its carbon atoms

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49
Q

polyunsaturated fatty acid

A

fatty acid with more than 1 double bond in between its carbon atoms

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50
Q

cis-fatty acid

A

unsaturated fatty acid with hydrogen atoms that are on the same side of double bond

forms a bent chain

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51
Q

trans-fatty acid

trans fat

A

unsaturated fatty acid with hydrogen atoms that are on different sides of double bond

forms a straight chain

artificially produced through partial hydrogenation of vegetable oils or fish oils

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52
Q

shape of cis-fatty acid

A

bent at the double bond

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53
Q

effect of shape of cis-fatty acid

A

bad at packing together in regular arrays

lower melting point

typically liquid at room temperature (oil)

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54
Q

shape of trans-fatty acid

A

straight

55
Q

effect of shape of trans-fatty acid

A

higher melting point

typically solid at room temperature (fat)

56
Q

functions of lipids

A

energy storage (as fats in animals and oils in plants)

thermal insulation

buoyancy

cell membrane structure

hormones and vitamins

57
Q

structure of steroids and cholesterol

A

formed by 4 fused carbon rings

58
Q

hydrogenated lipids

A

saturated fat formed by adding additional H2 molecule to an unsaturated fat

59
Q

location of hydrogen bonds in water

A
60
Q

significance of hydrogen bonds in water

A

gives water its unique properties

61
Q

properties of water caused by hydrogen bonding

A

cohesion

adhesion

capillary action

62
Q

cohesion

A

attraction of molecules of 1 kind to other molecules of the same kind

63
Q

adhesion

A

attraction of molecules of 1 kind to molecules of a different kind

64
Q

significance of cohesive properties of water

A

important for water transport in plants

determines surface tension of water

65
Q

significance of adhesive properties of water

A

responsible for cappilary action

important for water transport in plants

useful in leaves (where water adheres to cellulose molecules in cell walls)

66
Q

thermal properties of water

A

high specific heat capacity

high latent heat of vaporization

high boiling point

67
Q

latent heat of vaporization

enthalpy of vaporization

A

amount of energy that must be added to a liquid substance to transform a quantity of that substance into a gas

68
Q

cause of high specific heat capacity of water

A

motion of water molecules is restricted by hydrogen bonds and increased temperature is necessary to break hydrogen bonds

69
Q

cause of high latent heat of vaporization of water

A

motion of water molecules is restricted by hydrogen bonds and increased temperature is necessary to break hydrogen bonds

70
Q

cause of high boiling point of water

A

motion of water molecules is restricted by hydrogen bonds and increased temperature is necessary to break hydrogen bonds

71
Q

effect of high latent heat of vaporization of water

A

evaporation of water has a coolant effect because it requires so much heat

72
Q

cause of solvent properties of water

A

polar nature of water causes formation of shells around charged and polar molecules which prevents them from clumping together (and keeps them in solution)

73
Q

hydrophilic substance

A

substance which is chemically attracted to water

substance which is soluble in water

74
Q

type of molecules which are hydrophilic

A

polar molecules

particles with positive or negative charges

75
Q

hydrophobic substance

A

substance which is insoluble in water (although it may dissolve in other solvents)

76
Q

types of molecules which are hydrophobic

A

nonpolar molecules

particles without positive or negative charges

77
Q

polypeptide

A

chain of amino acids

linked together by condensation reactions on ribosomes through translation

main component of proteins (sometimes only component)

78
Q

oligopeptide

A

chain of fewer than 20 amino acids

79
Q

amount of amino acids used to make polypeptides

A

20

80
Q

part of amino acid which gives polypeptide its properties

A

functional group (“R group”)

81
Q

role of ribosomes in forming polypeptides

A

linking amino acids together (one-at-a-time)

making peptide bonds between any pair of amino acids

82
Q

possible number of sequences for polypeptide of n amino acids

A

10n

83
Q

storage of polypeptide sequence code

A

within base sequence of a gene (using genetic code)

requires 3 bases of gene per amino acid

84
Q

functions of collagen (and how)

A

structural (provide tensile strength in tendons, ligaments, skin, and blood vessel walls)

85
Q

functions of hemoglobin (and how)

A

transport (transports oxygen to tissues that need it)

86
Q

functions of ‘myosin and actin’ (and how)

A

movement (contraction of muscle fibers and movement in animals)

87
Q

functions of immunoglobin

A

defense (antibodies which fight bacteria and viruses)

88
Q

determination of conformation of protein

A

amino acid sequence of protein and constituent polypeptides

89
Q

fibrous proteins

A

proteins which are formed with an amino acid sequence that prevents folding up and ensures chain of amino acids remains in elongated form

90
Q

conformation of fibrous proteins

A

elongated

repeated structure

91
Q

solubility of fibrous proteins in water

A

insoluble in water

92
Q

functions of fibrous proteins

A

provide strength and support to tissues

93
Q

globular protein

A

proteins which are formed by folding of amino acids as they are added one-by-one

94
Q

conformation of globular proteins

A

have intricate shape

includes parts that are helical or sheet-like

95
Q

solubility of globular proteins in water

A

nearly soluble (forms colloids)

96
Q

functions of globular proteins

A

pigments

transportation of proteins

assist with immune system

97
Q

primary uses for proteins

A

catalysts

muscle contraction

cytoskeletons

tensile strengthening

blood clotting

transport of nutrients and gases

cell adhesion

membrane transport

hormones

receptors

packing of DNA

immunity

98
Q

biotechnical uses for proteins

A

enzymes for removing stains

monoclonal antibodies for pregnancy tests

insulin for treating diabetics

99
Q

genome

A

all of the genes of a cell, a tissue, or an organism

100
Q

proteome

A

all of the proteins produced by a cell, a tissue, or an organism

101
Q

variability of genome and proteome of organism (and why)

A

genome is fixed (because all cells in organism have same genes)

proteome is variable (because different cells in organism make different proteins)

102
Q

4 levels of protein structure

A

primary structure

secondary structure

tertiary structure

quaternary structure

103
Q

primary structure

primary structure of protein

A

number and order of amino acids in polypeptide

determined by genetics (not random)

read from amino terminal to carboxyl terminal

104
Q

secondary structure

secondary structure of protein

A

coils and folds of polypeptide which contribute to overall structure of protein

105
Q

α helix

alpha helix

A

right-hand helix conformation of polypeptides within secondary structure of protein

contains hydrogen bond at every 4th amino acid

106
Q

β pleated sheet

beta pleated sheet

A

side-by-side conformation of polypeptides within secondary structure of protein

connected by hydrogen bonds

107
Q

tertiary structure

tertiary structure of protein

A

3-dimensional conformation of folds within polypeptides

held together by hydrogen bonding, ionic bonds, and disulfide bridges

108
Q

quaternary structure

quaternary structure of proteins

A

overall structure of aggregated polypeptides into 1 fuctional macromolecule

109
Q

conjugated protein

A

protein which includes binding of prosthetic group

110
Q

denaturation

A

structural change in protein that results in loss of biological properties

111
Q

enzyme

A

globular protein (often with prosthetic groups)

often called “biological catalyst”

lowers activation energy and yields faster rates for biochemical reactions

unchanged by reactions which it speeds up

112
Q

catalyst

A

substance which speeds up chemical reactions

113
Q

suffix to molecule which signifies that it is an enzyme

A

“-ase”

114
Q

substrate

A

molecule upon which an enzyme acts

115
Q

general equation of enzyme-catalyzed reaction

A
116
Q

enzyme-substrate specificity

enzyme-substrate complex

A

ability of an enzyme to choose exact substrate from group of similar chemical molecules

117
Q

active site

A

region of enzyme where substrate molecules bind and undergo chemical reaction

118
Q

lock-and-key theory

A

explanation of enzyme-substrate specificity by considering an enzyme to be a lock and a substrate to be the key which fits perfectly within

older and over-simplified explanation of enzyme-substrate specificity

119
Q

induced fit theory

A

explanation of enzyme-substrate specificity

takes into account adaptability of shape of enzymes

120
Q

enzyme activity

A

catalysis of reaction by enzyme

121
Q

3 stages of enzyme activity

A

collision (binding of substrate or substrates to active site of enzyme)

occurrence of chemical reaction within active site

separation of products from active site

122
Q

factors which affect enzyme activity

A

temperature

pH

substrate concentration

123
Q

effects of temperature on enzyme activity

A

moderate increase in temperature causes increase in enzyme activity

excessive increase in temperature can cause denaturation of enzyme through destruction of bonds and structural changes to enzyme

124
Q

effect of pH on enzyme activity

A

activity of enzyme is highest at its pH optimum

125
Q

effect of substrate concentration on enzyme activity

A

increased substrate concentration causes increased enzyme activity (up to the point at which active site is occupied by maximum amount of substrate)

126
Q

immobilized enzymes

A

enzyme attached to an inert and insoluble material so that it may be held in place

seen frequently in commercial use

127
Q

advantages of enzyme immobilization

A

simple separation of enzyme and products so that chemical reaction can be stopped at ideal time

allows enzyme to be recycled after use

increased stability of enzymes to changes in pH

exposure of higher enzyme concentrations

128
Q

types of nucleic acids

A

ribonucleic acid (RNA)

deoxyribonucleic acid (DNA)

129
Q

functions of nucleic acids

A

determination of inherited characteristics of every living thing

carrying of information

directing of protein synthesis

130
Q

DNA

deoxyribonucleic acid

A

nucleic acid which stores all hereditary information of an animal

stores primary structures of proteins

131
Q

RNA

ribonucleic acid

A

nucleic acid which carries protein-coding instructions from DNA to ribosomes

132
Q

nitrogenous bases of DNA

A

adenine

guanine

thymine

cytosine

133
Q

types of nitrogenous bases in DNA

A

purines (adenine and guanine)

pyrimidines (thymine and cytosine)

134
Q

nitrogenous base pairs of DNA

A

adenine and thymine

guanine and cytosine