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chp 1 biological chem DAT Flashcards

CHP 1 - foundations of bio

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1
Q

what is matter ?

A

anything that takes up space and has mass

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2
Q

what is an element ?

A

a pure substance that takes up space and has mass

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3
Q

what is an atom ?

A

the smallest unit of matter

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4
Q

what is a molecule ?

A

2 or more atoms join together

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5
Q

what are the 2 forces for molecule attraction ?

A

intermolecular and intramolecular

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6
Q

what is intermolecular ?

A

the force BETWEEN molecules

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7
Q

what is intramolecular ?

A

the force WITHIN a molecule

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8
Q

what are monomers ?

A

a single molecule with ability to polymerize

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9
Q

what is polymerization ?

A

a process where monomers chemically combine to make a chain which the chain is then called polymers.

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10
Q

what are polymers ?

A

substances made of many monomers linked together

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11
Q

what 2 reactions govern polymerization ?

A

dehydration and hydrolysis

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12
Q

what is dehydration?

A

also called CONDENSATION - it takes a small monomers subunits , puts them together while releasing water molecule.

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13
Q

what is hydrolysis ?

A

also called DEPOLYMERIZATION- uses water to break bonds. so water is used

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14
Q

CARBS -

A
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15
Q

what are carbs ?

A

carbohydrates are used for both fuel and structural support

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16
Q

what are carbs composed of ?

A

carbon , hydrogen, oxygen

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17
Q

what are the types of carbs ?

A

mono , di , poly

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18
Q

shape for carbs ?

A

rings

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19
Q

what is a monosaccharide ?

A

the simplest type of carb

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20
Q

what are common mono carbs ?

A

glucose, fructose , ribose

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21
Q

what are disaccharides ?

A

made of 2 monosaccharides that are joined by a glycosidic bond.

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22
Q

what is reaction is required for glycosidic bond ?

A

dehydration reaction.

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23
Q

what are common disaccharides?

A

glucose and fructose = sucrose

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24
Q

what group forms a glycosidic bond ?

A

hydroxyl groups- they are main elements in carb composition therefore making them ready to be linked = glycosidic bond

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25
Q

what are polysaccharides ?

A

multiple monosaccharides together in a long polymer held by a glycolic bond

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26
Q

what are types of polysaccharides ?

A

-starch ; energy storage in plants and help with cell wall.
-glycogen ; energy storage in animals ( this can be hydrolyzed, resulting in glucose and then used as energy.
-cellulose ; structural support , made of many glucose monomers. ( cell wall )

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27
Q

PROTEINS-

A
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28
Q

what are proteins?

A

the building blocks of proteins are amino acids

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29
Q

what are amino acids composed of ?

A

carbon, hydrogen, oxygen and nitrogen

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30
Q

what is the basic structure of amino acids?

A

R group, carboxyl group ( COOH) and Amino group (NH2)

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31
Q

what are polypeptides ?

A

a polymer that is made of amino acids

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32
Q

what holds together polypeptides ?

A

peptide bonds

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33
Q

how are peptide bonds created ?

A

by dehydration reactions, and broken down by hydrolysis.

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34
Q

what are the protein levels ?

A

primary, secondary , tertiary, quaternary

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35
Q

what is the primary Level?

A

the simplest sequence of amino acids that is resulted from mRNA translation.

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36
Q

what Is the secondary level?

A

this is where alpha helices and beta sheets are formed.

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37
Q

what is the tertiary level?

A

this is the 3D structure that is formed by the R group interactions.

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38
Q

what interactions are used to hold these structures ?

A

3 types - hydrophobic, disulfide and additional tertiary interactions.

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39
Q

what is hydrophobic interactions?

A

afraid of water - so these interactions will be counting on non polar R groups

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40
Q

what are disulfide bonds ?

A

covalent bonds between 3 sulfide atoms

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41
Q

what are additional tertiary interactions?

A

hydro and ionic interactions between R groups.

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42
Q

what is the quaternary structure ?

A

multiple tertiary structures together

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43
Q

what are conjugated proteins?

A

they are protein made of amino acids and non protein components

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44
Q

what are metalloproteins?

A

proteins that contain a metal cofactor

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45
Q

example of metalloprotein ?

A

hemoglobin ; this is a molecule responsible for carrying oxygen throughout the blood within RBCs- the iron in Hg is the cofactor , its bound to the Hg protein that allows for interaction in the oxygen.

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46
Q

what are glycoproteins?

A

these are protons that have a carb group

47
Q

what is protein denaturing ?

A

when a protein has loss its function and higher order structure

48
Q

what are factors of protein denaturing ?

A

temp , Ph , salt concentrations

49
Q

what are some functions of proteins?

A

storage
hormones - signaling molecule
receptos - binding to signaling molecule
structure - strength
immunity- anitbody
enzymes - regulating rate of chem reaction

50
Q

ENZYMES -

A
51
Q

what Is a catalyst ?

A

it is a substance that INCREASES the reaction rate by DECREASING activation energy

52
Q

how do catalyst work ?

A

you can reach the transition state WITHOUT a catalyst but it will require HIGH amount of energy, WITH a catalyst you can reach transition state with less energy

53
Q

what does a catalyst not do ?

A

it DOES NOT shift the equilibrium or alter spontaneity

54
Q

what do catalyst do ?

A

increase reaction rate and decrease activation energy

55
Q

how do enzymes facilitate catalytic activity ?

A

by having an active site

56
Q

what is an active site ?

A

it is where and enzyme can receive material (substrate) and start reaction

57
Q

what is specificity constant?

A

measuring enzyme binding efficiency for substrate

58
Q

what are some theories for enzymes ?

A

induced fit theory - this expresses that the active site molds to favor the substrate binding
lock and key theory - this is outdated , this is where the active site of enzyme fits perfectly ( indicating that is is very selective)

59
Q

can enzymes denature ?

A

yes , due to temp and ph

60
Q

what are some common enzymes ?

A

phosphatase - cleavage of phosphate groups ( dephosporylate by using water to remove P )

phosphorylase - directly ADDS P group ti substrate

kinase - indirectly adds a phospho group to sub. this is because kinase doesn’t have a P group attached instead it will use a molecule that has a P

61
Q

what are some NON PROTEIN enzymes ?

A

ribozymes - RNA molecules that are able to act as enzymes.

cofactor - non protein molecules that help enzyme function.

coenzymes - organic and inorganic molecule (vitamin, metals ..)

62
Q

what is a holoenzyme ?

A

complex formed when enzyme binds to cofactor

63
Q

what Is apoenzyme ?

A

enzyme without a cofactor

64
Q

prosthetic groups ?

A

tightly/covanlent bond to enzyme

65
Q

what affects a enzyme reaction rates ?

A

if a molecule either than the desired one bind to the active site or allosteric site

66
Q

what is an active site ?

A

it is a receipt region that is specific for desired reaction

67
Q

what is an allosteric site ?

A

separate region on the enzyme that is not the active site but substrate is still able to bind

68
Q

what are types of enzyme inhibition ?

A

competitive and non competitive

69
Q

what is competitive ?

A

it is when there is direct competition for the active site - this is inhibitor vs sub. This can cause the reaction rate to decrease due to the inhibitor using the active site.
- this can be solved by increasing the substrate concentration. This way the inhibitor will be diluted and overcome.

70
Q

what is non competitive ?

A

this is where the inhibitor bind to the allosteric site. They are giving the sub to the active site. ThIs leads to a change in the active site which results in decreased rate reaction. this cant be solved

71
Q

what is uninhibited ?

A

enzyme and sub at active site = success

72
Q

what is Michaelis constant ?

A

this is the sub concentration required to reach half of the Max velocity

73
Q

how does this relate to affinity ?

A

km has an inversely relationship to the enzyme sub biting strength

74
Q

what is the desired result for km ?

A

if an enzyme can get to 1/2 V max with the smallest amount go sub available = affinity would be strong

75
Q

HIGH km -

A

more sub is required to get to 1/2 v max

76
Q

LOW km -

A

less sub is required to get to 1/2 v max

77
Q

Km in a competitive inhibitor -

A

km will increase but vmax has no change (km increases because we need more sub but since we can dilute inhibitor Vmax is the same)

78
Q

Km in a non com inhibitor -

A

vmax is decreased but km doesnt change (if less enzymes available vmax will decrease - km is the same because affinity is not manipulated )

79
Q

what is feedback ?

A

feedback describes how the product of reaction affects the rate of reaction

80
Q

neg feedback -

A

reaction products will slow/ inhibit reaction

81
Q

pos feedback -

A

reaction products will activate/ increase reaction

82
Q

LIPIDS -

A
83
Q

what are lipids ?

A

Lipids are fatty, waxy, or oily compounds that are soluble in organic solvents and insoluble in polar solvents such as water

84
Q

what are the components of lipids ?

A

carbon, hydrogen, oxygen

85
Q

what are fatty acids ?

A

Fatty acids can be defined as carboxylic acids with long aliphatic chains

86
Q

what are saturated fatty acids ?

A

hydrocarbon chains WITHOUT double bonds ( all carbons in the can are full with hydrogens ) = TIGHT

87
Q

what are unsaturated fatty acids ?

A

hydrocarbon chain with a double bond. = LESS TIGHT

88
Q

what are triglycerides ?

A

triglycerides or triaglycerol is a lipid containing glycerol backbone and 3 fatty acids (most triglycerides are hydrophobic and nonpolar )

89
Q

what is glycerol backbone?

A

has 3 carbons that serve as anchors for the fatty acid chains.

90
Q

what are phospholipids?

A

composed of a glycerol backbone , 1 phosphate group, and 2 fatty act tails.

91
Q

amphiphatic

A

has both hydrophilic and hydrophobic regions

92
Q

Lipid subtypes

A

waxes, carotenoid , lipoproteins and cholesterol

93
Q

what factors affect the fluidity of the membrane?

A

temp, cholesterol, degree of fatty acid unsaturation

94
Q

cholesterol

A

its an amphipathic lipid. it maintains stability in both low and high temps. precursor to steroid hormones, vitamin D and bile acids.

95
Q

lipoproteins

A

complex of lipids and proteins that caryry lipophilic (hydrophobic) molecules through the blood. Their coat is composed of phospholipids, cholesterol and proteins

96
Q

waxes and carotenoids

A

-waxes are simple lipids with long fatty acids chains connected to alcohols.
-carotenoids are lipid derivatives containing long carbon chains and conjugated double bonds that function ad pigment ( yellow , red and orange )
-sphingolipid are lipids with backbone containing aliphatic amino acids,
-glycolipids are lipids found in plasma membranes w carbs groups rather than phospho.

97
Q

NUCLEIC ACIDS-

A
98
Q

what are nucleic acids ?

A

they are composed of sugar monomers. they store genetic information, transfer molecules and gene silencing.

99
Q

what are the 2 main types of nucleic acids?

A

DNA and RNA

100
Q

what is a nucleoside ?

A

made of 1 ribose or deoxy sugar and 1 nitro base

101
Q

what is a nucleotide ?

A

made of 1 ribose or deoxy , 1 nitro base and a phospho group.

102
Q

RNA composition ?

A

ribose sugar with OH groups on 2’ and 3’

103
Q

DNA composition ?

A

ANTIPARALLEL double helix, has deoxyribose and OH on 3’ and H on 2’

104
Q

what is the sugar phosphate bone ?

A

it is how nucleic acids support themselves. it is a structural chain of alternating sugar and phosphates held together by phosphodiester bonds.

105
Q

what are the terminal ends ?

A

3’ OH and 2’ p group

106
Q

what is nucleic acid polymerization ?

A

it is when nucleic acids elongate as nucleoside triphosphate continue to be added to the 3’ OH group

107
Q

what are the types of RNA ?

A

mRNA-messenger
tRNA-transfer
rRNA-ribosomal
miRNA-micro
dsRNA -double strand

108
Q

mRNA-messenger

A

these result from DNA transcription. contains info to create proteins

109
Q

tRNA-transfer

A

protein synthesis by carrying AA to ribosomes

110
Q

rRNA-ribosomal

A

protein synthesis by complexing with proteins ti make ribosomes that read mRNA

111
Q

miRNA-micro

A

silencing gene expression. they go the opposite direction. disrupts info passage and shuts down expression

112
Q

dsRNA -double strand

A

genetic info reservoir , used by viruses

113
Q
A

biological chem DAT (12 decks)

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