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MCAT Biology > Chapter 1 > Flashcards

Chapter 1 Flashcards

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1
Q

hydrolysis

A

how most macromolecules are broken apart

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2
Q

dehydration

A

how most molecules are formed

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3
Q

lipid

A

any biological molecule that has low solubility in water and high solubility in nonpolar organic solvents

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4
Q

6 types of lipids

A

fatty acids, triacyglyceroles, phosopholipids, glycolipids, steroids and terpenes

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5
Q

fatty acids

A

long chains of carbons, COOH at the end

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6
Q

saturated fatty acids

A

contain only single carbon-carbon bonds

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7
Q

unsaturated fatty acids

A

1 or more C-C double bonds

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8
Q

fatty acid oxidation

A

liberates large amounts of chemical energy for a cell

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9
Q

fats reach cells as

A

fatty acids

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10
Q

triacylglyercols/triglycerides

A

3 Carbon backbone called glycerol, which is attached to 3 fatty acids

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11
Q

adipocytes

A

(fat cells), specialized cells whose cytoplasm contains almost nothing but triglycerides

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12
Q

phospholipids

A

glycerol backone, polar phospate group replaces one one of the fatty acid – phosphate group at the opposite side of the glycerol

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13
Q

amphipathic

A

one end polar, one end non polar

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14
Q

glycolipids

A

1 or more carbohydrates attached to the 3 carbon glycerol backbone

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15
Q

steroids

A

4 ringed structures

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16
Q

terpenes

A

vitamin A

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17
Q

lipoproteins

A

how lipids are transported in the blood, have a hydrophobic core and a hydrophilic shell

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18
Q

proteins/poly peptides

A

chain of aminoacids, linked together by peptide bonds

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19
Q

essential amino acids

A

cannot be produced in the body (10 of them)

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20
Q

digested proteins

A

reach cells as single amino acids

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21
Q

primary structure

A

and sequences of amino acids in a polypeptide

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22
Q

alpha helix

A

single chain of AA twist itself into

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23
Q

beta pleated sheet

A

AA chains lie along itself, lie parallel or antiparalled

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24
Q

secondary structure

A

alpha helix and beta sheets, contribute to the conformation of the protein, reinforced by hydrogen bonds between the carbonyl oxygen and the hydrogen on the amino group

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25
Q

teritary structure

A

3D shape formed when peptide chain curls and folds

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26
Q

5 forces that contribute to teritary structure

A

covalent disulfide bonds, electrostatic interaction, hydrogen bonds, van der Waals forces, hydrophobic side chains

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27
Q

quaternary structure

A

2 or more polypeptides bound together

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28
Q

proline

A

induces ftursn in the polypeptide disrupt both alpha helix and beta pleated sheet formation

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29
Q

denatured

A

when protein conformation is disrupted

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30
Q

globular proteins

A

enzymes, hormones, membrane pumps and channels, membrane receptors, osmotic regulators, intra and intercellular transport and storage

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31
Q

structural proteins

A

maintain and add strength to cellular and matrix structure

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32
Q

glycoproteins

A

proteins with carb groups attached

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33
Q

see nitrogen

A

think protein

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34
Q

cytochromes

A

proteins that require a prosthetic heme group in order to function

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35
Q

carbohydrates

A

made from carbon and water

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36
Q

six carbon carbohydrate

A

glucose

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37
Q

glucose

A

essentilaly all digested carbs reaching body cells have been converted to ____ by the the liver or enterocyes

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38
Q

alpha glucose

A

hydroxyl group on the anomeric carbon and the methoxy group are on opposite sides of the ring

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39
Q

beta glucose

A

hydroxyl group and methoxy group are on the same side of the carbon ring

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40
Q

enough ATP glucose is polymerized to the polysaccharide

A

glycogen or converted to fat

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41
Q

glycogen

A

found in all animal cells, large amounts in muscle and liver cells

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42
Q

liver cells

A

capable of reforming glucose from glycogen and releasing back into blood stream

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43
Q

cells capable of absorbing glucose against concentration gradient

A

certain epithelial cells in the digestive tract and the proximal tubule of the kidney (done via secondary active transport)

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44
Q

how cells absorb glucose

A

facilitated diffusion

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45
Q

without insulin only ____ and ___ are capable of absorbing sufficient amounts of glucose via facilitated transport system

A

neural and hepatic cells

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46
Q

plants form __ and ___ from glucose

A

starch and cellulose

47
Q

types of startch

A

amylose and amylopectin

48
Q

amylose

A

isomer of cellulose that may be ranched or unbranched, same alpha linkages as glycogen

49
Q

amylopectin

A

resembles glycogen has a different branching structure

50
Q

cellulose

A

beta linkages

51
Q

most animals

A

only have enzymes to digest alpha linkages of starch and glycogen

52
Q

nucleotides

A

5 carbon sugar, nitrogenous base, phosphate group

53
Q

polymers of nucleotides

A

nucleic acids – DNA and RNA

54
Q

nucleotides joined together by

A

phosphodiester bonds btwn phosphate group of one nucleotide and 3rd carbon of the pentose of the other nucleotide forming long strands

55
Q

nucleotides written

A

5’ –> 3’

56
Q

DNA

A

two strands joined together by hydrogen bonds to make double helix

57
Q

2 h bonds

A

adenine and thymine

58
Q

3 h bonds

A

cytosine and guanine

59
Q

DNA is written

A

top strand – 5’ –> 3’ ; bottom strand 3’ –> 5’

60
Q

RNA

A

single strand, uracil replace thymine

61
Q

important nucleotides

A

ATP, cyclic AMP, NADH, FADH2

62
Q

minearls

A

dissolved inorganic ions inside and outside the cell, assist transport of substances entering and exiting cells by creating electrochemical gradient, also act as cofactors

63
Q

enzymes

A

globular proteins, act as catalyst, don’t change eq of a reaction

64
Q

substrates

A

reactants upon which an enzymes works

65
Q

active site

A

position on the enzymes where substrate binds

66
Q

enzyme-substrate complex

A

enzyme bound to substrate

67
Q

enzyme specificity

A

enzymes only work on a specific substrate or group of closely related substrates

68
Q

lock and key theory

A

active site of the enzyme (lock) has a specific shape that only fits a specific substrate (key)

69
Q

induced fit

A

shape of enzyme and substrate altered upon binding

70
Q

saturation kinetics

A

relative concentration, rate of rxn increases, to a lesser and lesser degree until Vmax is reached

71
Q

Vmax

A

proportional to enzyme concentration,

72
Q

Km

A

substrate concentration at which rxn rate = to 1/2 Vmax, doesn’t vary when enzyme concentration is changed

73
Q

temperature and pH and enzymes

A

optimal temp == 37 C , optimal pH depends on enzyme eg – pepsin below 2, trypsin works best between 6 and 7

74
Q

cofactor

A

non protein component that many enzymes need to reach optimal activity, coenzymes or metal ions

75
Q

coenzymes

A

vitamins or their derivatives

76
Q

irreversible inhibitors

A

bind covalently to enzymes and disrupt their function, toxic

77
Q

competitive inhibitors

A

bind reversibly with covalent bonds to the active site, raise Km don’t change Vmax

78
Q

noncompetitive inhibitors

A

bind non-covalently to an enzyme at a spot other than the active site, change the conformation of the enzymes, don’t resemble substrate, commonly act on more than one enzyme, lower Vmax, Km is the same

79
Q

inactive form of an enzyme

A

zymogen or proenzyme, when specific peptide bonds are cleaved – irreversibly activated

80
Q

allosteric interactions

A

modification of the enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme

81
Q

negative feedback / feedback inhibition

A

product downstream in a rxn comes back and inhibits enzymatic activity in an early reaction, shut down mechanism

82
Q

positive feedback

A

product returns to activate the enzyme

83
Q

allosteric regulation

A

feedback inhibitors bind to an enzyme and cause conformational change

84
Q

allosteric inhibitors and activators

A

both exist, alter Km w/o changing Vmax

85
Q

positive cooperativity

A

first substrate changes the shape of the enzymes allowing other substrates to bind more easily

86
Q

negative cooperativity

A

occurs as well

87
Q

enzymes

A

“-ase”

88
Q

lyases

A

catalyzes the addition of one substrate to a double bond of a second substrate

89
Q

ligase

A

require energy from ATP

90
Q

kinase

A

phosphorylates something

91
Q

phosphotates

A

dephosphorylates something

92
Q

metabolism

A

all cellular chemical reactions

93
Q

respiration

A

energy acquiring stages

94
Q

anaerobic respiration

A

respiration where oxygen is not required

95
Q

glycolysis

A

glucose broken down into 2 3C molecules of pyruvate, 2 net molecules of ATP, 2 molecules of NADH, occurs in the cytosol

96
Q

substrate level phosphorlyation

A

formation of ATP from ADP and inorganic phosphate using the energy released from the decay of high energy phosphorylated compounds as opposed to using the energy from diffusion

97
Q

fermentation

A

anaerobic respiration, glycolysis, reduction of pyruvate to ethanol or lactic acid and oxidation of NADH back to NAD+

98
Q

aerobic respiration

A

requires oxygen

99
Q

products of glycolysis

A

move into matrix of a mitochondria, pyruvate and NADH pass via facilitated diffusion

100
Q

inner mitochondrial matrix

A

less permeable, pyruvates moves in via facilitated diffusion, NADH require hydrolysis of ATP to move in

101
Q

inside matrix pyruvate becomes

A

acetyl CoA, rxn produces NADH and CO2

102
Q

Krebs Cycle

A

each turn produces 1 ATP, 3 NADH and 1 FADH2

103
Q

ATP Production occurs via

A

substrate level phosphylation

104
Q

metabolism of fats

A

fatty acids converted into acyl CoA, brougth into matrix, acetly CoA produced, produces FADH2 and NADH for every 2 C of the original fatty acid

105
Q

metabolism of proteins

A

AA deminated in liver, this product is converted to pyruvic acid or acetyl CoA or it may enter Krebs cycle at various stages

106
Q

Electron transport chains

A

proteins in the inner membrane of mitochondria

107
Q

1st protein complex

A

oxidizes NADH by accepting its high energy electron, electrons passed down series

108
Q

Electrons passed down

A

ultimately accepted by oxygen to form water,

109
Q

proton motive force

A

protons are pumped into intermembrane space for each NADH as electrons are passed along,

110
Q

ATP synthases

A

protons propelled through this to produce ATP

111
Q

Oxidative phosphorylation

A

uses energy released by the oxidation of products to create ATP

112
Q

pH of intermembrane space

A

lower than that of the matrix

113
Q

glucose + oxygen

A

carbon dioxide and water, combustion reaction

114
Q

Amount of ATP Made in total

A

36 ATP

MCAT Biology (7 decks)

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