Mcat Exam Krackers Biology Ch.1

Front 1

cohesive forces from hydrogen bonds push ____ molecules away from water and cause them to aggregate

Back 1

hydrophobic

Front 2

why do hydrophilic molecules dissolve easily in water

Back 2

b/c their negatively charged ends attract the positively charged hydrogen bonds of water and their positively charged ends attract the negatively charged oxygen of water so water molecules surround (solvate) hydrophilic molecules separating them from the group

Front 3

6 groups of lipids

Back 3

fatty acids, triacylglycerols, phospholipids, glycolipids, steroids, and terpenes

Front 4

fatty acids are made of

Back 4

carbon-carbon bonds (usually an even number) with a carboxylic acid at the end

Front 5

max number of carbons in fatty acids in humans

Back 5

24

Front 6

what are triacylglyerols (or triglycerides) are made of (2)

function: (3)

Back 6

3 carbon backbone called glycerol that is attached to 3 fatty acids; store energy, thermal insulation, padding

Front 7

Adipocytes are made of

Back 7

triglycerides

Front 8

what are phospholipids made of (2)

-what is the polar part

-what is the nonpolar part

Back 8

a glycerol backbone, but a polar phosphate group replaces one of the fatty acids; phosphate group; fatty acid end

Front 9

amphipathic:

Back 9

a molecule that has both a hydrophobic and hydrophilic end

Front 10

glycolipids are made of:

-where are they found

Back 10

1 or more carbohydrate attached to the 3 carbon glycerol backbone instead of the phosphate group; in membranes of myelinated cells composing the nervous system

Front 11

what are the amphipathic fatty acids:

Back 11

phospholipids, glycolipids

Front 12

what are steroids made of:

-where are they found

Back 12

4 ringed structures; hormones, vitamin D, and cholesterol

Front 13

where are terpenes found?

Back 13

vitamin A (for vision)

Front 14

what is this

Back 14

phospholipid

Front 15

what is this?

Back 15

fatty acid

Front 16

what is this

Back 16

triacylglyceride/triglyceride

Front 17

what is this

Back 17

glycolipids

Front 18

what are these

Back 18

terpenes

Front 19

what transports lipids throught blood

Back 19

lipoproteins

Front 20

what are lipoproteins made of (2)

Back 20

lipid core surrounded by phospholipids

Front 21

3 types of lipoproteins

Back 21

VLDL: very low density lipoproteins, LDL: low density lipoproteins, HDL: high density lipoproteins

Front 22

what are the acidic amino acids (2)

Back 22

aspartic acid and glutamic acid

Front 23

what are the basic amino acids (3)

Back 23

lysine, arginine, histidine

Front 24

how many essential amino acids are there? what are they?

Back 24

10; valine , arginine, lysine, leucine, isoleucine, phenylalanine, tryptophan, threonine, methionine, histidine,

Front 25

5 forces that create the tertiary structure

Back 25

covalent disulfide bonds b/t 2 cysteines, electrostatic (ionic) interactions mostly b/t acids and bases, hydrogen bonds, van der waals forces, and hydrophobic side chains

Front 26

when are quaternary structures formed

Back 26

2 or more polypeptide chains that bind together

Front 27

what protein structure can't be denatured

Back 27

primary structure

Front 28

what are the types of proteins (2)

Back 28

globular and structural

Front 29

function of globular proteins:

Back 29

enzymes, hormones, membrane pumps and channels, receptors, hemoglobin and myoglobin, immune responses (antibodies)

Front 30

function of structural proteins

Back 30

maintain and add strength to cellular and matrix structures ex. collagen, microtubules

Front 31

glycoproteins:

where are they found

Back 31

proteins with a carbohydrate group attached; plasma membranes

Front 32

proteoglycans:

Back 32

mix of carbohydrates and proteins

Front 33

cytochromes:

ex.

Back 33

proteins that require a prosthetic heme group in order to function; hemoglobin

Front 34

structure of glycogen

Back 34

branched glucose polymer with alpha linkages' alpha 1,4 linkage

Front 35

structure of alpha anomer in ring.

-beta anomer structure

Back 35

carbon 1 OH is opposite of methoxy group on carbon 5; carbon 1 OH is on the same side of the methoxy group on carbon 5

Front 36

cellulose structure

Back 36

beta 1,4 linkage

Front 37

types of nucleotides

Back 37

DNA, RNA, nucleic acid, atp, cyclic amp, nadh, and fadh2

Front 38

a nucleoside has no

Back 38

phosphate group

Front 39

function of minerals (3)

Back 39

create an electrochemical gradient across membranes or solidify and give strength to a matrix, act as cofactors ex iron in heme

Front 40

the lock and key theory and induced fit theory are an example of ___

Back 40

enzyme specificity

Front 41

saturation kinetics:

Back 41

as concentration of substrate increases the rate of the reaction also increases but to a lesser and lesser degree until Vmax is reached due to as more substrate is added individual substrates have to wait in line for a free enzyme

Front 42

turnover number:

Back 42

number of substrate molecules one enzyme active site can convert to a product in a given unit of time when an enzyme solution is saturated with substrate

Front 43

Michaelis constant (Km):

-does Km vary when the enzyme concentration is changed

Back 43

substrate concentration at which the reaction rate is equal to 1/2Vmax; no

Front 44

cofactor:

Back 44

non-protein component that helps enzyme

Front 45

2 types of coenzymes:

Back 45

cosubstrates and prosthetic groups

Front 46

cosubstrates:

ex:

Back 46

reversibly bind to a specific enzymes and transfer some chemical group to another substrate and the cosubstrate is converted back to its original form by another enzymatic reaction; ATP

Front 47

prosthetic groups:

ex:

Back 47

remain covalently bound to the enzyme throughout the reaction; heme bind with catalase to break down hydrogen peroxide

Front 48

apoenzyme:

Back 48

an enzyme without its cofactor (is nonfunctional)

Front 49

haloenzyme:

Back 49

an enzyme with its cofactor

Front 50

irreversible inhibitors:

ex:

Back 50

agents that bind covalently to enzymes and disrupt their function; penicillin

Front 51

competitive inhibitors raise the __and don't change the ___

Back 51

Km; Vmax

Front 52

how do you reach the Vmax with a competitive inhibitor

Back 52

increase the substrate concentration

Front 53

noncompetitive inhibitors:

they lower the ___ and ___ stays the same

Back 53

bind noncovalently to an enzyme at a spot other than the active site (allosteric site) and change the conformation of the enzyme; Vmax (alters the enzyme so substrate can't bind properly); Km (don't lower enzyme affinity for the substrate)

Front 54

4 ways enzymes are regulated

Back 54

1. proteolytic cleavage

2. reversible covalent modification

3. control proteins

4. allosteric interactions

Front 55

proteolytic cleavage

ex:

Back 55

enzymes can be released in zymogen or proenzyme forms that are cleaved and become activated; pepsinogen to pepsin by low pH

Front 56

reversible covalent modification:

Back 56

enzymes can be activated or deactivated by phosphorylation or other types of modification

Front 57

control proteins:

ex (2):

Back 57

proteins that activate or inhibit enzyme function; G proteins, calmodulin

Front 58

allosteric interactions/enzymes:

Back 58

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

Front 59

positive cooperativity:

Back 59

If the change in shape of the first subunit makes easier the binding of substrate to the second subunit

Front 60

negative cooperativity:

Back 60

binding of a molecule to the first subunit makes more difficult the binding of substrate to the second

Front 61

aerobic:

anaerobibc:

Back 61

with oxygen; without oxygen

Front 62

steps of metabolism (3)

Back 62

macromolecules are broken down to their constituent parts releasing mild to no energy

2. constituent parts are oxidized to acetyl CoA, pyruvate and other metabolites (no oxygen used)

3. if oxygen is available, metabolites go into the citric acid cycle and oxidative phosphorylation

(steps 2 and 3 are called respiration)

Front 63

___ is the 1st step of aerobic and anaerobic respiration

Back 63

glycolysis

Front 64

where does glycolysis occur?

Back 64

cytosol of cells

Front 65

pyruvate and NADH pass via ____ diffusion into the mitochondria through a ____

Back 65

faciliated; porin

Front 66

pyruvate is converted to ___ once in the matrix of the mitochondria

-what are the byproducts

Back 66

acetyl CoA; NADH and CO2

Front 67

Back 67

...

Front 68

acetyl CoA:

Back 68

coenzyme who's function it is to bring the acetyl group to the krebs cycle

Front 69

where does the krebs cycle take place?

Back 69

in the matrix of the mitochondria

Front 70

krebs cycle produces (3)

-what is lost (1)

Back 70

1 ATP, 3 NADH, and 1 FADH2; 2 carbons as CO2

Front 71

Back 71

...

Front 72

Back 72

....

Front 73

process of ATP production in the krebs cycle is called ___

Back 73

substrate level phosphorylation

Front 74

where are amino acids deaminated?

-what is the product?

Back 74

liver; ammonia which is then converted to urea

Front 75

where does the electron transport chain take place

Back 75

inner membrane of the mitochondria

Front 76

how much ATP does NADH produce ? FADH2? during the electon transport chain

Back 76

3; 2

Front 77

types of enzymes (6)

mnemonic: LI'L HOT

Back 77

oxidoreductase, transferases, hydrolases, lyases, isomerases, ligases

Front 78

oxidoreductases:

-usually are accompanied by a ____

ex (3)

Back 78

catalyze oxidation-reduction rxns by transferring electrons b/t molecules; a cofactor like NAD+ or NADP+; dehydrogenases, oxidase or reductase

Front 79

reductant:

oxidant:

Back 79

electron donor in rxn catalyzed by a oxidoreductase enzyme; electron acceptor

Front 80

transferases:

-ex

Back 80

catalyze the movement of a functional group from one molecule to another; kinases (transfer phosphate)

Front 81

hydrolases:

-ex (4)

Back 81

catalyze the breaking of a compound into 2 molecules using the addition of water; phosphatase (cleaves phosphates), peptidase(break down protein), nuclease(nucleic acid), lipase(lipids)

Front 82

lyases:

Back 82

catalyze the cleavage of a single molecule into 2 products

Front 83

synthase:

Back 83

a lyase the catalyzes the formation of 1 molecule from 2 smaller molecules

Front 84

isomerase:

Back 84

catalyze the rearrangement of bond w/in a molecule

Front 85

ligases:

-require

Back 85

catalyze the addition or synthesis rxn b/t large similar molecules

Front 86

vitamins 2 classes:

Back 86

fat and water soluble

Front 87

water soluble vitamins:

Back 87

B, C

Front 88

fat soluble vitamins:

Back 88

A, D, E ,K

Front 89

velocity equation of enzyme substrate rxn

Back 89

v = vmax[S]/Km + [S]

Front 90

hill's coefficient:

- > 1 =

- < 1 =

- = 1 =

Back 90

value indicates the nature of the cooperativity; ; positive cooperativity; negative cooperativity; enzyme doesn't have cooperative binding

Front 91

mixed inhibition:

-where do they bind?

-what changes? what doesn't?

Back 91

inhibitor can bind to either the enzyme or the enzyme-substrate complex; at the allosteric site; decreases Vmax, if inhibitor binds to enzyme it increases Km (lower afinity), if inhibitor binds to eynzme-substrate complex it decreases Km (increase affinity)

Front 92

uncompetitive inhibitor:

where does it bind?

-what changes? what doesn't?

Back 92

bind only to the enzyme-substrate and lock the substrate in the enzyme preventing its release (increases affinity b/t enzyme and substrate);allosteric site; lower Km (increase affinity) and lowers Vmax

Front 93

irreversible inhibition:

Back 93

active site is made unavailable for a long period of time or enzyme is permanently altered;

Front 94

kcat equation:

Back 94

kcat = Vmax/[E]