Exam Review

Front 1

Define dehydration synthesis

Back 1

when 2 subunits get linked through removal of H2O

Front 2

what type of reaction is this

Does it form or break down macromolecules

Back 2

anabolic

forms

Front 3

Define hydrolysis rxn

Back 3

subunits break apart by adding H2O

Front 4

What are carbs?

Back 4

short term energy ce;;s

Front 5

what linkages are they joined by? What rxn produces this bond

Back 5

glycosidic linkages

condensation rxn

Front 6

Define monosaccharides

Back 6

simple sugar units

Front 7

what are the main three examples? (GFL)

Back 7

glucose

fructose

lactose

Front 8

describe glucose. fructose and lactose

Back 8

primary energy fuel of cell

found in fruit

found in milk

Front 9

what important sugar is also a monosaccharide which is used in our DNA?

Back 9

deoxyribose

Front 10

Define isomers

Back 10

chemically the same but structurally different

Front 11

what are the four main types of polysaccharides?

(SGCC)

Back 11

starch

glycogen

cellulose

chitin

Front 12

Describe starch

Back 12

energy storage in plants

Front 13

Describe glycogen

Back 13

energy storage in human

Front 14

cellulose

Back 14

structural components of plant cells

Front 15

chitin

Back 15

Makeup shell of anthropods

Front 16

Define what a lipid is?

Back 16

non-polar

Front 17

What are the main categories? (FaFPSW)

Back 17

fatty acids

fats

phospholipids

steroids waxes

Front 18

what is the roles of lipids

Back 18

energy

insulation

chemical messengers

Front 19

Define a fatty acid

Back 19

provide structure for most lipids

Front 20

how does the fatty acid look structurally

Back 20

hydrocarbon chain with carboxyl group

Front 21

Difference between saturated and unsaturated fatty acid

Back 21

saturated= single bond b/w C atoms making it straight hydrocarbon chains allowing more to fit together and more LDF

unsaturated= kink shape 1+ C=C

Front 22

Define fats

Back 22

fatty acid+glycerol joined by condensation rxn

Front 23

Define hydrogenation

Back 23

H atoms added to double bonds in unsaturated triacylglycerol

Front 24

Define phospholipid

Back 24

2 fatty acids+phosphate group

Front 25

Waxes

what is their role

Back 25

hydrophobic

waterproof coating keep feather dry form honeycombs

Front 26

Define steroids

Back 26

compact hydrophobic molecule with 4 hydrocarbon rings

Front 27

what is steroids not composed of

Back 27

fatty acids

Front 28

difference between fats and oils

Back 28

fats=hiher saturated fatty acids oils=higher unsaturated fatty acids

Front 29

what are good cholesterol and bad cholesterol called?

Back 29

good=HDL

bad=LDL

Front 30

define proteins

Back 30

made of many amino acids

genetic info of DNA code only for protein

Front 31

function of proteins

Back 31

enzyme

carriers

immunoglobulins

Front 32

what bonds hold proteins together and what are the monomers

Back 32

amino acids

peptide bond

Front 33

how are the peptide bonds formed?

Back 33

dehydration synthesis

Front 34

describe the primary secondary, tertiary and quaternary protein structures

Back 34

1=polypeptide chains

2=a-helix + b-pleated sheats

3=more folding

4=functional protein

Front 35

what model of the cellular membrane do we follow?

Back 35

fluid mosaic model

Front 36

what is passive transport?

Back 36

susbtance moves across membrane w/o energy

Front 37

diffusion

Back 37

high to low concentration

Front 38

what 4 factors determine rate of diffusion? (TSaToMCg)

Back 38

temp

surface area

type of molecule being diffused

steepness of [] gradient

Front 39

define transport proteins

Back 39

provides pathway for molecules to cross membrane

Front 40

what are the two types?

Back 40

channel

carrier

Front 41

define active transport

Back 41

against [] gradient using energy via pumps

Front 42

what are the three types of active transport?

Back 42

Protein pumps

endocytosis

exocytosis

Front 43

what is endocytosis used for and what are the two types

Back 43

large amounts

phagocytosis = large solid particles

pinocytosis=extracellular materia

Front 44

what does exocytosis do?

Back 44

remove material

Front 45

hypotonic soln and names in different cells

Back 45

lower [] of solute outside takes in H2O

AC=lysed

PC=turgid

Front 46

hypertonic soln and names in different cells

Back 46

higher [] outside so shrinks

AC=shrivels

PC=plazmolyzed

Front 47

isotonic

Back 47

equal []

ac=normal

pc=flaccid

Front 48

define a substrate

Back 48

reactant enzyme will act on

Front 49

where does the substrate bind? After binding what is created

Back 49

Active site

enzyme-substrate complex

Front 50

What are the two models of susbtrate binding?

Back 50

lock and key model

induced fit model

Front 51

describe lock and key model

Back 51

match substrate exactly

Front 52

induced fit model

Back 52

enzyme=changes to fit substrate

Front 53

what are the 4 factors affecting enzyme activity

Back 53

amount of substrate

enzyme []

temp

pH

Front 54

what are the two types of enzyme inhibition and how do they work?

Back 54

competitive: bind to active site

non-competitive bind at allosteric site changing shape

Front 55

how are enzymes regulated?

Back 55

allosteric

Front 56

what do activators do?

Back 56

bind allosterically controlled enzymes to stabalize shape

Front 57

allosteric inhibition

feedback inhibition

Back 57

stabilize inactive form of enzyme

rxns make common product which travels back and inhibits earlier enzyme

Front 58

Define oxidation and reduction

Back 58

LEO

GER

Front 59

reducing agent vs oxidizing agent

Back 59

reducing- loosing electrons

oxidizing-gaining

Front 60

ATP vs ADP

Back 60

adenosine triphosphate

adenosine diphosphate

Front 61

Phosphorylation

Back 61

rxn of ATP when coupled with endo rxn where Pi bonded to other molecule

Front 62

What makes up ATP?

Back 62

adenine

ribose

3 phosphate groups

Front 63

it is catalyzed by ATPase. What is the sig of this?

Back 63

aids in hydrolysis of Pi from atp

Front 64

what are the usuages (MTC)

Back 64

mechanical

terminal chemical

Front 65

how is glucose oxidized?

Back 65

substrate level phosphorylation

oxidative phosphorylation

Front 66

define substrate-level phosphorylation

Back 66

ATp forms directly in enzyme catalyzed rxn

Front 67

oxidative

Back 67

ATP forms indirectly thru series of redox rn with ) as final e- receptor

Front 68

where does glycolysis occur and what does it not require

Back 68

cytoplasm

oxygen

Front 69

what is the goal

Back 69

break glucose into pyruvate releasing ATP

Front 70

where does pyruvate oxidation occur?

Back 70

mitochondrion

Front 71

what are the parts to the mitochondrion

Back 71

matrix (inside)

intermembrane

Front 72

pyruvate oxidation

Back 72

aerobic

makes acetyl CoA

Front 73

Steps:

Back 73

1. carbonyl group removed= CO2 released

2. pyruvate=oxidized by NAD+ =NADH

3. Coenzyme A attaches to aceytl= Acetyl CoA

Front 74

How does ATP count affect the acetyl CoA

Back 74

atp=low then goes to Krebs Cycle

atp=high then fatty acids for energy storage

Front 75

Describe fermentation and what is the goal?

Back 75

b/c of O2 lack; anaerobic no ATP

regenerate NADH+

Front 76

Lactic Acid Fermentation

Back 76

when muscles use O2 faster than can be replenished. pyruvate stays in cytoplasm

Front 77

How many NADH oxidized to produce lactate

Back 77

2

Front 78

Alcohol Fermentation

Back 78

pyruvate converted to ethanol using 2 NADH

Front 79

Why is the Krebs Cycle called the Kreb Cycle?

Back 79

oxaloacetate product in step 8 and reactant in step 1

Front 80

how many acetyl-CoA enter and how many time does Krebs Cycle occur per glucose

Back 80

2

twice

Front 81

Steps

Back 81

acetyl-CoA +oxalacetate = citrate

NAD+ reduced to NADH

FAD reduced to FADH2

ATP= substrate level phosphorylation

CO2 released

Front 82

Describe the structure of electron transport chain and chemiosmosis

Back 82

e- acceptors embedded in inner mitochondrial membrane, arranged in increasing electronegativity

Front 83

weaker e- attractor

strongest

Back 83

NADH dehydrogenase

Oxygen

Front 84

What role do NADH and FADH2 play?

Back 84

transfer e- to proteins in inner mitochondrial membrane

Front 85

Chemiosmosis

Back 85

mvmnt of ions across semi-permeable membrane down electrochemical gradient

Front 86

what two processes occur in photosynthesis?

Back 86

light rxns

calvin cycle`

Front 87

what is the goal of Calvin Cycle?

Back 87

fix C to organic compounds for energy storage

Front 88

what are the three phases

Back 88

1. Carbon Fixation

2. reduction rxn

3. regeneration of RuBP

Front 89

what happens during carbon fixation

Back 89

3 RuBP +3CO2= 6 3-C molecules. attached by enzyme of rubisco

Front 90

reduction rxn

Back 90

3-C molecule+ATP+NADPH= 1 G3P leave cycle

Front 91

Regeneration of RuBP

Back 91

5G3P +3 ATP= 3 RuBP

Front 92

What is G3P

Back 92

sugar

Front 93

Describe rubisco

Back 93

slow enzyme

can attach to O2 and CO2

Front 94

Describe rubisco carboxylase

Back 94

CO2+RuBP= Calvin cycle

Front 95

describe rubisco oxygenase

Back 95

fixes O2= doesnt need product

Front 96

Photorespiration

Back 96

uses O2 releases CO2= decrease of output b/c no ATP

Front 97

What enzyme do C4 and CAM use

Back 97

Pep carboxylase

Front 98

Photosystem I

Photosystem ii

Back 98

thylakoid= chlorphyll P700

Chlorophyll P680

Front 99

What protein in photosystem II splits up H2O

Back 99

Z protein

Front 100

What is the first step of DNA Replication?

Back 100

DNA separates at replication origin

Front 101

what is the replication fork?

Back 101

y-shaped structure formed by 2 separating parent strands

Front 102

What are the challenges and solutions

Back 102

Tension= topoismerase enzymes cut and rejoin near replicaiton fork

Annealing= SSBs attach to end to stop rejoining

Front 103

what happens in the second step

Back 103

complementary strands are builtw

Front 104

what enzyme lays down what in order to signal the enzyme to start

Back 104

Primase lays down RNA primers for DNA polymerase

Front 105

What happens to the Okazaki fragments once copied

Back 105

joined by phosphodiester bonds by DNA ligase

Front 106

what is the final stage and what happens

Back 106

Proofread and Repair

DNA polymerase proofreads replicated strand

Front 107

Describe the initiation stage o f Transcription

Back 107

Initiation: RNA polymerase binds to helix at promoter region

Front 108

Elongation

Back 108

mRNA= synthesized as RNA polymerase moves along. then reaches termination sequence

Front 109

termination

Back 109

RNA polymerase recognizes the sequence and stops

Front 110

What three post-transcriptional modifications occur

Back 110

Capping: 5' cap added

Tail: Poly-A-Tail added to 3'

Spliceosomes=remove introns (non-coding regions) and join exons (coding regions)

Front 111

Describe the ribosome unit

Back 111

small and big subunit= intact ribosome which clamps mRNA

Front 112

Initiation

Back 112

begins at AUG at P site. 2nd codon in A site. tRNA delivers Amino Acid

Front 113

Elongation

Back 113

2nd tRNA enters A site, bringing 2nd AA forming peptide bonds. Ribosome moves over

Front 114

termination:

Back 114

continues until stop codon read

Front 115

release factor does what?

Back 115

recognize ribosome has stopped and releases the polypeptide chain

Front 116

Why do we have gene expression

Back 116

b/c not every protein is needed all the time

Front 117

house keeping genes vs specialized genes

Back 117

continuous

only when needed

Front 118

operons

Back 118

cluster of linked genes that function together and regulated by one promoter

Front 119

restriction enzyme

Back 119

cut DNA at recognition site= sticky sends or blunt ends

Front 120

methaylase

Back 120

needed for restriction enzyme to work

Front 121

plasmids

Back 121

circular pieces of DNA in bacteria. RE used to splice genes into plasmids

Front 122

Ectotherm vs endotherm

Back 122

activity regulated by environment

maintain constant body temperature

Front 123

osmoregulation

Back 123

balance of water ion [ ] in fluid