Cell Phys Final Exam

Front 1

The size of the cell should be measured in

Back 1

micrometers

Front 2

Prokaryotes have a nucleus and plasma membrane but do not

Back 2

have highly organized cytoplasm

Front 3

Hydrogen is

Back 3

the most abundent element in the body

Front 4

Ionic bond is a transfer of

Back 4

electrons

Front 5

The trade of nitrogenous base is

Back 5

DNA, thymine/ RNA, Uricil

Front 6

DNA double strands are held together by

Back 6

hydrogen bonds

Front 7

Amino acid side chains

Back 7

NH2 and COOH

Front 8

Sodium and Potassium

Back 8

Net charge of +1

Front 9

Glutamic acid can form ionic bonds

Back 9

because of its negative side chain

Front 10

The most important factor in reaction stability is

Back 10

shape and surface compatiability between the two molecules

Front 11

Fourth type of interaction between phospholipid bilayer

Back 11

hydrophobic interaction

Front 12

Chemical bonds store

Back 12

energy, used to generate biological molecules

Front 13

Heat

Back 13

increases disorder

Front 14

The nature of polar bonds is to

Back 14

unequally share electrons across a covalent bond

Front 15

The highest increase in standard free energy, delta G

Back 15

most favored

Front 16

Equilibrium constant

Back 16

k=x/y

Front 17

Enzymes

Back 17

lower the activation barrier that a reaction must overcome

Front 18

Hydrogen bonds are the backbone of

Back 18

A and B secondary folding

Front 19

Km

Back 19

respresents the enzyme and substrate binding affinity

Front 20

Vmax-Km

Back 20

represents the overall turnover number

Front 21

Glutamine

Back 21

produced by adding phosphate to glutamic acid

Front 22

Urea disrupts

Back 22

the hydrogen bond among water molecules

Front 23

Urea is used

Back 23

to denature proteins

Front 24

Protein domain is

Back 24

a protein segment that folds independently

Front 25

Unfolded proteins form

Back 25

protein aggregates

Front 26

Lowering the energy cost can also be termed

Back 26

decreasing the stability

Front 27

Lysozyme would be classified as

Back 27

a hydrolase

Front 28

hydrolase

Back 28

is a an enzyme that speeds up the catylase of proteins

Front 29

Lysozyme lowers the energy required for its substrate

Back 29

by distorting the substrate in a shape and speeding up the rate at which water molecules collide with the substrate

Front 30

Explaination for decrease in enzyme activity

Back 30

could be the absense of negative charges in the active site

Front 31

If an enzyme as two different pathways that are inhibited

Back 31

The spot of the pile up, the point where they cross will most likely be the spot for negative feedback

Front 32

Decrease in the rate of hydrolysis of GTP by Ras

Back 32

causes proliferation of the cell, cancer

Front 33

Ionic bond

Back 33

salt

Front 34

molecular bond

Back 34

molecule

Front 35

Molecules have a characteristic

Back 35

bond length

Front 36

Equal sharing of electrons

Back 36

non-polar

Front 37

Polar

Back 37

is unequal sharing

Front 38

Noncovalent bonds are

Back 38

weaker and critical for 3D shape

Front 39

Domain is

Back 39

modular unit from which many single-chain proteins are constructed

Front 40

Some proteins are composed of more than one

Back 40

subunit

Front 41

SH2 domain

Back 41

Phosphotyrosine

Front 42

SH3 domain

Back 42

Proline rich motifs such as RKXXPXXP and PXXPXPR

Front 43

FYVE domian

Back 43

PI3P

Front 44

PH domain

Back 44

Several Phospholipids

Front 45

Nuclease

Back 45

breaks down nucleic acids ny hydrolyzing bonds between nucleotides

Front 46

ATPase

Back 46

hydrolyze ATP

Front 47

Polymerase

Back 47

catalyzes the polymerization reaction, DNA and RNA synthesis

Front 48

Phosphatase

Back 48

Catalyzes the hydrolytic removal of phosphate group from the s molecule

Front 49

Hydrolase

Back 49

enzyme that catalyzes a hydrolytic clevage reation

Front 50

Protease

Back 50

breaks down proteins by hydrolyzing bonds between amino acids

Front 51

Kinase

Back 51

catalyze the addition of phosphate groups to molecules

Front 52

Syntease

Back 52

synthesize molecules in anabolic reaction via condensation

Front 53

Isomerase

Back 53

catalyze the rearrangement of bonds within a single molecule

Front 54

First protein structure solved in 1957

Back 54

myoglobin

Front 55

set of 20 amino acids can make

Back 55

160,000 combinations

Front 56

Heat effects enzyme reaction

Back 56

increased heat, increases the movement of molecules, with increase the kinetic energy

Front 57

Membrane lipids

Back 57

diffuse within the plane of the membranes

Front 58

Lipids with hydrocarbon tails that are shorter and have many double bonds

Back 58

are not effected much by temperature, tend to keep the same membrane fluidity

Front 59

New membrane pospholipids are on

Back 59

the cytosolic side of the endoplasmic reticulum

Front 60

Detergents

Back 60

purify a membrane protein

Front 61

The nuclear localization sequence

Back 61

bound by cytoplasmic proteins that direct the nuclear proteins to the nuclear pore

Front 62

Oligosaccharides are

Back 62

on the outside of the target cells, white blood cells example

Front 63

The deletion of proteins forming tight junctions

Back 63

would cause the redistribution of proteins around the entire cell

Front 64

FRAP

Back 64

Floresent Recovery after photo bleaching

Front 65

SPT

Back 65

single particle targeting

Front 66

The principle anion in the extracellular space that balances the sodium is

Back 66

Cl

Front 67

Out of glucose, water, gycerol, and ethanol

Back 67

glucose has the lowest rate of diffusion

Front 68

Proteases attacking transport proteins would result

Back 68

in the inability to import sugar into the cell

Front 69

Transporters

Back 69

bind and involve confrontational change

Front 70

K coupled

Back 70

is not a common active transport, Na ATP and light are however

Front 71

Ca pumps are important

Back 71

for preventing Ca from altering the activity of molecules in the cytosol

Front 72

Gated ion channels

Back 72

open more frequenctly in response to a given stimuli

Front 73

Na Open and

Back 73

resting membrane potential becomes more positive

Front 74

Voltage-gated ca channels are required

Back 74

for secreation of neurotransmitters in response to action potential

Front 75

Three cell types do not all express

Back 75

an acetylcholine receptor that belongs to the transmitter gated ion channel family

Front 76

Extracellular signal molecules that are hydrophobic

Back 76

must bind to a cell surface receptor so as to signal a target cell to change behavior

Front 77

Opening Cl channels prevents

Back 77

postsynaptic cells from firing an action potential in inhibitory nurotransmitters

Front 78

Protein kinases tranfers the

Back 78

terminal phosphate from ATP onto protein

Front 79

When a G protein is actived

Back 79

the alpha subunit exchanges its bound GDP for GTP

Front 80

Promoting uncontrolled cell proliferation a mutation that inactivates the protein tyrosine phosphatase

Back 80

that normally removes the phosphates from the tyrosine on the activated receptor

Front 81

Protein kinase can act as

Back 81

a signal integrating devise in signaling if it is activated by two or more proteins in different signaling pathways

Front 82

Inactivating an active RTK

Back 82

does not dephosphorylation by serine/threonine phosphatases

Front 83

PI 3 Kinase

Back 83

Phosphorylates a specific phospholipid in the membrane

Front 84

Brainy transcription

Back 84

a mutation in the gene that encodes cAMP phosphodiesterase that makes the enzyme inactive

Front 85

Most likely candidate to form a transmembrane region

Back 85

cannot contain R,T, and S, they are polar so would not be in a non polar region

Front 86

Addition of a drug that blocks portein Y from interacting with its target

Back 86

would turn off Ras downstream signal

Front 87

NO

Back 87

disolved extracellular gas

Front 88

Cytokine receptors associated with cytoplasmic tyrosine kinases call

Back 88

JAK

Front 89

Cytoplasmic transcriptional regulators

Back 89

STATs

Front 90

Proteins that posphralate each other

Back 90

example is MAP kinase

Front 91

DAG and IP3 are created by

Back 91

Phospholipase C cleaving the sugar phosphate head

Front 92

Membrane lipids are amphipathic

Back 92

which means it can have specialized functions determined by proteins

Front 93

Phospholipids

Back 93

are the most common lipids

Front 94

glycolipids

Back 94

are only on the outside of the cell

Front 95

Pholspholipid membrane proteins

Back 95

are in the membrane of the ER

Front 96

Proteins enter the nucleus

Back 96

unfolded

Front 97

Cytosol proteins do not contain

Back 97

sorting signals

Front 98

Proteins transported to the Golgi Apparatus buy

Back 98

transport vesicles

Front 99

ER tansport by

Back 99

protein transloctors, folded

Front 100

Clathrin

Back 100

forms a protein coat around vesicals

Front 101

Compact chromosomal segments

Back 101

heterochromosomal segement

Front 102

N-terminus for histones

Back 102

does not bind to DNA in a sequence specific manner

Front 103

Base pairs

Back 103

GC 3, AT 2

Front 104

Chromatin remodeling complex

Back 104

thrdrolysis move nucleosomes and slide

Front 105

Semi conservative

Back 105

each daughter DNA molecule consists of one strand from DNA molecule and one new strand

Front 106

Sliding clamp

Back 106

keeps the histone tight

Front 107

Repair DNA

Back 107

always repair the newly sythnesized

Front 108

A nick in the new strand

Back 108

makes for them to be prepared

Front 109

Deanimated

Back 109

C replaced by U

Front 110

Thymidine dimers

Back 110

do not covalently link across strands

Front 111

Transposase gene

Back 111

must be minimally carried on transponsons

Front 112

DNA and RNA are similar

Back 112

in that they run 5-3

Front 113

UTRs are not

Back 113

part of the introns

Front 114

The transcription of a eukaryotic gene can be influenced by

Back 114

additional porteins that bind for from the promoter that may affect the gene expression as a response to the cell signaling

Front 115

the sigma subunit

Back 115

recognizes promoter consensus in the DNA

Front 116

Ribosomes do not bind to the

Back 116

mRNA before it is exported

Front 117

The genetic code

Back 117

is redundant

Front 118

Anti codon CUU

Back 118

carries Lysine, GAA translated, must be read backwards

Front 119

rRNA is the catalytic component

Back 119

of the ribosome that joins amino acids together

Front 120

Ribosomes binding to the mRNA require

Back 120

a specific DNA sequence

Front 121

Regulates the amount of protein

Back 121

gene trascription efficiency, ribosomes can bind to a single mRNA molecule, proteins can be tagged for degradation

Front 122

Ribosymes

Back 122

RNA spicing

Front 123

Gene expression

Back 123

mostly transcription

Front 124

Mediator is not involved in

Back 124

post-transcriptional control

Front 125

The Lac repressor

Back 125

does not bind when lactose is present in the cell

Front 126

When tryptophan is available to the bacteria

Back 126

the Trp operon gets turned off because the repressor bound to trp will bind to the operator region

Front 127

Riboswitches

Back 127

self reguling mRNA to change it conformation

Front 128

Histone acetylse attach an acetyl group

Back 128

to selected lysine amino acid to the tail of histone proteins

Front 129

Cytocine

Back 129

only one that can DNA methylation