Cell And Molecular Biology Exam 1

Front 1

name the 4 most abundant elements in the human body

Back 1

Nitrogen
Carbon
oxygen
hydrogen

Front 2

List the essential elements other than N,C,O & F.

Back 2

Sodium (Na)
Potassium (K)
Magnesium (Mg)
Calcium (Ca)
Phosphorus (P)
Sulfur (S)
Chlorine (Cl)

Front 3

Atomic weight?

Back 3

protons + neutrons

Front 4

Term for atoms tendency to establish completely full outer energy levels?

Back 4

Octet Rule

Front 5

sharing electrons between atoms forms _______ ?

Back 5

Covalent bonds

Front 6

strongest bond?

Back 6

Covalent

Front 7

Bond formed by the transferring of electrons?

Back 7

Ionic bonds

Front 8

Bond due to molecular polarity?

Back 8

Hydrogen bonds

Front 9

a force due to fluctuating electrical charges?

Back 9

Van der Waals Attraction

Includes :dipole-induced dipole,
induced dipole-induced dipole.
and
dipole-dipole

Front 10

term for the repulsion force from water?

Back 10

hydrophobic forces

Front 11

forces that are weak in water, but in the absence of water are very strong (as in salt).

Back 11

Electrostatic attraction

Front 12

functional group name for OH

Back 12

Hydroxyl

Front 13

functional group name for O=C

Back 13

Carbonyl

Front 14

functional group name for
O=C-OH

Back 14

Carboxyl

Front 15

functional group name for
H-N-H

Back 15

Amino

Front 16

functional group name for
O
O-P-O
O

Back 16

phosphate

Front 17

functional group name for
S-H

Back 17

Sulfhydryl

Front 18

functional group name for
H
H-C-H

Back 18

Pyruvate

Front 19

How do Ketones differ from aldehydes?

Back 19

In ketones the carbonyl (C=O) is placed between two carbons rather than at the end of a carbon skeleton (with a Hydrogen)

Front 20

functional group that features a carbonyl group (C=O) bonded in between two other carbon atoms?

Back 20

Ketone
eg: acetone is most common

Front 21

Functional group in which a carbonyl group is bonded between the end of a carbon skeleton and a hydrogen.

Back 21

Aldehyde

*many fragrances are aldehydes.

Front 22

term for adding a phosphate to a substrate-

Back 22

Phosphorylation

Front 23

Term for adding a carboxyl group to substrate?

Back 23

Carboxylation

Front 24

Term for removal of carboxyl?

Back 24

De- carboxylation

Front 25

Term for removal of a hydrogen from substrate?

Back 25

De- hydrogenation

Front 26

Term for removal of amino group from substrate?

Back 26

De-amination

Front 27

4 Major types of macromolecules in cells?

Back 27

1. polysaccharides
2. fats/lipids
3. proteins
4. nucleic acids

Front 28

Monosaccharide containing an aldehyde group?

Back 28

Aldose
Eg: glucose

Front 29

Monosaccharide containing a ketone group?

Back 29

ketose
Eg: fructose

Front 30

similarity and difference between fructose and glucose?

Back 30

both are 6 carbon sugars

Different STRUCTURES:
Fructose is in the ketose group (contains C=O)
Glucose is in the Aldose group (contains H-C=O)

Front 31

Term for isomers in which the geometrical positioning of atoms and functional groups in space differs- MIRROR IMAGES

Back 31

Optic isomers
or
Stereoisomers

Front 32

Term for isomers in which the atoms and functional groups are joined together in different ways

Back 32

Structural isomers

Front 33

Configuration when OH group is on the same side as carbon 6?

Back 33

Beta Configuration

Front 34

Configuration when OH group is on the opposite side of carbon 6?

Back 34

Alpha configuration

Front 35

define condensation.

Back 35

A water molecule is released and two monosaccharides become one polysaccharides.

Front 36

define hydrolysis.

Back 36

a water molecule is added to a polysaccharide resulting in 2 monosaccharides.

Front 37

Term for when a water molecule is added to a polysaccharide resulting in 2 monosaccharides.

Back 37

hydrolysis

Front 38

what is a sugar derivative?

Back 38

When a hydroxyl group of a simple Monosaccharide is replaced by a different group.

Front 39

sugar derivative that is the building block of chitin?

Back 39

Acetylglucosamine

Front 40

sugar derivative with a amine group on carbon #2?

Back 40

glucosamine

Front 41

sugar derivative with a carboxyl group?

Back 41

glucuronic acid

Front 42

disaccharide with 2 glucoses?

Back 42

Maltose

Front 43

Disaccharide with 1 glucose and 1 galactose?

Back 43

lactose

Front 44

disaccharide with 1 glucose and 1 fructose?

Back 44

sucrose

Front 45

saccharide with 30-50 sugars?

Back 45

oligosaccharide

Front 46

saccharide with over 50 sugars?

Back 46

Polysaccharide

Front 47

polymer of glucose used in energy storage in animals?

Back 47

glycogen

(starch in plants)

Front 48

polymer of glucose used in energy storage in plants?

Back 48

starch

(glycogen in animals)

Front 49

in the cell walls of plants.
an unbranched polymer of glucose used for structre and other things.

Back 49

Cellulose

Front 50

glycogen, starch and cellulose are all examples of what kind of sugars?

Back 50

POLYSACCHARIDES.

Front 51

a large molecule (macromolecule) composed of repeating structural units with covalent bonds

Back 51

polymer

Front 52

This polymer of glucoronic acid and acytlglucoamine is a structural component of cartilage.

Back 52

Chondroitin sulfate
(part of proteoglycan)

Front 53

This polysaccharide of glucose enhances WHITE blood cell function.

Back 53

Glucan
(the mushrooms!....beta glucan used against tumor cells!)

Front 54

carbohydrates in the human body are stored in the _____.

Back 54

liver

Front 55

a protein "decorated" with oligosaccharide. ?

Back 55

glycoprotein

Front 56

function of glycoprotein?

Back 56

-regulates white blood cell extravasation (leakage)
-cell surface proteins for immune response (ID!)
-cell-cell interactions
structural, etc.

Front 57

polysaccharides "Decorated" with protein?

Back 57

Proteoglycans

Front 58

Function of Proteoglycans?

Back 58

mostly structural

Front 59

lipids with a carbohydrate attached?

Back 59

glycolipids

Front 60

function of glycolipids?

Back 60

component of cell membrane
energy
cellular recognition

Front 61

1 meter ^-9?

Back 61

nanometer (nm)

Front 62

1 Liter ^ -6?

Back 62

microliter (μL)

Front 63

which is the preferred light microscope for microbiology which shows the image in 3D?

Back 63

interference contrast microscope

Front 64

how would you describe the image displayed by a Bright Field Optics microscope?

Back 64

grey, low contrast, 2D, light microscope (vs electron microscope)

Front 65

which light microscope shows a highly contrasted 2D image?

Back 65

Phase Contrast Optics Microscope

Front 66

what is the maximum resolution for a light microscope?

Back 66

0.2 μm

Front 67

What is the maximum resolution for an electron microscope?

Back 67

0.002 μm
*this is one hundred times more precise than a light microscope!

Front 68

What are the 2 types of electron microscopes and their corresponding resolutions?

Back 68

Transmission (TEM): resolution .002 μm in 2D
Scanning (SEM): resolution 0.02 - 0.003 μm in 3D

*These use LASER light!

Front 69

What is the central dogma of microbiology?

Back 69

Transcription and translation!

Front 70

What are the macromolecules in microbiology and their corresponding "building blocks"?

Back 70

1. Polysaccharides made of sugars.
2. Fats/Lipids/Membranes made of fatty acids.
3. Proteins made of amino acids.
4. Nucleic acids made of nucleotides.

Front 71

what are the basic shapes of prokaryotic cells?

Back 71

spherical, rod shaped and spiral.

Front 72

proteins outside the cell which support the cell and are crucial to it's survival.

Back 72

Extracellular matrix

Front 73

Which element has a unique atomic weight and why?

Back 73

Hydrogen...weight of only 1 because it has no neutron!

Front 74

the INNER (cytosolic) membrane of the lipid bilayer contains this important phospholipid......

Back 74

PhosphatidyLINOSITOL

Front 75

the OUTER membrane of the lipid bilayer contains this important phospholipid......

Back 75

PhosphatidylCHOLINE

Front 76

This enzyme helps transfer phospholipids to the other half of bilayer to balance cell membrane...

Back 76

flippase

*It FLIPS!

Front 77

chemical property of having a hydrophyllic carboxylic head and a hydrophobic hydrocarbon tail?

Back 77

amphipathy
(or having both polar and non-polar properties)

Front 78

the hydrophyllic head of a phospholipid is made of _____.

Back 78

polar group, such as choline or inositol
and a phosphate

Front 79

a fat in which all covalent bonds are used up by hydrogens?

Back 79

saturated

Front 80

a fat in which there are fewer hydrogens, causing the molecule to kink?

Back 80

unsaturated

Front 81

basic structure of a lipid?

Back 81

fatty acids (hydrocarbon chain)
+
glycerol backbone

Front 82

Isoprenoid

Back 82

lipids with multiples of isoprene in the form of (C5H8)n

Front 83

What are 2 examples of molecules made from isoprene (a lipid) units?

Back 83

Steroids
&
Terpene (eg. vitamin A)

Front 84

lipid derivative with a carbohydrate attached?

Back 84

glycolipids

Front 85

a fat soluble enzyme which digests, transports and processes stored lipids for use within the body?

Back 85

lipase

Front 86

what are the 4 main biological functions of lipids?

Back 86

1. Structure of membranes
2. energy storage
3. essential vitamins (A, D, E & K)
4. Cell signaling

Front 87

fats vs carbs: kcal per gram?

Back 87

carbs: 4 kcal
fats: 9 kcal

Front 88

where are vitamins A,D,E,& K stored?

Back 88

liver, fatty tissues

Front 89

4 fat soluble vitamins that are isoprene based?

Back 89

A,D,E & K
(stored in liver and fatty tissues)

Front 90

3 components of a phospholipid?

Back 90

1. Hydrophyllic head: polar group (like choline on outer or Inositol on inner) + phosphate
2. Linker: glycerol
3. Hydrophobic tail: fatty acids

Front 91

how thick is the lipid bilayer?

Back 91

5 nm

Front 92

Surface of cell membrane is____.

Back 92

fluid.

lateral diffusion, flexion, rotation, and flip-

Front 93

Where are phospholipids synthesized?

Back 93

endoplasmic reticulum

* Then new phospholipids are added to the cytosolic side of cell membrane.

Front 94

what effect does cholesterol have on a cell membrane?

Back 94

stiffens it.

Front 95

what are the 4 main types of membrane proteins?

Back 95

1. transporters
2. anchors
3. receptors
4. enzymes

Front 96

function of transporter proteins in membrane?
(example)

Back 96

Eg: Na+ pump
pumps sodium out and potassium in.

Front 97

function of anchor proteins in membrane?

(example)

Back 97

eg. integrins
link intracellular actin filaments to extracellular matrix

Front 98

function of receptor proteins in membrane?

Back 98

transmit growth signals
(for example, by binding an extracellular molecule)

Front 99

function of enzyme proteins in membrane?

Back 99

eg. use extracellular signal to begin production of intracellular molecules

Front 100

membrane proteins with oligosaccarides?

Back 100

glycoproteins

Front 101

membrane proteins with polysaccharides?

Back 101

proteoglycans

Front 102

The meshwork of fibrous proteins attached to the CYTOSOLIC surface of the membrane?

Back 102

Cell cortex

Front 103

the major component of the cell cortex.
Long thin flexible rod proteins about 10 nm long.

Back 103

Spectrin

Front 104

How are membrane proteins arranged within the cell membrane??

Back 104

locally confined, forming functionally specialized regions

Front 105

in what ways do cells create membrane domains (4)

Back 105

cell cortex
extra-cellular marix
proteins of another cell
diffusion barrier (tight junction)

Front 106

What do we call the tight junction that cells form?

Back 106

diffusion barrier

Front 107

How are intestinal epithelial cells unique?

Back 107

they forms distinct apical and baso-lateral membrane domains.

Front 108

what are small amphipathic molecules called?

Back 108

detergents

Front 109

what are the two most common detergents we need to know?

Back 109

SDS (sodium dodecyl sulfate, but call it SDS)
and
Triton X-100 (number indicates strength)

Front 110

basic structure of an amino acid?

Back 110

4 parts:
-amino (NH)
-Alpha Carbon attached to side chain (aka R group) (and a hydrogen on the other side)
-Carboxyl (C=O)

R
I
-N-C-C-
I . I . II
H-H-O

Front 111

what is an R group?

Back 111

side chain of an amino acid

Front 112

dehydration forms
___________ to link amino acids.

Back 112

peptide bonds

Front 113

what are the types of bonds that give proteins their 3D structure? (5)

Back 113

1. ionic bonds(between CHARGED amino acids)
2. Hydrogen (with N or O or NH)
3. Van der Waals
4. hydrophobic (attract other hydrophobic)
5. covalent (between sulfurs)

Front 114

a covalent bond between 2 sulfurs in protein structure?

Back 114

disulfide bridge

Front 115

levels of protein structure:
the amino acid sequences.

Back 115

primary structure

Front 116

levels of protein structure:
alpha helix or beta sheet

Back 116

secondary structure

Front 117

levels of protein structure:
combination of alpha helices and beta sheets (eg. a-b-a)

Back 117

motif
(a motif of secondary structures)

Front 118

levels of protein structure:
final folded shape of a polypeptide (protein unit)

Back 118

tertiary structure

Front 119

levels of protein structure:
a combination of multiple protein units.

Back 119

quaternary structure

Front 120

a segment of a polypeptide chain (protein) which forms a compact stable structure and ysually carries out a function. (usually enzymatic)

Back 120

Domain

Front 121

another word for a polypeptide chain?

Back 121

protein

Front 122

amino acid represented by
D

Back 122

Aspartic Acid
Asp
negative side chain

Front 123

amino acid represented by
E

Back 123

Glutamic Acid
Glu
negative sidechain

Front 124

amino acid represented by
R

Back 124

Arginine
Arg
positive side chain

Front 125

amino acid represented by
K

Back 125

Lysine
Lys
positive side chain

Front 126

amino acid represented by
H

Back 126

Histidine
His
positive side chain

Front 127

amino acid represented by
N

Back 127

Asparagine
Asn
Uncharged polar side chain

Front 128

amino acid represented by
Q

Back 128

Glutamine
Gln
Uncharged polar side chain

Front 129

amino acid represented by
S

Back 129

Serine
Ser
Uncharged polar side chain

Front 130

amino acid represented by
T

Back 130

Threonine
Thr
Uncharged polar side chain

Front 131

amino acid represented by
Y

Back 131

Tyrosine
Tyr
Uncharged polar side chain

Front 132

amino acid represented by
A

Back 132

Alanine
Ala
nonpolar side chain

Front 133

amino acid represented by
G

Back 133

Glycine
Gly
nonpolar side chain

Front 134

amino acid represented by
V

Back 134

Valine
Val
nonpolar side chain

Front 135

amino acid represented by
L

Back 135

Leucine
L
nonpolar side chain

Front 136

amino acid represented by
I

Back 136

Isoleocine
Ile
nonpolar side chain

Front 137

amino acid represented by
P

Back 137

Proline
Pro
nonpolar side chain

Front 138

amino acid represented by
F

Back 138

Phenylalanine
Phe
nonpolar side chain

Front 139

amino acid represented by
M

Back 139

Methionine
Met
nonpolar side chain

Front 140

amino acid represented by
W

Back 140

Tryptophan
Trp
nonpolar side chain

Front 141

amino acid represented by
C

Back 141

Cysteine
Cys
nonpolar side chain

Front 142

Amino acids with negative side chains?

Back 142

Asparitic acid/ asp/ D
Glutamic acid / Glu/ E

DE acids.

Front 143

Amino acids with positive side chains?

Back 143

Arginine /Arg /R
Lysine/ Lys/ K
Histidine/ His/ H

Front 144

amino letters which don't make sense...

Back 144

Dasp (-)
gluE (-)
Rarg (+)
lysK (+)
asnN
Ytyr
Wtrp
Qgln

Front 145

differences between negative "acids" and the uncharged polar abbreviations for
aspartic acid vs asparagine
and
glutamic acid vs glutamine

Back 145

acids: first 3 letters (asp, glu)
uncharged polar: first 2 letters +n.(asn, gln)

*Asn, Gln, Ile (Isoleocine) & Trp (tryptophan) are the ONLY abbreviations that don't start with the first 3 letters!

Front 146

How many nonpolar side chains?

Back 146

10...that's half.

Front 147

how many uncharged polar side chains?

Back 147

5... a quarter of them.

Front 148

How many basic and acidic side chains?

Back 148

3 basic (Arg, Lys & His)

2 acidic (Asp & Glu)

Front 149

C. elegans:
sexes and ratio of sexes?

Back 149

most are hermaphroditic
1 in 500 are male

Front 150

C. elegans:
Life cycle and lifespan?
*important to differentiate!

Back 150

life cycle: 3 days
life span: 3 weeks

Front 151

C. elegans vocab:
Dauer

Back 151

larva goes into a type of stasis and can survive harsh conditions
(can be over 6 months)

Front 152

C. elegans: reasons they're good for genetic research?

Back 152

Dauer (stasis) makes it low maintenence.
-genome is sequenced
-short life cycle
- we can manipulate it for lonegevity, cell structure, etc.

Front 153

Power and benefit of a dissecting microscope?

Back 153

6.3X to 30X magnification

large working space for dissection.

Front 154

C. elegans vocab:
oviduct

Back 154

one of a pair of ducts through which eggs travel from ovary to uterus.
(formerly fallopian tubes)

Front 155

C. elegans vocab:
oocyte

Back 155

immature egg of all animals and some protists

Front 156

C. elegans vocab:
cloaca

Back 156

chamber or duct in last portion of gut of some animals that serves in excretion, reproduction and sometimes respiration

Front 157

C. elegans vocab:
spicule

Back 157

a small hard needle-like piece of bony material, as in the skeleton of a sponge.

Front 158

C. elegans vocab:
alimentary canal

Back 158

the passage in the body through which food passes as it's digested. from mouth to anus. aka: digestive tract?

Front 159

4 functions of extracellular proteins?

Back 159

1. structure (eg. collagen)
2. enzymes (eg. lysozyme)
3. growth factor (Fibroblast growth factor)
4. immune response (antibodies)

Front 160

4 functions of membrane proteins?

Back 160

1. transporters, e.g. __ion channels__
2. anchors, e.g. __integrins___
3. receptors, e.g. growth factor receptors
4. enzymes, e.g. adenylyl cyclase coverts extracellular molecule to an intracellular messenger.
5. recognition, e.g. _glycoproteins___

Front 161

6 Functions of intracellular proteins?

Back 161

1. enzymes, e.g. _kinases__
2. structural proteins, e.g. actin filaments, spectrin
3. motor proteins, e.g. myosin
4. receptors, e.g. __hormone receptors__
5. signal transduction
6. special functions, e.g. _DNA bind proteins__ involved in replication, transcription, translation

Front 162

enzymes are always made of _____.

Back 162

proteins

Front 163

Where do enzymes serve functions?

Back 163

in cell, in membrane and extracellular

Front 164

what are growth factor proteins?

Back 164

these are extra cellular proteins like FGF (fibroblast growth factor) that bind with a receptor protein in the cell membrane that in turn alters intracellular molecules creating a response.

Front 165

How do membrane recognition proteins function?

Back 165

Recognition proteins are usually glycoproteins with the carbohydrate portion projecting out of the cell and into the extracellular space. These give the cell a biochemical personality (like ID) and are important in cell-to-cell recognition.

Front 166

How do membrane enzymes function?

Back 166

they convert extracellular molecules to intracellular messengers.

Front 167

what is ligase?

Back 167

a DNA binding protein (special function intracellular protein)
binds 2 strands of DNA together end to end.
It is an enzyme.

Front 168

chaperones (molecular):
What do they do and where are they found?

Back 168

molecules that assist in protein folding
ER

Front 169

Where are motor proteins found?

Back 169

intracellular!
(move along microtubule substrate)

Front 170

Where are structural proteins found?

Back 170

intra & extra cellular
(collagen, actin, etc)

Front 171

where are receptor proteins found?

Back 171

membrane and intracellular

Front 172

signal transduction?

Back 172

the process by which a cell responds to an extracellular signal

Front 173

Where are signal transduction proteins found?

Back 173

intracellular

Front 174

What connects elastin fibers?

Back 174

"cross links" = covalent bonds

Front 175

What are the "Special functions" performed by some intracellular proteins?

Back 175

transcription, translation, RNA modification, etc

Front 176

fibrous proteins that are a major component of the extracellular matrix and connective tissues?

Back 176

collagen & elastin

Front 177

what are the side effects of protein denaturing?

Back 177

lose function, cause disease

Front 178

special mis-folded proteins that cause scapie, mad cow, sickle cell anemia?

Back 178

Prion

Front 179

the region where an enzyme interacts with another molecule?

Back 179

active or binding site

Front 180

how do protein aggregates form?

Back 180

a misfolded protein converts normal Prp to abnormal conformation creating aggregates.

Front 181

PrP?

Back 181

prion proteins

Front 182

The place on an enzyme where a molecule that is not a substrate may bind, important for conformation.

Back 182

allosteric site

Front 183

allosteric site?

Back 183

The place on an enzyme where a molecule that is not a substrate may bind, thus changing the shape of the enzyme and influencing its ability to be active. (proper conformation)

Front 184

Enzymes, receptor and antigens: what does each interact with?

Back 184

enzyme- substrate
receptor- ligand
antibody- antigen

Front 185

What is immunuglobulin?

Back 185

antibodies

Front 186

shape of antibody/ immunoglobulin?

Back 186

Y shaped

Front 187

what gives antibodies their Y shape?

Back 187

many intra and inter molecular S-S (disulfide) bonds

Front 188

a domain of an antibody that binds a specific antigen?

Back 188

variable domain

Front 189

Why is an antibody called a tetramer?

Back 189

4 parts: composed of two heavy and two light chains.

Front 190

technique to separate proteins by charge, size, affinity to other substances or proteins using specific solutions
(matrices)?

Back 190

Chromoatography

Front 191

technique to separate proteins by their molecular weight (and net charge)?

Back 191

electrophoresis ,
including the now obsolete SDS

Front 192

technique that separates denatured proteins by isoelectric point and then by molecular weight.

Back 192

Two-dimensional gel electrophoresis

Front 193

technique which obtains high resolution image of crystal structure of proteins?

Back 193

X-ray crystallography

Front 194

basic description of X-ray crystallography

Back 194

beam of x rays through protein crystals, then they obtain a diffraction pattern which they convert to computer image.

Front 195

generates a 3-D structure (like x-ray crystallography) but with lower resolution

Back 195

NMR spectroscopy

Front 196

extracellular (ECM)
vs
intracellular proteins (cytoskeleton)

Back 196

extra: collagen and elastin
intra: spectrin and actin

Front 197

what are integrins?

Back 197

membrane anchor proteins

Front 198

where are antibodies located?

Back 198

extracellular

Front 199

example of a proteoglycan?

Back 199

chondroitin sulfate , a structural component of cartilage