Print Options

Card layout: ?

← Back to notecard set|Easy Notecards home page

Instructions for Side by Side Printing
  1. Print the notecards
  2. Fold each page in half along the solid vertical line
  3. Cut out the notecards by cutting along each horizontal dotted line
  4. Optional: Glue, tape or staple the ends of each notecard together
  1. Verify Front of pages is selected for Viewing and print the front of the notecards
  2. Select Back of pages for Viewing and print the back of the notecards
    NOTE: Since the back of the pages are printed in reverse order (last page is printed first), keep the pages in the same order as they were after Step 1. Also, be sure to feed the pages in the same direction as you did in Step 1.
  3. Cut out the notecards by cutting along each horizontal and vertical dotted line
To print: Ctrl+PPrint as a list

192 notecards = 48 pages (4 cards per page)

Viewing:

Microbiology Unit 2

front 1

Radioisotope

back 1

has two extra neutrons and results in an unstable nucleus that will undergo beta decay.

front 2

Products when 1 neutron decays

back 2

1 proton, a beta particle, and energy

front 3

pH scale

back 3

used to measure the levels (concentration) of H+ ions in a solution

front 4

Formula to calculate pH

back 4

-log10 [H+]

front 5

Neutral pH

back 5

7

front 6

One water molecule has:

back 6

one H+ and one OH-
H+ = OH-
neutral pH

front 7

Acid

back 7

has a higher concentration of H+ than OH-

front 8

Base (alkaline)

back 8

has a higher concentration of OH- than H+

front 9

Range of pH scale

back 9

0-14
No unit qualifiers

front 10

pH scale of measurement

back 10

logarithmic scale

front 11

0-6.9 =

back 11

acidic

front 12

7.1-14 =

back 12

basic

front 13

Functional Groups

back 13

interact and form chemical bonds (chemical reactions)
important role in the structure and function of the molecule

front 14

Hydroxyl Group

back 14

OH (oxygen and hydrogen)

front 15

Alcohols

back 15

molecules containing hydroxyl groups

front 16

Methyl Alcohol

back 16

methanol
wood alcohol
used as a preservative

front 17

Ethyl Alcohol

back 17

ethyl
drinkable alcohol
used as a decolorizer

front 18

Isopropyl Alcohol

back 18

isopropyl
rubbing alcohol
used as a decolorizer

front 19

Reagent Alcohol

back 19

combination of methyl, ethyl, and isopropyl alcohol

front 20

Carbonyl Group

back 20

CO
carbon and oxygen (double covalent bond)

front 21

Aldehyde

back 21

terminal carbonyl

front 22

Ketone

back 22

internal carbonyl

front 23

Terminal Carbonyl

back 23

a tail

front 24

Internal Carbonyl

back 24

centered between 2 ends

front 25

Carboxyl Group

back 25

COOH
one carbonyl group + one hydroxyl group

front 26

Characteristics of a Carboxyl Group

back 26

H+ donor
organic acid

front 27

Amino Group

back 27

NH2

front 28

Amines

back 28

amino-group molecules

front 29

Characteristics of Amino Group

back 29

weak bases
H+ acceptor

front 30

Phosphate Group

back 30

PO4

front 31

Characteristics of Phosphate Group

back 31

lots of negative charge
interactive functional group
(how much potential energy is available to do work = free energy released)

front 32

Sulfhydryl Group

back 32

SH
sulfer atom attached to a hydrogen

front 33

Thiols

back 33

any molecule that has a sulfhydryl group

front 34

Characteristics of Sulfhydryl Group

back 34

archae bacteria use as a source of food
found in skunk odors, rotten eggs, and trash
use an iron indicator to determine

front 35

Four Functional Groups

back 35

carbohydrates, lipids, proteins, and nucleic acids

front 36

Carbohydrates

back 36

often polar/hydrophilic
have glycosidic bonds

front 37

Polar

back 37

when placed in water they will develop a partial positive or negative charge

front 38

Hydrophilic

back 38

"water loving"
interacts easily with water

front 39

Isomer

back 39

same molecular formula but different chemical structure

front 40

Examples of isomers

back 40

glucose, fructose, and galactose

front 41

Glycosidic bond

back 41

link 2 or more monosaccharides (covalent bond)

front 42

Building blocks of Carbohydrates

back 42

monosaccharides

front 43

Monosaccharides

back 43

glucose, and fructose

front 44

Smallest Monosaccharide

back 44

glycerol

front 45

6 Carbon chain

back 45

mannitol

front 46

5 Carbon ring

back 46

deoxyribose (H) & ribose (OH)

front 47

Disaccharides

back 47

sucrose, lactose, and maltose

front 48

Polysaccharides

back 48

starch, glycogen, and cellulose

front 49

Starch

back 49

sugar storage in plants

front 50

Glycogen

back 50

sugar storage in animals

front 51

Cellulose

back 51

cell wall material for plants

front 52

Glycosidic bond

back 52

link 2 or more monosaccharides (covalent bonds)

front 53

Lipids

back 53

are often non polar and hydrophobic

front 54

Lipids

back 54

composed of carbons and hydrogens
contain less oxygen than carbohydrates

front 55

Nonpolar

back 55

no distribution of charge

front 56

Hydrophobic

back 56

avoids water

front 57

Triglycerides

back 57

neutral lipids
phospholipids
steroids
oils
waxes

front 58

Phospholipids

back 58

construct of biological membranes

front 59

Esther bond

back 59

linkage between fatty acid and glycerol

front 60

Types of steroids

back 60

cholesterol
testosterone
estrogen
Vitamin D

front 61

Dehydration reaction

back 61

releases water as a product

front 62

Steroids

back 62

a four ring structure

front 63

Phospholipid

back 63

2/3 - fatty acid attachment (hydrophobic)
1/3 - other charged side group (hydrophilic)

front 64

When will phospholipids form a micelle?

back 64

in an aqueous solution

front 65

Micelle

back 65

single layer of phospholipids that have formed a compartment

front 66

Liposome

back 66

2 layers of non polar fatty acids tails facing each other
AKA lipid bilayer

front 67

Proteins

back 67

have the greatest diversity of structure

front 68

Peptide bond

back 68

covalent bonds between 2 or more peptides

front 69

Primary structure

back 69

peptide bonds
looks like a straight cord

front 70

Secondary structure

back 70

begins to coil and fold
looks like a coiled phone cord

front 71

Types of secondary structures

back 71

alpha helix (curly cord)
beta-plated sheet (fan-like)

front 72

Tertiary structure

back 72

tanged coiled and folds
due to interactions of side groups

front 73

Myoglobin

back 73

oxygen holding molecule
may have non-protein (prosthetic group) or metal ions attached (captures oxygen)

front 74

Quaternary structure

back 74

ex. hemoglobin
each have their own prosthetic group

front 75

Globular

back 75

rounded
ex. hemoglobin & moglobin

front 76

Fibrous

back 76

linear
ex. collagen

front 77

Proteins can be:

back 77

scaffolding (gives cell shape and passageways)
transport
molecular motors
motility
enzymes
defenses
receptors/ligands

front 78

Temperature & pH

back 78

range of minimum, optimum, and maximum

front 79

pH denatures proteins at:

back 79

minimum and maximum

front 80

temperature denatures proteins at:

back 80

maximum & become irreversibly damaged

front 81

Protein denaturation

back 81

when you exceed temp. and pH maximum, there is a loss of biological activity
a typical protein that goes through this will not regain activity

front 82

Amphibolic metabolic pathway

back 82

contains anabolic and catabolic pathways

front 83

metabolism

back 83

sum of all biochemical reactions

front 84

anabolism

back 84

biosynthesis
taking small molecules & free energy & making things the cell could use

front 85

catabolism

back 85

taking a large molecule & breaking it down releasing small molecules & free energy

front 86

Metabolism of fats

back 86

beta oxidation

front 87

Metabolism of carbohydrates

back 87

glycolysis

front 88

Metabolism of proteins

back 88

amino acid catabolism

front 89

Enzymes

back 89

structured to facilitate the change of substrate (reactant) by presence of an active site to combined enzyme-substrate complex to product

front 90

Enzymes have a high degree of...

back 90

specificity for substrate

front 91

Enzyme-substrate

back 91

very specific for substrate has a flexible fit

front 92

Enzymes

back 92

help form or break chemical bonds
can participate in multiple chemical reactions
reactions occur with less energy used
reactions occur faster

front 93

Energy of activation

back 93

the amount of energy required

front 94

Enzyme suffix

back 94

-ase & -zyme

front 95

Controlling enzymes

back 95

inhibitors and activators

front 96

Active site

back 96

where the substrate fits

front 97

coenzyme

back 97

derived from vitamins

front 98

cofactors

back 98

derived from minerals

front 99

Aponenzyme

back 99

scaffolding to which everything is attached to (usually protein and a small amount of RNA)

front 100

Competitive inhibitor

back 100

similar shape to block active site; metabolism is stopped

front 101

Noncompetitive inhibitor

back 101

attach themselves to allosteric site and changes the shape of the active site

front 102

Glycolysis

back 102

not dependent upon the presence of oxygen
1.) substrate phosphorylation from ATP (ATP converted to ADP)
2.) breaking a 6-carbon molecule, glucose, into 2-3 carbon molecules
3.) transfer of 2 electrons to NAD (turns in to NADH+)
4.) capture energy in ATP

front 103

ATP

back 103

source of PO4 (phosphate groups)

front 104

Glucose

back 104

kinase phosphorylates (attached to a phosphate atom)

front 105

Isomerase

back 105

Glucose - P => Fructose - P

front 106

Products of glycolysis

back 106

2 net yield of NADH
2 net yield of ATP (substrate phosphorylation)
2 pyruvate

front 107

Dephosphoralation

back 107

removal of a phosphate

front 108

substrate phosphoralation

back 108

transferred from one organic molecule to another

front 109

What can a cell do with pyruvic acid?

back 109

fermentation & TCA & respiration

front 110

Homolactic acid fermentation

back 110

produces lactic acid

front 111

Bacteria that perform homolactic acid fermentation

back 111

Lactobacillus & streptococcus

front 112

Alcoholic fermentation

back 112

produces ethyl alcohol & CO2

front 113

Bacteria that perform alcoholic fermentation

back 113

saccharomyces (yeast)

front 114

mixed-acid fermentation

back 114

produces acetic acid, succinct acid, ethyl alcohol, CO2, & hydrogen

front 115

Bacteria that perform mixed-acid fermentation

back 115

escherichia, acetobacter, shigella

front 116

Propionic fermentation

back 116

produces propionic acid, acetic acid, & CO2

front 117

Bacteria that perform propionic fermentation

back 117

Propionibacterium
swiss cheese

front 118

Butanediol fermentation

back 118

produces butanedial & CO2

front 119

Bacteria that perform butanediol fermentation

back 119

enterobacter & klebsiella

front 120

Butyric-butylic fermentation

back 120

produces butyric acid butanol, isopropyl alcohol, acetone, and CO2

front 121

Bacteria that perform butyric-butylic fermentation

back 121

clostridium
solvents & gangreeene

front 122

microbial or ecological succession

back 122

yeast => lactic acid bacteria => acetic acid bacteria

front 123

Alcoholic fermentation

back 123

reduces bitterness
saccharomyces cerevisiae

front 124

lactic acid fermentation

back 124

lactobacillus & streptococcus

front 125

Products of citric acid cycle per 1 acetyl group

back 125

3 NADH
1 FADH2
2 CO2
1 GTP <=> ATP - substrate phosphorlaytion
12 net ATP

front 126

Cellular respiration

back 126

electron pairs donated from NADH and FADH2
electron transport and terminal electron acceptor = oxygen or inorganic molecule (If anaerobic)
proton motive force used to make ATP
ADP + Pi (ATPsynthase) yields ATP

front 127

Chemiosmosis

back 127

movement of hydrogen ions (protons) increase changes pH (acidic)

front 128

ATPsynthase allows protons...

back 128

to move back into the cell.

front 129

Oxidative phorphorylation

back 129

use inorganic phosphate groups

front 130

Beta oxidation

back 130

catabolism of a neutral lipid (separates glycerol backbone and shuttles it into glycolysis)

front 131

hydrocarbons

back 131

manufacture acetyl-COa from 2 carbon units. transported by coenzyme a

front 132

2 carbons in the krebs cycle =

back 132

12 ATP

front 133

Lipase

back 133

enzyme that breaks down lipids

front 134

Protease

back 134

breaks down proteins

front 135

Bioremediation

back 135

microbes cleaning up

front 136

Bioreclamation

back 136

environment returning to normal due to cleaning

front 137

Decarboxylation

back 137

removing carboxyl group
leaves a two carbon group to be given to krebs cycle

front 138

biosynthesis

back 138

building molecules, manufacturing amino acids, carbohydrates, nitrogenous bases (almost every intermediate)

front 139

Chemical energy for bioluminescence

back 139

special enzymes that use ATP & release light (locate in specific structures)
ex. angler fish

front 140

generation time

back 140

time it takes to grow from one generation to the next (one cell to two cells)
normally about 20-30 minutes

front 141

Lag phase

back 141

no change in number of bacteria (internally active)

front 142

Log phase

back 142

cell development (rapid increase in numbers)

front 143

Stationary phase

back 143

same number of cells dying that are being produced

front 144

Death phase

back 144

more cells dying than are being produced

front 145

Direct microscopic cell count

back 145

Petro F-Hauser counting chambers - specialized gritted slides that we place a known amount of bacteria
problem: only know number or absent or presence of bacteria, not alive or not

front 146

Viable cell counts
plate counts

back 146

qualitative (quadrant streak) & qualitative (urine streak)
answers yes or no for bacteria

front 147

Membrane filtration

back 147

has a ton of pores placed in a funnel & liquid is vacuumed through
anything trapped on the surface is placed on an agar plate, which can be colonized & counted
liquid in the bottom is sterilized
used in water and waste water management

front 148

Turbidity

back 148

cloudiness of a liquid that could be due to microorganisms (shine light through to determine blockage of light)

front 149

Most Probable Number (MPN)

back 149

determine presence of microbes in water or liquid
based on statistical numbers and estimates
different concentrations
incubate and look for turbidity

front 150

Psychrophile

back 150

cold lover 4 to 30 degrees Celsius

front 151

Mesophile

back 151

body temp
35-37 degrees celsius

front 152

Thermophile

back 152

40 to 60 degrees celsius

front 153

Hyperthermophile

back 153

80 to 110 degrees celsius

front 154

Acidophile

back 154

below pH of 7

front 155

Alkalophile

back 155

above pH of 7

front 156

Thermoplasma acidophilum

back 156

hot
often grows in sulferous, acidic environment (yellow stone)

front 157

Alcaligenes faecalis

back 157

cold

front 158

Barophilic

back 158

grows under extreme pressure

front 159

example of barophilic

back 159

methanococcus jannaschii

front 160

Obligate aerobe

back 160

must have oxygen for growth

front 161

Pellicle

back 161

growth of the organism at the top

front 162

Metabolic pathway of obligate aerobe

back 162

cellular or aerobic respiration
terminal electron acceptor = oxygen

front 163

Facultative anaerobe

back 163

oxygen required but may be used
most versital and thus most often associated with causing disease

front 164

How many ATP are produced during aerobic respiration per glucose?

back 164

38 ATP

front 165

How many ATP are produced during fermentation per glucose?

back 165

2 ATP

front 166

Aerotolerant anaerobe

back 166

oxygen is not used
cloudiness is the same throughout

front 167

metabolic process of aerotolerant anaerobes

back 167

fermentation

front 168

Obligate (strict) anaerobe

back 168

oxygen kills these anaerobes
no growth in the oxygen rich zone

front 169

metabolic pathways for obligate anaerobes

back 169

fermentation

front 170

Clostridium tetani

back 170

obligate anaerobe causes tetanus (lockjaw)

front 171

Microaerophile

back 171

requires less oxygen
2% - 6% oxygen required

front 172

metabolic pathways used by microaerophile

back 172

fermentation and cellular respiration

front 173

Capnophilic

back 173

"carbon dioxide loving"
5% CO2

front 174

example of capnophilic bacteria

back 174

neisseria species
causes gohnorreia

front 175

Organic compounds

back 175

biological molecules that contain carbon

front 176

Organic molecules commonly include:

back 176

carbon, hydrogen, oxygen, and nitrogen

front 177

Inorganic molecules

back 177

molecules that do not contain carbon

front 178

Molecular formula for glucose

back 178

C6 H12 06

front 179

Chemical bonds

back 179

linkages made between the atoms in molecules

front 180

An atom comprises:

back 180

a nucleus orbited by negatively charged electrons

front 181

Protons

back 181

positively charged

front 182

Neutrons

back 182

no charge

front 183

Nucleus is made up of:

back 183

protons and neutrons

front 184

Ionic bonds

back 184

result from the electrostatic attraction between two ions of opposite charge

front 185

Ions form when:

back 185

they have lost or gained an electron

front 186

Cation

back 186

ion with a positive charge
lost an electron

front 187

Anion

back 187

ion with a negative charge
gained an electron

front 188

Covalent bond

back 188

forms when electron pairs between two atoms are shared

front 189

Hydrogen bond

back 189

weak H to O or H to N attractions between different molecules

front 190

Hydrogen bonding is important:

back 190

in the formation of a wide variety of biological molecules such as proteins and nucleic acids (DNA)

front 191

Disulfide bond

back 191

AKA sulfer bridge
is a single covalent bond between two sulfur containing atoms

front 192

Cysteine

back 192

a sulphur containing amino acid