Biology 105 Test 2

Front 1

matter

Back 1

- occupies space and has mass
- composed of elements
- elements are composed of atoms

Front 2

nucleus

Back 2

- central core of an atom
- composed of protons and neutrons

Front 3

protons

Back 3

have a positive charge and a mass of 1 atomic mass unit

Front 4

neutrons

Back 4

carry no charge and have a mass of 1 amu

Front 5

atomic mass

Back 5

# protons + # neutrons

Front 6

isotopes

Back 6

different forms of an element due to variations in atomic mass

Front 7

radioactive isotopes

Back 7

unstable, decay into other elements with the release of energy

ex: carbon 14 decays to nitrogen 14

Front 8

half-life

Back 8

measurement of radioactive decay

amnt of time for 1/2 of a given amnt of a radioactive isotope to decay

Front 9

electrons

Back 9

- one negative charge
- mass of 1/1860 amu
-"orbit" around nucleus in defined patterns

Front 10

# of electrons = # of

Back 10

protons in an uncharged atom

Front 11

Atomic bond

Back 11

connecting atoms together

Front 12

formation of compounds

Back 12

2 or more atoms connected together to form a chemically discreet entity

Front 13

molecule

Back 13

single grouping of atoms

Front 14

ionic bond

Back 14

- gain/loss of electrons between atoms

Front 15

ions

Back 15

gain or lose electrons

Front 16

gain an electron

Back 16

net negative charge

Front 17

lose an electron

Back 17

net positive charge

Front 18

+ and - ions ______ each other in proportion of charges

Back 18

attract

Front 19

covalent bond

Back 19

sharing of electrons between atoms

shared in pairs, one electron from each atom

ex: water- H electron-sharing-0-electron-sharing-electron-H

Front 20

hydrogen bonds

Back 20

in water and other molecules, slight charges attract

Front 21

Water

Back 21

50-95% of organisms
75% of earth's surface

Front 22

biological importance of water

Back 22

-bathing
-raw material for metabolism
-carries substances in and out of cells
-internal medium for cells

Front 23

solvent properties

Back 23

- polar and other ionic substances dissolve best in water

Front 24

hydrophilic

Back 24

polar substances that dissolve well in water

Front 25

hydrophobic

Back 25

nonpolar substances that do not dissolve well inw ater

Front 26

cohesion

Back 26

hydrogen bonds hold water molecules together to act as a unit

Front 27

adhesion

Back 27

attraction of polar water molecules to other substances

Front 28

suface tension

Back 28

pull of water molecules of surface molecules creates a coherent surface

Front 29

caillary action

Back 29

water is drawn into a small tube due to water being attracted to the tube (adhesion) , and the film of water on the tube in turn attracts other water molecules (cohesion)

Front 30

high heat retention

Back 30

-hard to evaporate because the hydrogen bonds must be broken to separate molecule

= requires more heat energy than other substances

-retains lots of heat

-sweating = excess heat is carried away by water evaporating fromthe sweat

Front 31

acid

Back 31

gives up a proton easily in water

weak acid does not give up H+ as readily as a strong acid

hydrophilic

0-<7

Front 32

base

Back 32

gives up an OH- group easily in water

hydrophilic

7-14

Front 33

pH=

Back 33

-log(H+) = negative log of the hydrogen ion concentration

Front 34

the numbers show a difference in acidity/basicity by a factor of ___

Back 34

ten

Front 35

chemical reactions

Back 35

involve breaking and re-forming bonding patterns

Front 36

breaking of bonds ____ energy

Back 36

releases

ex: things on stove- energy is released as light and heat

Front 37

formation of bonds _________ of energy

Back 37

requires input of energy

Front 38

oxidation

Back 38

reactions that release energy

loss of an electron

ex: burning

***oxidation and reduction are coupled, i. e., occur simultaneously -when a substance is oxidized, another substance in the overall reaction is reduced

Front 39

reduction

Back 39

reactions that require/store energy

gain of an electron

***oxidation and reduction are coupled, i. e., occur simultaneously -when a substance is oxidized, another substance in the overall reaction is reduced
ex: photosynthesis

Front 40

reduced compounds

Back 40

higher energy stored

Front 41

oxidized compounds

Back 41

lower energy stored

Front 42

polymer

Back 42

large molecule composed of many repeating subunits called monomers

ex: starch

Front 43

synthesis

Back 43

building

-monomers have an H on one side of the molecule and an OH on the other

-synthesis involves removing a hydrogen from one monomer and an -OH from the other monomer unit, then the H and OH are combined to form water and the two monomers are joined together.

also called dehydration synthesis

Front 44

hydrolosis

Back 44

breakdown of a polymer, using water

-a water molecule is broken down and as the monomers are separated, the H from the water is attached to one monomer and the OH from the water is attached to the other monomer unit

Front 45

energy

Back 45

ability to do work

Front 46

kinetic energy

Back 46

energy of motion

Front 47

potential energy

Back 47

stored energy

Front 48

first law of thermodynamics

Back 48

cannot create or destroy energy

Front 49

second law of thermodynamics

Back 49

Some useful energy is lost to a system when a conversion takes place. [No energy conversion is ever 100% efficient.]

order -------- > disorder ===>energy lost as heat and possibly some useful energy is released

disorder ------> order =requires a useful energy input from outside system

Example: Whe you eat a piece of bread, you break down the oder of the starch molecules to release their energy. You can never absorb all of the energy released from the starch, and some of it is used to increase order in (buildup) your body, and some is lost as heat. Thus the starch order goes to disorder, and within your body, disorder goes to order.

Front 50

organic

Back 50

compounds containing carbon

Front 51

carbohydrates

Back 51

sugars

Front 52

monosaccarides

Back 52

simple sugars
3-7 carbon atoms
straight chain or ring form

Front 53

disaccharides

Back 53

two covalently bonded monosaccarides

Front 54

polysaccharde

Back 54

polymer of monosaccharides

Front 55

functions of carbohydrates

Back 55

energy source
energy storage
structure

Front 56

lipids

Back 56

fats, waxes, oils, sterols
strongly hydrophobic

Front 57

neutral fats

Back 57

subunits: glycerol and fatty acids

-3 fatty acids join 1 glycerol by synthesis to form a neutral fat

Front 58

glycerol

Back 58

3-carbon unit with an -OH attached to each carbon

Front 59

fatty acid

Back 59

long chain of C's and H's

-number of carbons always an even number

-saturated fatty acid - all C's joined by single bonds

-unsaturated fatty acid - some C's joined by double bonds

-different fatty acids have different chain lengths and differing number of of double bonds (12 to more than 40 carbons long)

Front 60

unsaturated fatty acids

Back 60

neutral fat that is liquid a room temp. => oils

-derived from plants (some animal sources)

Front 61

saturated fatty acids

Back 61

neutral fat that is solid at room temperature => fats

-derived from animals (some plant sources)

Front 62

soap

Back 62

fatty acid + base

Front 63

sterols/steroids

Back 63

-four ring backbone -side groups determine the exact compound steroid. examples of steroids: cholesterol, testosterone, estrogen

Front 64

functions of lipids

Back 64

1. energy source

2. energy storage

3. structure

4. hormones

Front 65

proteins

Back 65

basic unit: amino acids

20 amino acids in living things

various proteins differ in the number, kind, and linear arrangement of constituent amino acids

Front 66

peptide

Back 66

short chain of amino acids protein: long chain of amino acids - may be thousands long

Front 67

primary protein structure

Back 67

linear arrangement of amino acids in the polymer

amino acids join by synthesis

-covalent bond between amino acids = peptide bond

Front 68

secondary protein structure

Back 68

primary chain coils like a spring (alpha-helix) or folds in a pleated sheet arrangement

-held in place by hydrogen bonds between amino acids

Front 69

tertiary structure

Back 69

coiled chain folds and forms bonds between R- groups of the aa's ===> globular or sheetlike appearance

-sulfur-containing amino acids form -S-S- (disulfide) bridges

Front 70

quaternary structure

Back 70

interactions of protein units to form a functioning unit

-not all proteins have quaternary structure

Front 71

denaturation

Back 71

-usually changes or destroys function

-heat, chemicals, radiation can cause denaturation

-frying an egg; hair perm

Front 72

functions of protien

Back 72

1. structural

2. energy source

3. enzymes

4. other: hormones; antibodies; carriers

Front 73

functions of nucleic acids

Back 73

-heredity and cellular/organismal control

-information storage and processing

Front 74

Types of nucleic acids

Back 74

dna and rna

Front 75

enzymes

Back 75

virgually all reactions in an organism

protiens

Front 76

organic caalyst

Back 76

speeds a reaction without being altered overall

E + S ---> ES complex ---> E + P

Front 77

active site

Back 77

place on the enzyme where catalysis occurs

-substrate binds at active site for reaction

Front 78

specifity

Back 78

enzymes are very specific - each does only one kind of reaction

ex: lock and key

Front 79

catalase

Back 79

catalyses the breakdown of toxic hydrogen peroxide to water. This is all that this enzymes does!

Front 80

amylase

Back 80

an enzyme in saliva that breaks starch down into glucose monomer units. This is the only substrate on which this enzyme works. Cellulose is also a polymer of glucose but amylase will not break down cellulose.

Front 81

mechanism for catalyzing reactions

Back 81

enzymes lower the activation energy of a reaction

Front 82

activation energy

Back 82

"prime" of energy to begin a reaction

Front 83

stopping enzyme activity

Back 83

1. competitive inhibiation
2. denaturation

Front 84

competitive inhibition

Back 84

ubstance similar in size and shape to the substrate "fools" the enzyme and gets into the active site

-binds up the enzyme because the reaction does not occur and enzyme cannot release the inhibitor

-destroys the activity of the enzyme

-analogy: getting the wrong key stuck in a lock

Front 85

denaturation

Back 85

- change in tertiary structure of protein changes the configuration (shape) of the active site and the substrate cannot bind which means that catalysis cannot occur

-causes of denaturation: anything that will alter the chemistry or destroy proteins

-pH - for most enzymes extremes of acidity or basicity will change the tertiary structure

-temperature - for example, cooking

-heavy metals - mercury, arsenic, lead, etc.

-radiation - UV light, radioactivity, etc. destroy protein structure by breaking the molecule apart

Front 86

conditions for enzyme activity

Back 86

optimum temperature and pH

Front 87

cofactors

Back 87

1. activators
2. coenzymes

Front 88

activators

Back 88

inorganic substances that bind w/ the protien to create a functioning enzyme

Front 89

coenzymes

Back 89

- change in tertiary structure of protein changes the configuration (shape) of the active site and the substrate cannot bind which means that catalysis cannot occur

-causes of denaturation: anything that will alter the chemistry or destroy proteins

-pH - for most enzymes extremes of acidity or basicity will change the tertiary structure

- temperature - for example, cooking

-heavy metals - mercury, arsenic, lead, etc.

-radiation - UV light, radioactivity, etc. destroy protein structure by breaking the molecule apart

Front 90

control of enzyme activity

Back 90

-control of enzyme activity is critical in regulating metabolism

-turning on enzymes when required

-turning off enzymes when not required

-regulating level of activity

mechanisms:
concentration of substrate
allosteric site

Front 91

concentration of substrate

Back 91

-low substrate concentration --> low enzyme activity

-presence of product may lower rate of enzyme activity

-feedback mechanism may lower rate of enzyme production, leads to lower activity

Front 92

allosteric sites

Back 92

-site away from the active site to which molecules bind

-changes shape of the active site, blocking catalysis

Front 93

noncompetitive inhibition

Back 93

the substance does not fit into the acitve site like a competitve inhibitor, but does halt enzyme activity

Front 94

biochemical pathway

Back 94

series of reactions within an organism that result in particular products being formed. Enzymes usually mediate each step of the reaction.

-each enzyme is specific to the step in the pathway that it catalyses

-various biochemical pathways can interconnect and these inteconnections can become quite complex within the metabolising cell

Front 95

cell theory

Back 95

organisms are composed of basic units called cells

1. living things are composed of cells
2. cells come from existing cells

1805

earlier idea: organisms composed of interwoven fibers, like cloth

Front 96

robert hooke

Back 96

1665
English
Observed "pores" in cork
named cells after monks's cells

Front 97

Antonie van Leeuwanhoek

Back 97

1677 Dutch
Ammature lensemaker and microscopist
single celled animas, spermatozoa

Front 98

Lorenz Oken

Back 98

-cell theory
- all organisms originate from and are composed of cells

Front 99

Matthias Schleiden; Theodore Schwann

Back 99

1839 Germans
-cell theory published, restatment of Oken

Front 100

Rudolf Virchow

Back 100

1855 German
-cell division
-all cells come from existing cells
-restatement of Oken

Front 101

Basic Cell Structure

Back 101

I. Outer Bounding Membrane
-cell membrane
II. Protoplasm
A. nucleus - if present
B. cytoplasm
1. organelles
2. ground substance
III. Cell Wall - if present

Front 102

Cell types

Back 102

eukaryotic and prokaryotic

Front 103

Eukaryotic

Back 103

* nucleus
* membrane-bound organelles
* generally larger cells

Front 104

Prokaryotic

Back 104

* no nucleus
* no membrane-bound organelles
* generally smaller cells

Front 105

Cell membrane

Back 105

completely surrounds cell

Front 106

Cell membrane acts to

Back 106

- control movement of substances into and out of cell
o selective
- hold cell intact
o cell dies if broken
- recognize other cells and molecules

Front 107

Membrane Structure

Back 107

two major components:
lipid bilayer
embedded protiens

Front 108

Lipid Bilayer major components

Back 108

phospholipid and cholestoral

Front 109

Phospholipid structure

Back 109

glycerol
"tail" of two fatty assets (hydrophobic)
phosphate head (hydrophlic)

Front 110

bilayer

Back 110

two layers of phospholipid.

in the membrane, tails are to the inside and head is it to the outside

Front 111

embedded proteins

Back 111

- interspersed in lipid bilayer
o “mozaic”
- partially or completely through lipid bilayer
- can move about within the lipid bilayer
o “fluid”
- often with complex carbohydrates attached
o glycoprotein (“glyco” = sugar)

Front 112

membrane function

Back 112

- acts as a barrier
- controls was crosses

Front 113

protein functions

Back 113

- cell-cell recog
- substance recog (only specific substances, relay a chemical message)
- carry substances across
- enzymes
- attach cells to eachother

Front 114

semipermeability

Back 114

- some substances pass through easily: water
- some hard: sugar
- alternate names: selectively permeable and differentially permeable

Front 115

amnt of semipermeability based on

Back 115

size and charge

- harder in large molecules
- small, nonpolar substances easily cross, larger polar do not

Front 116

Passive Transport

Back 116

transport across membranes
- does not require energy expenditure

Front 117

types of passive transport

Back 117

simple diffusion
osmosis
facilitated diffusion

Front 118

diffusion

Back 118

-based on random movement of molecules due to heat
- any temperature above absolute zero involves molecular motion
-little motion: solid, much motion: gas
-concentration gradient higher and lower concentrations of a substance

- NET movement of a substance from an area of higher to lower concentration

- In area of higher concentration, more molecules available to move in direction of lower concentration than vice versa

-eventually events out
-dynamic equilibrium- constantly balanced and unbalanced, but on average, balanced

Front 119

transport by diffusion

Back 119

- substance moves across membrane by simple diffusion
- solutes = dissolved substances
o diffusion across membrane = dialysis
- solvent = water
o diffusion across membrane = osmosis

Front 120

Osmosis

Back 120

* net movement (diffusion) of water across a semipermeable membrane
* dissolved substances lower the concentration of water in a solution
o more dissolved substance = lower water concentration
* across a membrane, this can create a concentration gradient --> diffusion

Front 121

hypotonic

Back 121

lower solute concentration

Front 122

hyper

Back 122

higher solute concentration

Front 123

net movement in osmosis

Back 123

hypertonic --> hypotonic

Front 124

isotonic =

Back 124

no net movement

Front 125

cell in hypotonic solution

Back 125

gains water

Front 126

cell in a hypertonic solution

Back 126

loses water

Front 127

Facilitated Diffusion

Back 127

* protein channel across
* selective
* allows diffusion of polar substances
* follows concentration gradient only

Front 128

transport across membranes and types

Back 128

requires energy expendature by cell

types:
-proten carriers
-vasiculation

Front 129

protein carriers

Back 129

* movement by change in shape in protein
* selective
* chemical energy (ATP) used
* movement against a concentration gradient
o accumulation of substances
o exclusion of substances

Front 130

vasiculation

Back 130

involves formation of membrane sacs

Front 131

vesticles

Back 131

membrane sacs

Front 132

endocytosis

Back 132

entry into a cell
cell membrane forms vesticle around engulfed object

Front 133

exocytosis

Back 133

exit from a cell
vesicle fuses with cell membrane, releases substance

Front 134

cell size

Back 134

20 um to ostrich egg

-as cell size increases, surface area becomes too small to serve volume -> limits on size

Front 135

protoplasm

Back 135

everything inside the cell membrane: nucleus and cytoplasm

Front 136

nucleus

Back 136

- defines eukaryotes
# surrounded by double membrane with large pores
# contains chromatin-heredity material
# often spherical and central

Front 137

functions of nucleus

Back 137

- regulates cellular activity
- storehouse of info
- reproduction

Front 138

nucleolus

Back 138

-area in nucleus of RNA synthesis
- not an organelle

Front 139

endomembrane System

Back 139

* interconnected and interacting membrane-bound organelles
* endoplasmic reticula
* Golgi apparatus
* lysosomes
* vacuoles and vesicles

Front 140

endoplasmic reticulum

Back 140

two types: rough and smooth
- interconnected network of membrane sacs

Front 141

rough ER

Back 141

* membrane sacs
* covered with ribosomes
o protein synthesis
o protein export
* forms vesicles
* forms new membrane

Front 142

Smooth ER

Back 142

* membrane tubules
* lack ribosomes
* lipid synthesis
o neutral fats
o steroids
* sugar control
* detoxification

Front 143

Golgi Bodies

Back 143

* stacks of membrane sacs
* packaging and secretion of substances
* receiving face-membrane from ER
* chemical modification
* vesicles form on transport side

Front 144

lysosomes

Back 144

* vesicles that contain digestive enzymes
* merge with food vesicles (from endocytosis) to digest food
* digest worn organelles
* “suicide sac” - if bursts, digests and kills cell => programmed cell death
o cells between developing fingers and toes
o disappearance of tadpole tail

Front 145

pompe's disease

Back 145

lysosome related disease
glcogen accumulates
lacks glycogen digesting enzyme

Front 146

tay-sach's

Back 146

affects nervous system
lacks lipid digesting enzyme

Front 147

Vacuoles

Back 147

* bounded by membrane
* storage
* plants: large central vacuole
o contains water - water relations
o contains wastes and pigments
+ cooking beets releases betacyanin - cooking water turns red
o stores nutrients

Front 148

Peroxisome

Back 148

* vesicles
* contain enzymes for breakdown of hydrogen peroxide to water and oxygen gas

Front 149

mitochondrion

Back 149

breakdown of substances to release energy in useful chemical form

double membrane- inner is folded, sight of enzyme activity

- cellular respiration
- all eukaryote

Front 150

cholorplast

Back 150

photosynthesis
* double membrane
* internal stacks of membrane sacs (grana)
* matrix (stroma)
* chlorophyll (green)
* photosynthesis
* plants and algae

Front 151

flagellum/cilium

Back 151

* cell extensions
* internal framework of tubes
o 9 doublets of tubes around 2 central tubes
+ 9+2 arrangement
o spokes of protein fibers
o protein arms on tubes use ATP energy to create movement

Front 152

flagellum

Back 152

* long and whiplike
* relatively few in number
* whiplike undulations cause movement

Front 153

cilium

Back 153

* short and bristlelike
* relatively numerous
* “breaststroke” movement - stroke/recovery movement

Front 154

basal body

Back 154

* anchors cilium or flagellum in cell
* 9 triples of tubes without central core = 9+0

Front 155

centrioles

Back 155

* similar to basal body - 9+0
* paired, lie at right angle nest to nucleus
* function in cell division
* not found in plants

Front 156

cytoskeleton

Back 156

* latticework of fibers and tubes
* not rigid - easily broken and re-formed

Front 157

cell wall

Back 157

* outside the cell membrane
* basketlike, very porous
* plants, fungi, algae, bacteria
* composed of:
o cellulose - plants => paper, cotton
o proteinaceous substance - bacteria
o chitin - fungi

Front 158

tight functions

Back 158

protein rivets, leakproof seal

*animals*

Front 159

anchoring junctions

Back 159

protein plates, allow substances to pass by

*animals*

Front 160

communicating junctions

Back 160

protein channel between cells

*animals*

Front 161

middle lamella

Back 161

pectic glue between cell walls

Front 162

plasmodesmata

Back 162

membrane-lined channels between cells

Front 163

plants do not have

Back 163

lysosomes centrioles

Front 164

animals do not have

Back 164

cholropasts
central vacuole
cell well

Front 165

prokaryotic cells

Back 165

no nucleus- DNA is naked in cytoplasm (nucleoid)
no membrane-bound organelles
cell wall proteinaceous

Front 166

energy

Back 166

ability to do work

Front 167

cellular work

Back 167

- metabolism
- transport
- reproduction

Front 168

cellular energy

Back 168

chemical energy
- readily available
- universal

Front 169

ATP

Back 169

bond between last 2 phosphates easily broken and releases energy

# ATP breaks down to ADP and a phosphate
- releases immediately useful energy to do work
- "energy currency" of the cell

Front 170

ATP formation

Back 170

ADP + Pi = ATP
stores energy for immediately cellular work

Front 171

chemiosmosis

Back 171

* energy used to pump H+ across membrane
* creates a charge across membrane = “battery”
* ATPase in membrane allows flow of H+
* H+ flow energy allows ATPase to form ATP
* mechanism of ATP formation

Front 172

photosynthesis

Back 172

* uses light energy to form energy-rich organic compounds
* reduction
* autotrophs
* cloroplasts
* grana- stacks of membrane sacs contain chlorophyll
* stroma- surrounding matrix and contains enzymes
* 6 CO2 + 12 H2O --> C6H12O6 + 6 O2 + 6 H2O

Front 173

Cellular respiration

Back 173

* releases stored chemical energy to form ATP
* oxidation
* autotrophs and heterotrophs
* occurs in cytopasm
* eukaryotes, continues in mitochondria

Front 174

suggests a two-step process:

Back 174

1) light reactions - harvest light energy
2) nonlight reactions - fix carbon into organics
* overall, carbon is reduced, storing energy

Front 175

aerobic respiration

Back 175

in mitochondria
requires oxygen gas
36 atp made
part of cellular respiration
all aerobic organisms

Front 176

alcoholic fermentation

Back 176

no ATP made (2 are made in glycolosis, available to organism)

Front 177

lactic acid synthesis

Back 177

no atp made
- occurs in the absence of oxygen gas

Front 178

# ATP made in glycolysis

Back 178

- 2 used as prime + 4 made = 2 net

Front 179

role of mitochondrion

Back 179

aerobic respiration
inner folded membrane site of ATP synthesis
chemiosmosis across the inner membranes
folds create pockets for H+ concetration buildup