Biology 12 Test 2

Front 1

Name the 4 major classes of biological molecules?

Back 1

carbohydrates, lipids, Proteins, Nucleic acids

Front 2

Which of the following biological molecules are macro molecules?

Back 2

carbohydrates and lipids may be macro molecules since they have a relatively large size and high molecular weight and proteins and nucleic acids are macromolecules

Front 3

What is the monomer in the biological molecules?

Back 3

Carbohydrate-saccharide (triangle)
Lipids(not truly a polymer)--
Proteins- amino acid (circle)
Nucleic acids- nucleotide (rectangle)

Front 4

Are biological molecules polymers?

Back 4

yes except lipids

Front 5

Define polymer

Back 5

macro molecule built by forming covalent bonds b/w a long chain of similar units (monomers)

Front 6

How are each of the 4 polymers (biological molecule) split and linked?

Back 6

split by hydrolysis and linked by dehydration synthesis

Front 7

another name for dehydration synthesis is....

Back 7

condensation

Front 8

Why are lipids different from the polymers?

Back 8

Lipids are composite molecules since they are comprised of several distinct parts that are joined to produce an operational whole

Front 9

is a carbohydrate an organic molecule?

Back 9

yes

Front 10

name the components of a carbohydrate and its formula

Back 10

carbon hydrogen oxygen C subscript x ( H subscript 2 O)subscript y

Front 11

what are the functions of a carbohydrate?

Back 11

energy metabolism and storage
structural material

Front 12

Where do people generally get their source of carbohydrates from?

Back 12

plants by process of photosynthesis

Front 13

What uses up the carbohydrate in a cell?

Back 13

used by mitochondria produce ATP energy during cellular respiration

Front 14

Name the four major types of carbohydrates

Back 14

Monosaccharide- one saccharide unit
Disaccharide- two saccharide units
Oligosaccharide- 3-10 saccharide units
Poly saccharide- more than 10 saccharide units

Front 15

Give the general formula for monosaccharide

Back 15

(C H subscript 2 O) subscript n where n=# carbon atoms ranging 3-7

Front 16

A single saccharide serves as a basic ______________________ of all carbohydrates

Back 16

Structural unit

Front 17

What are the most common examples of monosaccharides

Back 17

six- carbon hexose monosaccharides and five-carbon pentose monosaccharides

Front 18

name the hexose monosaccharides and give it's general formula

Back 18

Glucose-made during photosynthesis
Fructose-gives fruit sweet taste
Galactose-found in milk
(C subscript 6 H sub.12 O sub 6)

Front 19

disaccharides are formed by______________________ and split by______________________

Back 19

dehydration synthesis where a water molecule is removed from the sites of the union
Hydrolysis where large molecule broken into 2 smaller ones

Front 20

Name the common disaccharides

Back 20

Maltose-beer
Sucrose-table sugar
Lactose-milk
(C sub 12 H sub 22 O sub 11)

Front 21

What monosaccharides are created when water is added to a maltose, sucrose, lactose

Back 21

M-(glucose, glucose)
S-(glucose, fructose)
L-(glucose, galactose)

Front 22

Polysaccharides serve mainly as ___________ and __________ within organisms

Back 22

Energy storage
Structual material

Front 23

Name the 4 polysaccharides within animals and proteins state if storage or structure

Back 23

Starch- plant storage
Gylcogen- animal storage
Cellulose (Fibre)- plant structural
Chitin- animal structure

Front 24

Is it true that plant storage poly saccharide is made of a few glucose molecules joined together?

Back 24

no its made of hundreds or thousands of glucose molecules joined together

Front 25

name the two forms of starch

Back 25

Amylose
Amylopectin

Front 26

Are both Amylose and Amylopectin branched glucose chains?

Back 26

no amylose is unbranched an amylopectin is branched

Front 27

Is it true that animal storage polysaccharide (glycogen) is made of branched glucose chains

Back 27

yes

Front 28

Where is glycogen stored

Back 28

In the liver and muscle cells of animals

Front 29

another name for cellulose is

Back 29

FIbre

Front 30

plant structural poly saccharide (cellulose) is found where in plants

Back 30

cell wall

Front 31

Is cellulose branched or unbranched glucose molecules?

Back 31

unbranched

Front 32

Is it true that the CH sub 3 OH of the glucose molecule part alternate from side to side in a cellulose?

Back 32

no the CH sub 2 OH alternates

Front 33

do cellulose chains run parallel or anti parallel to one another?

Back 33

run parallel to one another in alternate layers providing extra stength

Front 34

where is chitin found and is it a modified form of cellulose?

Back 34

exoskeleton of insects/crustaceans.
and yes it is modified form

Front 35

Is it true that a lipid is an organic molecule that is soluble in water but insoluble in organic solvents such as ether and chloroform.

Back 35

no insoluble in water soluble in organic solvents

Front 36

How do you define a lipid?

Back 36

define it by its solubility characteristics rather than structural characteristics

Front 37

Are lipids hard to break down?

Back 37

yes

Front 38

3 major groups of lipids name them and list the units that they each consist of.

Back 38

fats/oils- glycerol & 3 fatty acids
phospholipids- Glycerol, 2 fatty acids & phosphate
steroids- contains core consisting of 4 fused carbon rings

Front 39

why are fats and oils important for warm blooded animals

Back 39

provides long-term energy storage and thermal insulation

Front 40

a fat or oil is chemically known as a _________________

Back 40

triglyceride

Front 41

what is the difference and similarity b/w fat and oil

Back 41

fat=solid at room temp. usually from animals
oil=liquid at room temp. from plants (except fish oil)
similar since have high C-H bonds insoluble in water.

Front 42

what does triglyceride consist of and what links them

Back 42

glycerol joined to 3 fatty acids molecules by ester linkages

Front 43

what does one fatty acid generally consist of

Back 43

organic acid (carboxyl)
hydrocarbon chain ( 4-24 carbons)

Front 44

classification of fats/oils and give brief explanation.

Back 44

saturated- fat which fatty acid hydrocarbon chain contains all single bonds and maximum # hydrogen atoms
mono unsaturated- fatty acid hydocarbon chain contains one double bond and less than max # of hydrogen atoms
poly unsaturated- fatty acid hydrocarbon chain contains two or more double bonds less than max # hydrogen atoms

Front 45

give an example of saturated, mono saturated and polysaturated

Back 45

Butyric acid- satur
Oleic acid- mono unsat
Linoleic acid-poly unsat

Front 46

why are plant fats (oils) easier to break down than animal fats?

Back 46

plant oils have double bonds animals fats do not have double bonds (carbon) and therefore harder break down

Front 47

where can phospholipids be found

Back 47

cell membranes

Front 48

which end of a phospholipids water soluble and insoluble

Back 48

phosphate end is polar so hyro-philic
hydrocarbon (chain) end of fatty acid is non-polar hydrophobic repels water

Front 49

4 ring steroid have ____ carbons

Back 49

17

Front 50

Is it true that steroids have 4 fused six ring carbons?

Back 50

no has 3 rings of 6 carbons and 1 ring 5 carbons

Front 51

what accounts for the difference b/w the various steroids?

Back 51

hydrogen atoms and functional groups that extend from the carbon core

Front 52

name 4 types of steriods

Back 52

Testosterone, Cortisone, Vitamin D, Cholesterol

Front 53

what is a sterol

Back 53

it has one or more OH groups in the molecule

Front 54

what is the most abundant sterol in humans

Back 54

cholesterol is an important part of cell membranes also associated w/ heart disease and circulatory probs.

Front 55

what do proteins consist of

Back 55

carbon, oxygen, hydrogen, nitrogen, sometimes sulphur occasionally phosphorus, and certain trace elements

Front 56

Is it true that proteins provide most nitrogen in body of animal

Back 56

yes

Front 57

There are nine important roles of proteins name them their function and give examples

Back 57

structural-support-keratin,collagen,elastin
storage-storage animo acids-ovalbumin
transport-transport of substances(gases)-hemoglobin
Hormonal-control body fun.-insulin
contractile(muscle)-movement-actin&myosin
defensive-protection against disease-antibodies
enzymatic-acceleration chem. reactions-maltase,sucrase,lactase
Pigment-respond light-Melanin
Clotting-blood clotting-prothrombin

Front 58

True or false a protein is a chain of animo acids consisting of 4 parts bonded covalently to the same central carbon atom.

Back 58

true

Front 59

what are the 4 parts of an amino acid

Back 59

carboxyl (organic acid)(C bond OH doubleb O)
amino group (NsubH)
carbon
R group

Front 60

what distinguishes b/w the animo acids

Back 60

R group

Front 61

how many different R groups commonly found in proteins

Back 61

20

Front 62

It is true that there are then 20 different amino acids which vary in shape, size, charge but same chemical properties

Back 62

true except different chemical properties

Front 63

what amino acid is referred to an imino acid? why?

Back 63

proline nitrogen atom bonded to two carbon atoms instead of bonded to usual one carbon atom.

Front 64

name the three aromatic amino acids

Back 64

Phenyl-alanine, Tryptophan, Tyrosine

Front 65

protein is a chain of amino acids joined together by_____________ b/w the carboxyl group of one amino acid to the amino group of another amino acid

Back 65

pep-tide bonds (amide linkage)

Front 66

each amino acid is known as a ____________. Therefore two of them make a __________________.

Back 66

Peptide unit
dipeptide

Front 67

Is a molecule comprised of 51 or more amino acids called a polypeptide?

Back 67

no it is a protein and poly peptide consists of 4-50 amino acids.

Front 68

Proteins consists of _____________ amino acids. On average proteins consist of approx.__________ amino acids.

Back 68

51-500
200

Front 69

Name the 4 different levels of structure of protein and give brief description.

Back 69

primary-sequence amino acids in poly peptide stabilized by peptide bonds
secondary-,globular shape, alpha helices and beta pleated sheets hydrogen bonding b/w groups along peptide bonded backbone
tertiary-called polypeptide unit, 3D shape, ionic covalent in addition to hydrogen bonding b/w R groups or peptide bonded backbone
quaternary- shape produced by combinations polypeptides bonds b/w R groups b/w peptide backbones different poly peptide

Example Hemoglobin

Front 70

what is a catalyst?

Back 70

substance increases speed of chemical reaction w/o itself being used in the chemical reaction.

Front 71

what is an enzyme called in living cells.

Back 71

Biological catalyst

Front 72

how are enzymes able to speed up chemical reactions?

Back 72

by lowering activation energy needed for reaction to take place.

Front 73

define activation energy

Back 73

initial energy needed for the chemical reaction to take place

Front 74

when enzymes act upon molecules the molecules are called _______________

Back 74

substrates

Front 75

can an enzyme act on any substrate

Back 75

no acts upon specific substrate known as enzyme specificity

Front 76

the site where the substrate temporarily joins with the enzyme is called __________________

Back 76

active site

Front 77

Give three steps to lock and key model.

Back 77

1. enzyme protein molecule w/ specific 3D shape due to tertiary structure match up w/ specific substrate.
2.enzyme bounds to substrate at active site by hydro.bonds forms enzyme substrate complex enzyme lowers activation energy needed by substrate to break apart
3.substrate broken into two products enzyme is released and ready start again.

Front 78

Apparently the active site is flexible and not rigid what is the name of the modified version of lock key?

Back 78

Induced fit model- active site forms complementary shape to substrate after binding

Front 79

4 factors affect enzyme activity name them

Back 79

pH
substrate concentration
Enzyme concentration
Temperature

Front 80

If temperature increases what happens to the enzymes and substrates

Back 80

more kinetic energy they move faster.

Front 81

If enzymes move faster will more collisions be likely to occur

Back 81

yes

Front 82

what is optimal temp. what is the opt temp of enzyme human body?

Back 82

temp at which enzyme works its best where balance b/w enzyme stability and kinetic energy. opt temp is 37 degrees human body.

Front 83

what happens when you go over optimal temp for enzyme?

Back 83

protein enzyme begins to break down during a process called denaturation. hydrogen, ionic and covalent bonds break down at high temp destroying active site of enzymes becoming irreversibly inactivated