Grade 12 Biology Mr.ferguson

Front 1

Chemical Terminology

Back 1

Chemistry terms

Front 2

Atomic Number

Back 2

Number of protons

Front 3

Atomic Mass

Back 3

Sum of protons and neutrons

Front 4

Element

Back 4

Smallest form of matter that cannot be broken down

Front 5

Molecule

Back 5

2 or more atoms

Front 6

Diatomic Molecule

Back 6

2 of the same Atoms. HOFBrNCl

Front 7

Physical Change

Back 7

Change of state

Front 8

Chemical change

Back 8

Change in substance

Front 9

Metal

Back 9

Left side of the staircase

Front 10

Non-Metal

Back 10

Right side of the staircase

Front 11

Metalloid

Back 11

On the staircase

Front 12

Molecular Formula

Back 12

Balanced chemical formula

Front 13

Covalent Bond

Back 13

Sharing of electrons between 2 or more non metals. Ex: Carbon has 4 bonds.

Front 14

Ionic Bond

Back 14

Transfer of electrons from a metal to a non-metal. Electrostatic bond

Front 15

Polar Molecule

Back 15

Molecules that have regions of different charge.

Front 16

Hydrogen Bond

Back 16

Bond between two water molecules.

Front 17

Acid

Back 17

Proton donor.pH 0-6.9

Front 18

Base

Back 18

Proton acceptor. pH 7.1-14

Front 19

Solute

Back 19

What is dissolved in the solution.

Front 20

Solvent

Back 20

What does the dissolving. (#1 water, #2 alcohol)

Front 21

Solution

Back 21

Solvent+solute

Front 22

Valence Orbital

Back 22

Outer most orbital of an element.

Front 23

Alkali Metals

Back 23

Group 1

Front 24

Alkaline Metals

Back 24

Group 2

Front 25

Halogens

Back 25

Group 17

Front 26

Inert gas (Noble Gases)

Back 26

Group 18

Front 27

Ions

Back 27

Addition or reduction in electron numbers. -1 plus electrons, +1 reduce electrons

Front 28

Isotopes

Back 28

Generally increase in the neutron number.

Front 29

Isomers

Back 29

Same molecular formula, different structural formula.

Front 30

Non-polar molecule

Back 30

Equal charge throughout the molecule. Diatomic molecule

Front 31

Hydrocarbon

Back 31

Molecule composed of hydrogen and carbon atoms.

Front 32

Organic

Back 32

Hydrogen, oxygen, carbon, phosphorus, nitrogen, sulfur

Front 33

Buffer

Back 33

Resist changes in pH

Front 34

Electronegativity

Back 34

An atoms attraction for its electrons. Ex: Fluorine is the most reactive.

Front 35

Universal Solvent

Back 35

Water. It dissolves substances that are polar.

Front 36

Cohesion

Back 36

Water binds to water.

Front 37

Adhesion

Back 37

Water binds to other substances.

Front 38

Temperature Moderation

Back 38

Specific heat capacity that takes a lot of energy to change.

Front 39

Anomalous Behaviour

Back 39

Water will expand when cooling between the temperatures of 4 degrees and 0 degrees.

Front 40

Surface Tension

Back 40

Things don't sink on water. Ex: Boats and aquatic bugs.

Front 41

Carbon

Back 41

Can make 4 bonds. Fairly reactive. Can form single, double, triple bonds. Can form straight chains or rings.

Front 42

Alkanes

Back 42

Hydrocarbon with single bonds in the parent chain.

Front 43

Alkenes

Back 43

Hydrocarbon with one or more double bonds in the parent chain.

Front 44

Alkyne

Back 44

Hydrocarbon with one or more triple bonds in the parent chain.

Front 45

Alcohol (hydroxyl group)

Back 45

A hydrocarbon with an OH group attached to the parent chain.

Front 46

Ketone (Carbonyl group)

Back 46

Oxygen molecule double bonded to the middle of a hydrocarbon parent chain.

Front 47

Aldehyde (Carbonyl group)

Back 47

Oxygen molecule double bonded to the end of a hydrocarbon parent chain.

Front 48

Carboxylic Acid (Carboxyl group)

Back 48

Carbon atom double bonded to an oxygen atom and single bonded to a hydroxyl group (OH). Ex: Fatty acids, citric acids, and pyruvic acids. At the end of a parent chain.

Front 49

Amine Group

Back 49

Nitrogen attached to the parent chain with two hydrogen atoms bonded to it. Amide bonds. Prefix amino

Front 50

Sulfhydryl Group

Back 50

Sulfur atom bonded to a hydrogen atom. Thial (SH)

Front 51

Phosphate Group

Back 51

Phosphate atom with one single bonded oxygen and one double bonded oxygen plus two single bonded oxygen ions.

Front 52

Anabolic Reactions

Back 52

Involves the construction of larger molecules.

Front 53

Catabolic Reactions

Back 53

Involves the breakdown of macromolecules into subunits.

Front 54

Condensation/dehydration synthesis

Back 54

Two molecules combine through covalent bonding, producing water

Front 55

Hydrolysis

Back 55

Covalent bond of a molecule breaks, a water molecule separates into H and OH and attaches to the exposed sites.

Front 56

Enzymes

Back 56

Biological catalyst that are produced by living systems to control the rates of reactions.

Front 57

Non-Polar Covalent Bonds

Back 57

Both atoms exert the same pull on the shared electrons.

Front 58

Carbohydrates

Back 58

Simple sugar or molecule composed of two or more sugar units. Contains C,H,O in a 1:2:1 ratio. Most abundant biological molecule.

Front 59

Monosaccharides

Back 59

Single molecule of sugar. One sugar unit that has at least two OH groups and a carbonyl group.Backbone of 5 or 6 carbon atoms.

Glucose, galactose, fructose, deoxyribose, and ribose.

Front 60

Disaccharides

Back 60

Short chain of two or three sugar units covalently bonded through glycosidic linkages. Formed by dehydration synthesis/condensation (remove an oxygen). Lactose (glucose+galactose), sucrose (glucose+fructose), and maltose (two glucose).

Front 61

Polysaccharides

Back 61

Straight or branched chain of sugar units.

Starch: large carbohydrate composed of many Glucose molecules. Plants store excess sugar as starch in roots and stems.

Cellulose: used as structural material in cell walls. *not in humans

Glycogen: Sugar storage molecule in animals.

Chitin: main structural material in external skeletons.

Amylose

Front 62

Lipids

Back 62

Fats, phospholipids, oils, and waxes. Made of glycerol and fatty acids.Long-term energy storage, provides 6 times as much energy as carbs. Provides structural support. Provides insulation (whale blubber).

Glycerol+Fatty Acid+Phophate

Front 63

Fatty Acids

Back 63

Contains 36 carbon atoms in its backbone, a carboxyl group at one end, and hydrogen atoms at most bonding sites.

Front 64

Unsaturated

Back 64

Contains one or more double bonds in carbon backbone. Weak intermolecular forces causes it to be liquid at room temperature and in the body (Plant Oils). Can be Hydrogenized- adding a hydrogen

Front 65

Saturated

Back 65

Contains only single bonds. Intermolecular forces are stronger making them firm and are associated with heart disease. (lard/butter)

Front 66

Neutral Fats (Triglycerides)

Back 66

Butter, lard, and oils. Aids in the absorption of vitamins, insulates the body, and protects delicate organs. Energy is released when bonds are broken and fats have more covalent bonds than carbs.

Front 67

Ester Linkage

Back 67

When alcohol reacts with a carboxylic acid. Glycerol and three fatty acids

Front 68

Phospholipids

Back 68

Two fatty acid tails and a hydrophilic head (with a phosphate group). Main component of the two lipid layers of cell membranes.

Front 69

Sterols

Back 69

Lipids with no fatty acid tails. Four-fused together carbon rings. Structural components of eukaryotic cell membranes (ex. cholesterol). Precursor of steroid hormones (testosterone and estrogen). Cholesterol is associated with heart disease and circulatory problems because of its shape.

Front 70

Waxes

Back 70

Long chains of fatty acids linked to long chain alcohols or carbon rings. (Ex. beeswax)

Front 71

Proteins

Back 71

Types of proteins:

Enzymes- make reactions proceed much faster

Structural Proteins- found in bones and cartilage

Transport protein- carry substances across the cells membrane.

Hormones- signals for change in cell activity

Immunity- white blood cells

Lowering activation energy

Makes up hair, skin, and fingernails

Front 72

Amino Acids

Back 72

Protein is made from combinations of 20 amino acids. 8 are essential meaning they cannot be made in our bodies. Made from an amino group, a carboxyl group, a hydrogen and one or more side chains (R group).

R Groups- all parts are covalently bonded to the same C atom.

Front 73

Amide Linkage

Back 73

When a carboxylic acid reacts with an amine.

Front 74

Peptide bonds

Back 74

Through a process called protein synthesis amino acids are linked together by...

Front 75

Polypeptide Chain

Back 75

When three or more amino acids are joined together. The sequence of each amino acid is unique to each protein and represents the primary structure.

Front 76

Fibrous Protein Shape

Back 76

Polypeptide chains organized in strands or sheets. Important to the shape, internal organization, and movement of the cells.

Front 77

Globular Protein Shape

Back 77

Polypeptide chains folded into a compact rounded shape.

Front 78

Primary Structure

Back 78

The unique sequence of amino acids in a polypeptide chain.

VASO Pressin- constricts blood vessels. 7 amino acids long and it is the longest chain.

There are an infinite number of polypeptides that can be produced from 20 amino acids.

Front 79

Secondary Structure

Back 79

Coiling and folds in a polypeptide caused by hydrogen bonds between between atoms near the peptide bonds.

Alpha Helix or B Pleated sheet

Kratin- hair, Collagen- Skin, Silk- Spiders and worms, Elastin- skin.

Front 80

Tertiary Structure

Back 80

Formed by interactions among the R groups. Myoglobin (whales, dolphins have a lot)-

To carry oxygen in the blood

Front 81

Quaternary Structure

Back 81

Formed by incorporating two or more polypeptide chains. 2 or more tertiary structures put together.

Hemoglobin in humans transports oxygen in the blood. Can bond to 4 oxygens.

Front 82

Denaturation

Back 82

Protein Changes shape and now loses its function.

Front 83

Nucleic Acid

Back 83

Stores hereditary information that determines the structure and function of living things.

Front 84

DNA

Back 84

Deoxyribonucleic acid. Where hereditary info is stored. Double stranded held together by hydrogen bonds.

A, T, G, and C

Front 85

RNA

Back 85

Ribonucleic acid reads the DNA and transports the instructions for making protein to the ribosomes in the cell.

A, G, U, and C

Front 86

Nucleotide Polymers

Back 86

DNA and RNA. Consist of 5 carbon sugar (ribose or deoxyribose), a phosphate group, and a nitrogenous base.

Front 87

Double ring Purines Nitrogenous Base

Back 87

A- Adenine and G- Guanine

Front 88

Single ring Pyrimidines Nitrogenous Base

Back 88

C- Cytosine and T- Thymine and U- Uracil

Front 89

ATP

Back 89

Adenosine Triphosphate is a nucleotide used to deliver energy from one reaction site to any other.

Front 90

Activation Energy

Back 90

The energy required to initiate a chemical reaction.

Front 91

Catalyst

Back 91

A substance that speeds up a chemical reaction by lowering the activation energy.

Front 92

Enzyme

Back 92

Protein that speeds up (catalyzes) a chemical reaction.

Front 93

Active Site (Maltose Enzyme)

Back 93

On enzyme where substrate binds.

Front 94

Inhibitor

Back 94

Molecule that binds to the active site or allosteric site. Does not allow the enzyme to function properly.

Front 95

Activator

Back 95

Molecule that binds to the alloseric site.

Front 96

Competitive Inhibitor

Back 96

Binds to the active site so substrate cannot bind.

Front 97

Non-competitive Inhibitor

Back 97

Binds to Allosteric site and denatures the enzyme so it cannot bind to the substrate. More dangerous.

Front 98

Enzyme Catalase

Back 98

Works on hydrogen peroxide.

Front 99

3 Factors From Enzyme Lab

Back 99

pH, Temperature, and Surface Area affect the enzymes activity.

Front 100

Glycosidic Linkage

Back 100

Covalent bonds between monosaccharides.