Grade 12 Bio Unit Test:1

Front 1

What is Biology

Back 1

the study of living things

Front 2

What do living things do?

Back 2

use energy, reproduce, grow, respond to stimuli, produce waste

Front 3

Metabolisim

Back 3

All chemical reactions of an organisim

Front 4

Anabolism

Back 4

is the building of complex molecules from simplier ones. with an input of energy.

Front 5

Catabolisim

Back 5

is the building of complex molecules into simpler ones with an output of energy.

Front 6

All chemicals of life consist mostly of

Back 6

Carbon

Front 7

Isotope

Back 7

Elements that contain different numbers of neutrons. Same atomic mass but different mass number.

Front 8

radioisotope

Back 8

radioactive atoms of an element that spontaneously decay into smaller atoms, subatomic particles and energy. Nuclear charge to a different movement.

Front 9

Half-life

Back 9

The time it takes for one half of the nuclei in a radioactive sample to decay.

Front 10

Intramolecular

Back 10

Bonds within molecules.

2 types: ionic and covalent

Front 11

Ion

Back 11

A charged atom (has to lose or gain electrons)

Front 12

Molecule

Back 12

A particle with two or more atoms combined with a covalent bond.

Front 13

Electronegativity

Back 13

A number that indicates how much an atom likes electrons. Scale of 0-4. Metals low. Non-metals high.

Front 14

Ionic Bonds

Back 14

-Metal and nonmetal.

- Transfer of electrons (metals give to nonmetal). -Electrostatic forces of attraction (no physical bond).

-Large difference in En

-Forms ionic compounds

Front 15

Covalent Bonds

Back 15

-between 2 nonmetals

-sharing of electrons

-physical bond that forms molecules

- small difference in En

-forms molecular compounds.

-2 types: pure, polar

Front 16

Pure Covalent Bonds

Back 16

-Electrons are shared equally

- En is the same

ie: Cl2

Front 17

Polar Covalent Bonds

Back 17

-Electrons are shared unequally

- En is different

-partial charges -ve & +ve

ie: HCl

Front 18

Molecular Polarity

Back 18

-If it has a +ve and a -ve that can be split it is a polar molecule

-If -ve & +ve cannot be identified then it is a non polar molecule.

Front 19

Intermolecular

Back 19

-Forces between molecules

-3 types: London dispersion, dipole-dipole & H-bond

Front 20

London dispersion

Back 20

-realatively weak between all molecules.

ie: O=O London dispersion O=O

Front 21

Dipole-Dipole

Back 21

-Attractive forces acting between polar molecules

-The +ve end of the molecule attracts the -ve of another molecule.

ie: H-Cl dipole-dipole H-Cl

Front 22

Hydrogen- Bonds

Back 22

-A realitively strong force between a S+ hydrogen on one molecule and S- on O,F, or N.

-water has h-bonds

ie: H-O-H Hydrogen bond H-O-H

Front 23

Water

Back 23

-Water is small, forms H-bonds, polar causes heating & cooling very slowly.

- density, why ice floats on water (solid is less dense than liquid.

-Cohesion and Adhesion (why a full glass does not overflow thanks to H-bonds)

Front 24

Solubility in ionic compounds

Back 24

-Water dissociates ionic bonds (breaks them apart).

ie: NaCl

Front 25

Solubility in molecular compounds:polar

Back 25

-Water surrounds polar molecules and creates d-d or h-bonds.

Front 26

Solubility in molecular compounds: non-polar

Back 26

-Non-polar molecule

-only london dispersion

-water will bond with itself and push out non-polar substance

-therefore insouluble

BUT NON-POLAR WILL DISSOLVE IN NON-POLAR

Front 27

Neutralitzation reaction

Back 27

Occurs in water whenever acid is mixed with a base. In these reactions water and salt is produced; salt is ionic.

Front 28

Buffer

Back 28

A chemical system that can donate H+ and take up H+, prevents changes in pH, the base gets neutralized by the buffer.

Front 29

Acids

Back 29

- A substance that when in a solution increase the concentration of Hydronium.

-Sour taste, conductable, turns blue litmus paper red.

Front 30

Bases

Back 30

A substance that when is a solution increases the concentration of hydroxcide.

Front 31

Macromolecules

Back 31

-polymers (long chains) made up of monomers.process is called polymerization.

- 4 major classes of biological macromolecules

1.Carbohydrates -> Monosaccarides

2.Lipids -> fatty acids + glycerol

3. Proteins -> amino acids

4. nucleic acid -> nucleotides

Front 32

Condensation Reactions

Back 32

- A reaction that creates a covalent bond between two internal subunits, linking them together, produces water molecules.

-also called dehydration synthesis

Front 33

Hydrolysis

Back 33

A catabolic recation in which a water molecule is used to break a covalent bond holding subunits together.

Front 34

Functional Group

Back 34

Reactive clusters of atoms attached to the carbon backbone of organic molecules.

Front 35

Carbohydrates

Back 35

are composed of the elements C,H,O. In a ratio of 1:2:1.

-are monosaccarides, disaccarides, polysaccarides usually ends in ose with the exception of startch.

1. glucose- made in photosynthesis by plants, fuel for cellular respiration

2. fructose- honey and fruit sugar

3.ribose- part of the structure in nucleic acids

Front 36

Isomers

Back 36

chemicals with the same chemical formula but different structure.

ie: glucose, galactose and fructose have the same formula C6H12O6 but a different arrangement.

Front 37

Disaccarides

Back 37

- double sugar formed wen two monosaccarides join.

-linkage between two molecules is called a glycosidic linkage.

Front 38

Polysaccarides

Back 38

-Two main functions are storage and structure

-They are many monosaccaride units condensed into huge macrosmolecules.

- 4 Types:

1. Startch - found in plants used for storage energy 2 types: amylose and amylopectin.

2. Cellulose- found in plants used for structure

3.Glycogen- found in animals used for storage in liver.

4.Chitin- found in exoskeletons. used in contacts and stitches.

Front 39

Lipids

Back 39

-Lipids contain C,H & O

-main function is for energy storage

-insulation

- hormones

- vitaman absorption

-protection of internal organs

-cell membrane

- 3 types, fats oils and waxes, steriods, and phospholipids,

Front 40

Fats oils and waxes

Back 40

-Triglyceride formed from 3 fatty acids and glycerol

-formed through a condensation reaction, liked by an ester linkage.

Front 41

Unsaturated vs Saturated

Back 41

double bond makes a higher boiling point and unsaturated.

Front 42

Phospolipid

Back 42

lipid with a phosphate group

Front 43

Steroids

Back 43

Cholesterol and sex hormones

Front 44

Proteins

Back 44

- 3-D shape ***

-made up of amino acids

-composed of C,H,O,N and S

Front 45

Protein functions

Back 45

-Enzyme-catalysts that regulate metabolisim

-Structure- hair, membranes, muscles

-Messenger- hormones

-Transport- carry materials around body

-antibodies- defend the body

-Energy- food reserves

Front 46

Amino Acids

Back 46

- 20 different, 8 esssiental

-the sequence for amino acids is found in DNA

-bond that is formed between 2 amino acids is called a peptide bond.

Front 47

Protein Structure

Back 47

Key feature is its shape which is determined by the sequence of amino acids and the interactions of the H,O,N and R side chains.

Front 48

Primary structure

Back 48

-All copies of a polypeptide of the same protein are the same. Can H-bond with itself.

Front 49

Secondary Structure

Back 49

-Usually takes form of a helix or pleated sheets. (caused by hydrogen bonds between H and O)

Front 50

Teritary Structure

Back 50

Super coiling of a polypeptide that is stabilized by side chain, R side chain interactions such as covalent bonds.

Front 51

Quaternary Structure

Back 51

Includes the bonding of a non-protein (ie metal ion iron and hemoglobin) This proteins consists of 4 polypeptides and an iron atom.

Front 52

Amino acid side groups

Back 52

- can make the molecule polar, nonpolar, electrically charged, acidic, basic.

- These groups determine the teritary structure of a protein.

Front 53

Cell Membrane

Back 53

- Seperates cytoplasam and ECF.

-controls what enters/exits the cell