Purple Pages

Front 1

What are the four major macromolecules of life?

Back 1

Proteins, Nucleic Acids, Lipids and Hydrocarbons

Front 2

Structure defines ___________.

Back 2

Function

Front 3

What is an isomer? Give an example.

Back 3

An isomer is a molecule with the same formula as another molecule but a different structure ie: glucose and fructose.

Front 4

Why is water so important to life?

Back 4

Water does not change forms relatively fast, and so exists mostly in liquid form. Its liquid form is better suited to harbour life due to its excellent solvent characteristics (hydration shell) and high specific heat capacity.

It is less dense in its solid form, which allows it to float. The attraction between water molecules causes a phenomenon known as cohesion, which allows water to move against the force of gravity.

Hint 4

Temperature

Front 5

What are the intermolecular and intramolecular forces studied in Biology?

Back 5

Hydrogen bonding, van Der Waals forces, ionic forces, covalent forces.

Front 6

What are the four steps of the scientific method?

Back 6

1. Characterisation

2. Hypothesis

3. Experimentation

4. Interpretation of Results

Front 7

A hypothesis must be _______ & ________.

Back 7

Falsifiable & testable

Front 8

An ________ variable is changed by the scientist. A _________ variable responds to changes in the ___________ variable. A controlled variable remains _________.

Back 8

Independent, dependent, independent & constant

Front 9

True or false: a light microscope is capable of viewing objects below a 100 nm in diametre.

Back 9

False; only electron microscopes

Front 10

The ________ is the basic unit of life.

Back 10

Cell

Front 11

What 4 elements make up 90% of matter in living organisms?

Back 11

Hydrogen

Oxygen

Nitrogen

Carbon

Front 12

Why are organisms different from each other in terms of functions and appearances?

Back 12

Different structures, proportions and arrangements of atoms.

Front 13

What is an isotope?

Back 13

Atom with same number of protons but different number of neutrons

Front 14

What are radioisotopes and why are they used in medicine?

Back 14

1. Unstable isotopes that decay and release energy

2. Energy is then used to measure speed of chemical processes or movemeny of substance ie diagnostics

Front 15

What nuclear reactor produces 30-40% of radioisotopes globally?

Back 15

Chalk river reactor in Canada

Front 16

Electrons move around protons in regions called __________, which are grouped in ______.

Back 16

Orbitals, shells

Front 17

The unequal sharing of electrons creates a ________ ________ bond.

Back 17

Polar covalent

Front 18

Hydrogen bonding helps with what in proteins?

Back 18

Creating 3D structure

Front 19

What are van der Waals forces?

Back 19

They are forces that develop between nonpolar molecules through the constant motion of electrons. This causes zones of positive and negative charges.

Front 20

What are buffers? Name an example.

Back 20

Buffers control pH of our blood ie dissociation of carbonic acid

Front 21

Name all important biological functional groups.

Back 21

Hydroxyl (-OH)

Carbonyl (-C=O)

Carboxyl (-COOH)

Amino (-NH2)

Phosphate (-PO4^2-)

Sulfhydryl (-SH)

Hint 21

There are 6

1) (-SH)

Front 22

Which type of reaction synthesizes a polymer? Which one breaks down a polymer?

Back 22

1. Dehydration

2. Hydrolysis

Front 23

What is the difference between a-glucose and b-glucose?

Back 23

Their structures differentiate them from each other and give them different functions. They are enantiomers. A-glucose (starch) is digestible while b-glucose (cellulose) is not.

Front 24

The base monomer of a carbohydrate is a __________. Many of these in a chain create a ________.

Back 24

Monosaccharide; polysaccharide

Front 25

Glucose + glucose = 1

Glucose + fructose = 2

Glucose + galactose = 3

Back 25

1. Maltose

2. Sucrose

3. Lactose

Front 26

Name the glycosidic linkages.

Back 26

Linear; branched; h-bonds; n-groups

Front 27

What are the different functions of proteins?

Back 27

Structural support

Storage

Transport

Enzymes in reactions

Cellular comms

Movement

Front 28

What is the basic structure of an amino acid?

Back 28

Amino group, side group and carboxyl group

Front 29

What is the base unit of a protein and what is it made of?

Back 29

Polypeptide; amino acids

Front 30

Name the nonpolar amino acids

Back 30

Alanine (Ala)

Valine (Val)

Leucine (Leu)

Isoleucine (Ile)

Glycine (Gly)

Cysteine (Cys)

Phenylalanine (Phe)

Tryptophan (Trp)

Methionine (Met)

Proline (Pro)

Front 31

Name the uncharged polar amino acids

Back 31

Serine (Ser)

Threonine (Thr)

Tyrosine (Tyr)

Asparagine (Asn)

Glutamine (Gln)

Front 32

Name the negatively charge amino acids

Back 32

Aspartic acid (Asp)

Glutamic acid (Glu)

Front 33

Name the positively charged amino acids

Back 33

Lysine (Lys)

Arginine (Arg)

Histidine (His)

Front 34

Describe the 4 protein structures

Back 34

Primary = linear sequence, not much info, R groups do not participate

Secondary = Alpha helix or beta pleated sheets, H bonds between Nitrogen and Oxygen partial charges, R groups do not participate

Tertiary = folding, R groups participate, structure is defined and so function is given, various bonds cause folding ie hydrogen, disulfide bridge, ionic, hydrophobic interaction etc.

Quaternary = >2 polypeptides come together to create functional protein ie collagen. Can have cofactors such as heme to create protein ie hemoglobin

Front 35

What are the subdivisions of nucleic acids?

Back 35

DNA

RNA

rRNA

tRNA

mRNA

Front 36

What is the monomer of a nucleic acid and what is its structure?

Back 36

Nucleotide: nitrogenous base, pentose sugar, 1-3 phosphate groups

Front 37

What are the differences between RNA and DNA? Which nucleotides are used in energy transfer?

Back 37

DNA = desoxyribose, Thymine

RNA = ribose, Uracil

Adenine and Guanine

Front 38

What is the basic structure of DNA and RNA? How do you read them?

Back 38

2 nucleotide chains, sugar-phosphate backbone; phosphodiester bonds, H bonds, nitro bonds

From 5' to 3'

Front 39

What allows us to predict the opposing strand of a DNA molecule?

Back 39

Complementary strands: G-C, A-T (DNA) or A-U (RNA)

Front 40

Describe the structure of a lipid.

Back 40

Nonpolar molecule with long hydrocarbon chains. Double bond causes a kink in chain.

Front 41

Name the three categories of lipids.

Back 41

Fats

Phospholipids

Steroids

Front 42

Difference between saturated and unsaturated fats?

Back 42

Sat fats have no carbon double bonds (all bonds saturated) while unsat fats have one or more. This makes unsat fats less dense and therefore liquid at room temp.

Front 43

Describe basic structure of a fat.

Back 43

Glycerol + fatty acids + 3 hydrocarbon chains = triglyceride

Front 44

What is a phospholipid?

Back 44

Lipid that has polar hydrophilic phosphate end and nonpolar hydrophobic fatty acid end. Two-chain structure with one chain having a double bond.

Front 45

What is a steroid?

Back 45

4 carbon ring structure with dual solubility. It is base form of cholesterol. Many hormones are sterol-based ie testosterone, estrogen, etc.