Topic 1-The Biology Of Life

Front 1

What 4 Chemicals make up 96% of living matter?

Back 1

Carbon, Hydrogen, Oxygen, and Nitrogen

Front 2

What are the 3 subatomic particles and their structure

Back 2

protons(positive) and neutrons (neutral) in nucleus
electrons (negative) orbiting

Front 3

atomic number

Back 3

number of protons of an element

Front 4

atomic mass

Back 4

sum of protons and neutrons

Front 5

What are the 5 types of bonds in order of strength from strongest to weakest

Back 5

Nonpolar covalent, polar covalent, ionic, hydrogen, Van der Waals

Front 6

two types of covalent bonds

Back 6

nonpolar covalent- electrons are shared equally between atoms
polar covalent- electrons are shared unequally (water)

Front 7

What are Ionic bonds

Back 7

Attraction of two ions because one will be positively charged and the other negatively charged

Front 8

Hydrogen Bonds

Back 8

relatively weak bonds between hydrogen of one molecule and the oxygen or nitrogen of another molecule

Front 9

Van der Waals interactions

Back 9

very weak connections between molecules that help with 3D shape of large molecules

Front 10

What are the properties of water?

Back 10

Cohesion, Adhesion, High Specific Heat, Ice is less dense than water, universal solvent

Front 11

Cohesion, Adhesion and their importance

Back 11

Cohesion- Water sticking to itself
Adhesion- Water sticking to other objects
Transpiration uses these to pull water up in xylem

Front 12

High Specific heat and importance

Back 12

the amount of heat required to raise or lower the temperature of a substance 1 degree Celsius
Earth's Oceans are stable enough for plant and animal life

Front 13

Less Dense ice and importance

Back 13

Ice acts as an insulator to oceans to moderate temperature underneath

Front 14

Universal Solvent

Back 14

dissolves hyrdophilic- ionic compounds, polar molecules, and proteins
hydrophoic- oils and nonpolar substances do not dissolve

Front 15

Buffers in living systems

Back 15

buffers- substances that minimizes changes in pH by accepting or donating hydrogen
Carbonic Acid H2CO3- moderates blood pH and oceans

Front 16

Hydroxyl group

Back 16

-OH
alcohols like ethanol, methanol; helps dissolve sugars

Front 17

Carboxyl group

Back 17

-COOH: carboxylic acids such as fatty acids and sugars

Front 18

Carbonyl group

Back 18

--CO
ketones and aldehydes like sugars

Front 19

Amino group

Back 19

-NH2
amino acids

Front 20

Phosphate group

Back 20

PO3
Organic phosphates, ATP, DNA, phospholipids

Front 21

Sulfhydryl

Back 21

-SH
some amino acids, disulfide bridges in proteins

Front 22

Dehydration Synthesis

Back 22

creating polymers from monomers by removing a molecule of water

Front 23

Hydrolysis

Back 23

water is added to split large molecules

Front 24

Carbohydrates

Back 24

exists in a 1 carbon:2 hydrogen: 1 Oxygen ratio
sugars(glucose, fructose)
polymers (starch)

Front 25

two functions of polysaccharides

Back 25

energy storage- starch in plants, glycogen in animals
structural support- cellulose in plants, chitin in arthropods, insects, and fungi

Front 26

4 types of lipids

Back 26

waxes, oils, fats, steroids

Front 27

Fat structure (triglyceride)

Back 27

made of glycerol molecule and 3 fatty acid chains

Front 28

Types of fatty acids

Back 28

saturated- no double bonds, solid, made by animals
unsaturated- at least one double bond,liquid, made in plants

Front 29

Function of fats

Back 29

Energy storage- twice calorie amount of carbs
protection and insulation in the body

Front 30

phospholipids

Back 30

glycerol and phosphate head and two fatty acids tails
form the cell membrane

Front 31

steroid structure and examples

Back 31

4 carbon rings fused together
cholesterol in cell membranes
estrogen and testosterone- steroid hormones

Front 32

Protein Structure

Back 32

Amino acids linked by peptide bonds
amino acids- central carbon with an amino group, carboxyl group, hydrogen and r group

Front 33

4 levels of protein structure

Back 33

primary- order of amino acids
secondary- beta pleats and alpha helix
tertiary structure- globular shape from hydrogen bonds, disulfide bridges, Van der Waals
quaternary-two or more polypeptide chains linked

Front 34

protein vs. function malfunction example

Back 34

sickle cell disease- results with a single amino acid substitution which changes the shape of the hemoglobin