AP Biology - Unit 1: BioChemistry (Overall Summary)

What are the elements of life

What are the elements of life

CHNOPS (carbon, hydrogen, nitrogen, oxygen, phosphorus, sulfur)

3 types of intramolecular bonds

1. Ionic bond

2. Polar covalent bond

3. Nonpolar covalent bond

Polar covalent bond

unequal sharing of electrons (one has more electronegativity)

6 properties of water

cohesion, adhesion, Universal solvent, hydrophobic, ice expands, high heat capacity

cohesion (water)

water attracts water

adhesion (water)

Water sticks to any surface that is polar or has exposed nitrogens or oxygens.

Universal solvent (water)

Most substances dissolve in it (because of polarity)

Hydrophobic reactions (water)

compartmentalization

does ice expand?

yes

high heat capacity

hydrogen bonds are so strong it takes a lot of heat to break them

functional group

a group of molecules that are responsible for organic molecules functional properties

hydroxyl

R-OH (polar)

Carbonyl (aldehyde)

C=O at end of molecule (polar)

Carbonyl (keytones)

C=O in the middle

Carboxylic Acid

R-COOH (acidic/polar)

Amino

H-N-H (basic/polar)

Phosphate group

PO4 (acidic/polar)

sulfhydrl

S-H (polar)

methyl group

A chemical group consisting of a carbon atom bonded to three hydrogen atoms.

Macro-Molecules

carbohydrates, lipids, proteins, nucleic acids

ending suffix of carbohydrates

-ose

carbohydrate functions

energy storage and structure

elements in carbohydrates

carbon, hydrogen, oxygen (1:2:1)

structure of carbohydrates

hexagon/pentagon, hydroxyl,

carbohydrate properties

polar, hydrophilic

condensation/dehydration synthesis

building polymers

hydrolysis

breakdown of polymers

mono-sacchride examples

glucose, fructose, galactose

di-sacchride examples

sucrose, lactose, maltose

poly-sacchride examples

starch (amylose), glycogen (stored sugar), fiber (cellulose)

Lipid examples

fats, oils, waxes, cholesterol

3 types of lipid polymer

tri-glycerides, phospholipids, cholesteral

Lipid elements

C, H, O (no ratio)

lipid properties

non-polar, no monomers

tri-glyceride components

glycerol + fatty acids

types of triglycerides

saturated and unsaturated fats

functions of triglycerides

energy storage, insulation, protection

phosophlipid components

phosphate group + glycerol + fatty acid

phospholipid function

cell membranes

cholesterol function

cell integrity, horomones, health

cholesterol properties

hydrophobic, non-polar

nucleic acid elements

C, H, O, N, P

nucleic acid monomer

nucleotides

nucleic acid properties

polar, hydrophilic

nucleic acid polymers

DNA and RNA

DNA properties

double helix, missing O-

Rna properties

Single helix, has O-

protien elements

C,H,O,N,S

protien monomer

amino acids

amino acid structure

amino group - central carbon + R group - carboxylic group

How many types of amino acids are there?

20

How many amino acids are essential?

9

what does the amino acid R-group dettermine?

the type of amino acid

what are amino acids connected with

di-peptide bonds

how many protien structure levels are there

4

whats the first protien structure level

primary protein structure: chain of amino acid, order determines final protein structure

whats the second protien structure level

secondary protien structure: amino chain folds on itself, held together with hydrogen bond, either pleated sheet or helix

whats the third protien structure level

tertiary protien structure: R-group interations, technically a protien, held with h-bond, ionic bond or di-sulfide bridge

whats the forth protien structure level

quaternary protien structure: R-group interations, globular protien, contains subgroups/subunits (tertiary connected with eachother)

what is protien denaturization?

loss of 3rd and 4th structure/R-group interations

causes or denaturation

heat and pH

What is an enzyme?

type of protien, biological catalyst, needed for all cellular proccesses

enzyme suffix

-ase

what the lock and key hypothesis

the shape of the enzyme must match the shape of the substrate in order to synthesize/digest the substrate

synthesize

build

digest

break down

substrate

reactant of an enzyme-catalyzed reaction

active site

The part of an enzyme reaction occurs.

conformational change

an alteration of the enzyme structure that impacts that protein's function

competitive inhibitor

A substance that reduces the activity of an enzyme by entering the active site in place of the substrate whose structure it mimics.

non-competitve inhibitor

A molecule that binds to the allosteric site of an enzyme, changing it's tertiary structure and shape of the active site so that the substrate can no longer fit

allosteric site

A specific receptor site on some part of an enzyme molecule remote from the active site.

cofactors (inorganic)

minerals, ions

coenzymes (organic)

vitamins

purpose of cofactors and coenzymes

help the enzymes

metabolism

sum of all of the chemical reactions that occur within an organism

4 factors that affect enzyme rate

pH, Temperature, substrate concentration, enzyme concentration.