AP Biology REVIEW

includes weird ways I remember stuff.... this is literally everything... or as much as I could put.... godspeed.

ionic bond

bond when electrons are transferred

covalent bond

co = share

bond when electrons are shared

polar

magnet poles are positive and negative, so they are…

not equal, hydrophilic

non polar

equal, hydrophobic

nonpolar covalent bond

covalent bond when electrons are shared equally

polar covalent bond

covalent bond where electrons are shared unequally

hydrogen bond

weak bond between a positive hydrogen and an electronegative atom, used for water’s adhesion, cohesion, surface tension

most common elements of life

CHONPS

carbon, hydrogen, oxygen, nitrogen, phosphorus, sulfur

water

• polar molecule/hydrophilic

• universal solvent

• less dense, so lakes don’t freeze solid

• high specific heat (takes a lot to make it go up a degree)

• causes transpiration in plants thanks to cohesion and adhesion

pH

pH level and amount of hydrogen ions are inverse

amount of hydrogen ions

acidic pH

dropping acid lowers pH

• high amount of hydrogen ions

• less than 7 pH

neutral pH

7 pH

basic pH

being based gets you more pH

• low amount of hydrogen ions

• more than 7 pH

about anabolic/catabolic and endergonic/exergonic reactions…

anabolic + endergonic: generally, creation takes energy

catabolic + exergonic: generally, destruction releases energy

anabolic

creating something

catabolic

catastrophes destroy

destroying something

endergonic

en = in

energy goes into the reaction

exergonic

ex = exit

energy exits the reaction

dehydration synthesis

dehydrate = get rid of water, synthesis = making something

releasing/getting rid of water to make a polymer

• anabolic = creation

• endergonic = energy into

hydrolysis

hydro = water, lysis = destruction

adding water to destroy something into monomers

• catabolic = destroy

• exergonic = energy exits

carbohydrates

• CHO 1:2:1

• quick energy

monosaccharides

monomers of carbohydrates

disaccharides

dimers of carbohydrates

polysaccharides

polymers of carbohydrates

ex: cellulose, starch, chtin, glycogen

lipids

• CHO, not 1:2:1

• cell membrane, energy storage, steroid hormones, insulation, myelin sheath

unsaturated fatty acid chains

lacking an extra hydrogen atom

• double carbon bond causes kink

• liquid at room temp

saturated fatty acid chains

has the full amount of hydrogen atoms

• single carbon bond makes it straight

• solid at room temperature

phospholipid head

touches the water so it’s hydrophilic

• polar = hydrophilic

• on the outside of the membrane

phospholipid tail

away from water so it’s hydrophobic

• nonpolar = hydrophobic

• on the inside of the membrane

proteins

• CHON (sometimes S)

• enzymes, structure, transport, signaling, protein carriers, antibodies

amino acids

• monomer of proteins

• carboxyl + amino group + central carbon + variable R group

carboxyl group

• COOH

• one end of amino acid

amino group

• NH2

• other end of amino acid

central carbon

• main part of amino acid

variable R group

• hydrophobic or hydrophilic

• determines chemical properties of the amino acid

protein folding

shape determines function

primary structure of protein

amino acid sequence

secondary structure of protein

chain/polypeptide backbone

• beta pleated sheet

• alpha helix

beta shape

who gives a sheet about betas

pleated sheet

alpha shape

helix

tertiary structure of protein

3d protein, a single polypeptide

quaternary structure of protein

multiple polypeptides/proteins

nucleic acid

• CHONP

• storage and transmission of genetic info

nucelotide

• monomer of nucleic acid

• nitrogen base + phosphate group + 5C deoxyribose sugars

DNA and RNA

polymers of nucleic acid

DNA function

carries genetic code

• eukaryotes: in nucleus on multiple linear chromosomes

• prokaryotes: single circular chromosome

DNA structure

• double helix

• deoxyribose sugars

• antiparallel strands

  • 3’ to 5’

  • 5’ to 3’

• made of nucleotides connected by hydrogen bonds

RNA

• single stranded

• ribose sugars

• ribonucleic acid

• AGCU

mRNA

copies genetic message

tRNA

transfers amino acids

rRNA

attaches mRNA makes up ribosomes by helping form peptide bonds

purines

Pure As Gold, there’s gold is strong = double ringed

• As = adenine

• Gold = guanine

• double ringed

pyrimidines

C.U.T. the Pie, get one slice = single ringed

• C = cytosine

• U = uracil

• T = thymine

• single ringed

nitrogen bond pairs

AT, AU, GC

• DNA: adenine + thymine

• RNA: adenine + uracil

• guanine + cytosine

GC base pair

Group Chats are strong

• stronger due to 3 hydrogen bonds

AT/AU base pair

A is the weakest letter

• weaker due to 2 hydrogen bonds

DNA transcription

• RNA polymerase

• in nucleus

• DNA into RNA

initiation of transcription

promoters binds to RNA polymerase

elongation of transcription

adds RNA nucleotides

termination of transcription

when RNA reaches a termination sequence

RNA polymerase reads…

DNA from 3’ to 5’

RNA polymerase synthesizes…

complementary mRNA in 5’ to 3’

mRNA editing

• splice out introns

• add polyA tail to 3’

• add GTP cap to 5’

• go to ribosome

intron

spliced out of mRNA

exon

expressed in final mRNA

translation

mRNA is ready and matched with tRNA (brings amino acids) to make a protein using the ribosome

DNA replication

• exact copies of DNA for mitosis/meiosis

• semi-conservative by copying the original strand

• DNA polymerase

helicase

enzyme unzips DNA strands by breaking hydrogen bonds

replication fork

splits strands into 5’ to 3’ and 3’ to 5’

RNA primers

made by RNA primase, starts replication process

DNA polymerase reads…

DNA from 3’ to 5’

DNA polymerase synthesizes…

complementary RNA in 5’ to 3’

leading strand

• continuous synthesis

• 5’ to 3’, towards replication fork

lagging strand

• discontinuous/lagging synthesis in okazaki fragments

• 3’ to 5’, away from replication fork

ligase

enzyme fuses okazaki fragments to lagging strand

topoisomerase

enzyme relieves tension of DNA by preventing tangles and knots

enzymes

proteins are catalysts that speed up chemical reactions by lowering activation energy

activation energy

how much energy is required for a reaction to happen

active site

enzyme region where substrates bond via enzyme/substrate complex

allosteric site

enzyme region where ligands bonds

substrate

the specifically shaped key to an enzyme

enzyme rate/function

based on enzyme and substrate collision

• optimal pH

  • depends on the enzyme

• temperature

  • increased temp means more collisions, so rate increases

  • too much heat denatures enzyme

• enzyme concentration

  • more enzyme = faster rate

substrate concentration

if your job is to fold paper, getting passed paper is helpful, but too much paper won’t speed it up

helps increase reaction rate but can plateau

competitive inhibition

competes with substrate for active site

non-competitive inhibition

• attaches at allosteric site

• changes enzyme shape to make it not function

integral protein

• permanently attached to the plasma membrane

• transports ions and molecules

peripheral proteins

• attached to the outside of the plasma membrane

• usually enzymes or signal transduction

glycolipids

stabilize the cell membrane with hydrogen bonds

glycoproteins

used for cell recognition

molecules that can freely move through thanks to selective permeability

• small

• nonpolar

• not charged

• hydrophobic

molecules that cannot freely move through thanks to selective permeability

• large

• polar

• ionized/charged

• hydrophilic

passive transport

high to low that’s how it goes

• down the concentration gradient

• high to low

• no energy

active transport

• against/up the concentration gradient

• low to high

• energy needed

simple diffusion

• passive

• no transport protein needed

facilitated diffusion

• passive

• channel/carrier proteins needed

channel protein

• passive transport

• no energy

• specific substances only

carrier proteins

• passive or active transport

• bind to molecules

• changes shape to transport

osmosis

water always wants to balance/dilute

movement of water

• high water concentrations to low water concentration

• or, water moves from low solute concentration to high solute concentration

hypertonic solution

hyper people are thin

cell will lose water to the environment and shrink

hypotonic solution

hypo = hippo = fat

cell will gain water from the environment and swell