AP Bio Unit 1 (1.3-1.7)

monomers

chemical subunits used to create polymers

polymers

macromolecule made of many monomers

dehydration synthesis

used to create macromolecules, pulls out an H2O

hydrolysis reactions

polymers are broken down (hydrolyzed) into monomers, adding a water molecule to break a bond

monosaccharide

carbohydrate monomer, ex. glucose, ribose

amino acid

protein monomer

nucleotide

nucleic acid monomer - 5-carbon sugar, phosphate group, and nitrogenous base

fatty acid*

foundation of lipids, not true monomers

isomer

same molecular formula w/ different atom arrangement

amino group, R-group/side chain, carboxyl group

parts of an amino acid

adenine, thymine (DNA), guanine, cytosine, uracil (RNA)

nitrogenous bases

store + transport hereditary info

function of nucleic acids

deoxyribose (DNA) and ribose (RNA)

DNA and RNA sugars

hydrophilic

polar, likes water

hydrophobic

non-polar, doesn’t like water

polysaccaride

complex carbohydrate, functions: storage (plants-starch, animals - glycogen), structure (plants - cellulose, arthropod, chitin)

saturated fatty acids

only single bonds between carbon atoms, solid at room temp, from animals

unsaturated fatty acids

at least 1 double bond between carbon atoms, results in a kink in the chain, liquid at room temp, from plants

fats

type of lipid that provides energy storage + supports cell function, some provide insulation

steroids

type of lipid - hormones that support physiological functions including growth and development, energy metabolism, and homeostasis

phospholipids

hydrophilic head, hydrophobic tail, group together to form the lipid bilayers in plasma and cell membranes

adenine-thymine

held together by 2 hydrogen bonds in DNA

guanine-cytosine

held together by 3 hydrogen bonds in DNA

3 prime end

which end can nucleotides be added to?

peptide bonds

name for covalent bonds in proteins

R-group

part of amino acid that can be/have hydrophobic/non-polar, ionic, disulfide bridges, or hydrophilic/polar

primary structure of protein

sequence of amino acids held together by peptide (covalent) bonds

secondary structure of protein

arises through local folding of the amino acid chain into elements such as alpha-helices and beta-sheets bc of hydrogen bonding

tertiary structure of protein

3D shape of protein - various types of bonds and interactions stabilize at this level

quaternary structure of protein

arises from interactions between multiple polypeptide units

phosphodiester bond

phosphate-sugar backbone in a nucleotide

purine

nucleic acids - adenine and guanine, 2 carbon/nitrogen rings

pyrimidine

nucleic acids - thymine + cytosine, 1 carbon/nitrogen ring

enzymes, defense, storage, transport, hormones, receptors, movement, structure

functions of proteins

chaperonins

assist in proper folding of proteins