BIO AP TEST REVIEW 😔

what are the four macromolecules (monomer, bond, function, example), and what are macromolecules made up in general?

macromolecules are made up of polymers and monomers

• carbohydrates: monosaccharides, glycosidic bonds, gives energy and structural support, glucose/starch/cellulose

• proteins: amino acids, peptide bonds, speeds up reactions + transport, enzymes

• lipids: fatty acids and glycerol, ester bonds, stores energy, fats/oils/phospholipids

• nucleic acids: nucleotides, phosphodiester bonds, stores genetic information, DNA/RNA

saturated fats vs unsaturated fats, and what are the 3 major groups of lipids

• saturated: no double bonds between carbon atoms, saturated with hydrogen atoms, solid

• unsaturated: one or more double bonds between carbon atoms, liquid

• fats: for insulation, energy, and protection

• phospholipids: cell membrane

• steroids: hormonal and structural components of cell membrane

four levels of protein structure

1. Primary structure: sequence of amino acids in polypeptide chain to determine genetic code

2. secondary structure: folding polypeptide chains into structures like alpha helices and beta sheets

3. tertiary structure: overall structure of a single polypeptide chain; protein changes through interactions with R-groups (side chains) to determine active sites

4. quaternary structure: multiple polypeptide chains come together into a single function protein

what is polymerization reaction? Hydrolysis?

The interaction with a smaller molecule (like water) that alters the shape of macromolecules

polymerization (dehydration) reaction: where monomers combine to form polymers with a loss of water

Hydrolysis: where a compound is broken down with the use of water

describe denaturation (reversible vs irreversible, what structures it affects, and the causes of denaturation)

a process that alters a protein’s natural structure and biological activity

• reversible denaturation: where a denatured protein can refold back to its original structure if the denaturing agent is removed

• irreversible denaturation: proteins cannot regain their original structure

• it affects the secondary, tertiary, and sometimes quaternary structures

• pH and temperature cause denaturation by changing its shape and function

adhesion, cohesion, surface tension, capillary action, evaporative cooling, heat of vaporization, floating of ice, hydrophilic vs hydrophobic

• adhesion: hydrogen bonds sticking to other surfaces

• cohesion: hydrogen bonds sticking together

• surface tension: the measure of how difficult it is to break the surface of a liquid

• capillary action: moving liquid up a tube

• evaporative cooling: as liquid evaporates, surface of liquid that is left behind cools down (ex: perspiration)

• heat of vaporization: amount of heat needed to turn liquid to gas

• floating of ice: ice is less dense due to oxygen held apart at cooler temps

• hydrophilic (likes water) vs hydrophobic (repels water)

catabolic vs anabolic pathways

catabolic: releases energy by breaking down pathways (cell respiration)

anabolic: consumes energy by building complicated molecules (photosynthesis)

exergonic vs endergonic reactions

exergonic: spontaneous with energy being released

endergonic: non-spontaneous with energy being absorbed

explain enzyme, active site, activation energy, and substrate and the relationship they have with each other

enzyme: speeds up metabolic reactions

activation energy: energy barrier required for reactions to occur

active sites hold substrate, and they work together to make products

in relation, enzymes have active sites that are used to produce products. enzymes lower activation energy so substrates can make products more easily.

cofactors and coenzymes

cofactors: nonprotein helpers that enzymes need for catalytic activity (inorganic or organic)

coenzymes: a specific cofactor that carries electrons or other functional groups (always organic- from vitamins)

competitive vs noncompetitve inhibitors

competitive: competes with substrate to prevent them from accessing active site (inhibits reaction)

noncompetitive: binds to allosteric site and alters enzyme’s function, reduces enzyme activity and cannot catalyze reaction (cannot be overcome with increasing substrate)

3 parts of nucleotide

• left: phosphate group- provides energy and links nucleotides together

• middle: 5-carbon sugar- links base to phosphate group

• right: nitrogenous base- carries genetic information in pairs with bases

covalent vs ionic bonds in electronegativity

electronegativity: