Final Review - Semester 1 Flashcards
Ionic bonds
transfer of electrons
boring/not very strong
Covalent bonds
sharing of electrons
very strong
Polarity
Polar covalent bonds
unequal sharing of electrons in covalent bonds, leading to unequal distribution of charge
(polar attracted to polar)
Hydrogen bonding in H2O
strongest attractions between most polar molecules
common in bio systems
Cohesion
sticking together
Adhesion
sticking to other things
Surface Tension
is created by cohesion
molecules stick to each other (the penny experiment)
Specific Heat temp of water
a measure of how much heat is absorbed/released before increase increase/decrease in temperature
Evaporative Cooling
like sweating
Density
the quantity of things (molecules) in a given area or space
Monomer
the simplest unit of a molecule
Polymer
large molecule of repeating monomers
Hydrolysis
Monomer division
reverse dehydration synthesis
(breaking with water)
anabolic and endergonic
Dehydration synthesis
Monomers joining
builds complex molecule by removing water molecule and replacing it with a bond
catabolic and exergonic
Macromolecules
very big molecules
- made of a few common atoms
- accomplishes all life functions
- put together in a specific way (STRUCTURE)
- can be incredibly complex
Carbohydrates
sugars and starches
made of C, H, O in 1:2:1 ratio
used for short term energy storage
Monosaccharides
monomers of carbohydrates
hexose sugars are most known
Disaccharides
glucose+glucose=maltose
glucose+fructose=sucrose
glucose+galactose=lactose
polysaccharides
massive polymers of sugars
used for short term energy storage and structural support
Plants: amylose(starch) and cellulose
Animals: glycogen
Protein Structure
Primary - the sequence of amino acids, joined together covalently
Secondary - repeating 3D structures in polypeptide chains ex: helix or beta sheet
Tertiary - specific 3D shape or conformation of polypeptide chains, all proteins have up to this level of structure
Quaternary - specific 3D shape made of more than 1 polypeptide chain, this is an optional level
Protein Structure bonds
Primary - covalent peptide bonds
Secondary - hydrogen bonds between backbones
Tertiary - interactions between R groups
Quaternary -
Protein Function
almost all life functions
storage, defensive, structural, hormonal, transport, contractile and motor, receptor, and enzymatic proteins
Denaturing of Proteins
change in structure of a protein
function will change (which won’t work very well)
Lipid characteristic that unite the group
fats, oils, waxes
made of C, H, O
used for long term energy storage and insulation
no polymers, only big molecules
hydrophobic