Macromolecules Flashcards
what do all living things contain
proteins, carbs, lipids
what do organic compounds contain
carbon (carbon backbone), can form long chains and combine with other atoms (H, O, N, P, S)
what do properties of an organic molecule depend on
- arrangement of the carbon skeleton (straight, branched, rings with long or short bonds)
- functional groups are attached to carbon skeleton (give molecule distinct chemical properties)
what are 7 functional groups
aldehyde
carbonyl
carboxyl
phosphate
hydroxyl
sulfhydryl
amino
Small change in form causes…
a change in function
what is a single unit of molecules
monomer
what is a chain or ring of monomers
polymer
how do you build polymers
dehydration synthesis where water is released which forms a new bond, enzyme acts as a catalyst
what is hydrolysis
when water is added and a bond is broken in the polymer chain
what are the four classes of biological molecules
carbs, lipids, proteins, nucleic acids
what is a carbohydrate
sugar, source of energy
what are carbohydrates used for
-broken down for cellular respiration
-short term energy reserves in muscles and liver in animals
-structure (cellulose)
how are carbohydrates stored in humans
glycogen
how are carbohydrates stored in plants
starch
what is the ratio for carbohydrates
CH^2O = 1:2:!
what type of sugars are monomers
simple sugars
what type of sugars are polymers
complex sugars
what is a monosaccharide
monomer of carbohydrates
what are types of monosaccharides
glucose, galactose, fructose
what are disaccharides
two linked monosaccharides
what is sucrose
glucose + fructose (table sugar)
what is lactose
glucose + galactose (milk sugar)
what is maltose
glucose + glucose (brewing sugar)
what are polysaccharides
polymers of monosaccharides
what are types of polysaccharides
storage and structural carbohydrates (starch, glycogen & cellulose, chitin)
what is special about herbivores
they eat plants that contain cellulose but do not produce enzymes to break them down. the bacteria in their digestive system breaks it down
what is special about lipids
they are hydrophobic (do not sdissolve in water)
what are 3 main types of lipids
-neutral fats
-phospholipids
-steroids
what are the functions of neutral fats
-long term energy reserve in fat tissue
-maintain body temperature through insulation
-protect vital organs
-buoyancy
what is the sustructure of fat
1 molecule of glycerol
1-3 molecules of fatty acids
what are 3 molecules of fatty acids is called
triglyceride
what is the difference between saturated and unsaturated fatty acids
saturated fatty acids have no double bonds between the carbon atoms while unsaturated fatty acids have double bonds
-saturated fatty acids are then easier to stack since there is no bend in the chain
what is the difference between cis unsaturated and trans unsaturated fatty acids
trans is less of a bend and cis is more of a bend
what is the function of phospholipids
major constituent of cell membranes
what is the structure of phospholipids
2 molecules of fatty acids
1 glycerol molecule
1 phosphate molecule
what is an amphipathic molecule
a molecule that has a side which is hydrophilic and a side that is hydrophobic (phospholipid) basically can interact with both fats and water
which part of the phospholipid is attracted/repelled by water
the head is attracted to water (hydrophilic)
the tail is repelled by water (hydrophobic)
how does the phospholipid assemble
into a double layer that has the hydrophobic portions facing each other
what are the functions of steroids
cell membrane (cholesterol)
vitamins
hormones
what is the structure of steroids
made from sterol (multiple rings of carbon)
what do proteins do
transport, enzymes (break down and build), antibodies, storage
what are proteins made of
amino acids (the polypeptides of protein)
what is a polypeptide
a polymer of amino acids
what is a protein
1 or more functional polypeptides folded/coiled into a specific shape
what is the structure of an amino acid
2 functional groups (amino and carboxyl)
1 variable group (R)
a hydrogen
how do you link amino acids to make a polypeptide and where
dehydration synthesis/condensation reaction
link at the n-terminus and the c-terminus (amino and carboxyl ends)
is the polypeptide polar
yes
why is the shape of a protein important
the shape of the protein determines its function
how many levels of structure are there in proteins
primary
secondary
tertiary
quaternary
what is the primary structure of proteins
the specific and unique sequence of amino acids that make up a polypeptide
- strong covalent bonding
how is the unique sequence of a.a. determined in the primary structure
by the nucleotide sequence of the gene that encodes the protein (genetically determined)
what happens to the protein if an amino acid get switched
it will change the form of the protein which will affect how it performs its function
what is the secondary structure of proteins
the folding and coiling of a sequence of amino acids within a polypeptide
what causes the folding/coiling of proteins
hydrogen bonds between the amino and carboxyl groups in the polypeptide’s backbone
what is an alpha helix and where do the h-bonds occur
coil
bond occurs every fourth amino acid
what is a beta pleaded sheet and where do h-bonds occur
pleated sheet of polypeptide lying parallel
h-bonds between amino and carboxyl group
what are alpha helix characteristics
common in fibrous proteins (hair, skin, nails)
h-bonds are strong when there are many bonds (weak individually)
able to stretch and reform
what are beta pleaded sheet characteristics
make up core of globular proteins and some fibrous proteins like fibroin (spider silk)
strong and flexible but not elastic
can twist
very strong
how is the distance between pleats decided in beta pleaded sheets
the strong covalent bonds of the polypeptide backbone
what is the tertiary structure of a protein
the forces holding a singular polypeptide together
what determines the the 3D structure of a single polypeptide
hydrogen bonds
ionic bonds
hydrophobic interactions
covalent/disulphide bonds
what are ionic bonds
results from ions/ plus minus charged particles
what are hydrophobic interactions
non-water soluble molecules interacting with each other
what is a covalent/disulphide bond
equal sharing of electrons between sulfide groups on a.a.
what is the quaternary structure
the fusion of two or more polypeptide
how is the quaternary structure formed
by the interactions among polypeptide chains
has the same types of bonds as the tertiary structure
ex: hemoglobin and collagen
what is a monomeric protein
protein made of a singular polypeptide chain (no quaternary structure)
what is an oligomeric protein
protein made of two or more polypeptide chains
what is denaturation
when a protein breaks down by unravelling or changing shape (permanent or temporary)
ex: egg frying
what happens during denaturation
disruption or destruction of secondary and tertiary structures
disrupts alpha h. and beta p.s so becomes a random shape
primary sequence remains due to the reaction not being strong enough to break the peptide bonds (except at very high temp.)
what can cause denaturation
heat and alcohol
what are 3 ribosome characteristics
displays quaternary structure
uses RNA to make other proteins
made in nucleolus
what are 3 kind of mutations
neutral
detrimental
beneficial
