Macromolecules Flashcards
macromolecules
4 important classes of large organic molecules
lipids
not polymers; big, mostly hydrophobic or amphipathic, have hydrocarbon regions
polymer
a chain of similar monomer subunits
dehydration (condensation) reaction
removes water in order to separate molecules
hydrolysis
splits water in order combine molecules
carbohydrates
made of monosaccharides (simple sugar)
ratio of carbohydrate elements
1C:2H:1O
proteins
made of amino acids
nucleic acids
made of nucleotides
monosaccharides
hydrocarbon chain with hydroxyl and carbonyl, “ose”
what is the shape of monosaccharides?
start as linear, but can form rings in water with a C-O-C bond
polysaccharide
many monosaccharides connected through dehydration (glycosidic linkages)
hydroxyl
carbon bonded to an OH group
carbonyl
carbon double bonded to an oxygen
glycosidic linkage
bonds between monosaccharides through dehydration
starch
a type of polysaccharide, stores energy
glycogen
a type of polysaccharide used in the body to store energy
cellulose
type of polysaccharide used to form structures in cells
chitin
type of polysaccharide used to form cell walls in plant cells
amino acid
has a central (alpha) carbon bonded to an amino group, a carboxyl group, an H, and an R group
polypeptide
another name for protein, multiple amino acids linked
carboxyl
C-O=O
amino group
N and H, basic
peptide bond
bond between amino acids through dehydration reaction between carboxyl and amine groups (C-N) bond
nucleotides
monosaccharide, nitrogenous base, and phosphates
how can you tell the difference between deoxyribose vs ribose?
ribose is missing an OH on the bottom right carbon in the monosaccharide
phosphodiester bond
bond between nucleotides, bond sugar to phosphate to sugar; removes 2 phosphates to create bond
nucleic acid
polymer of nucleotides
primary structure of proteins
sequence of amino acids in polymer which is built by the ribosome
secondary structure of proteins
bonding of 3 atoms that are part of the central chain; hydrogen bonding between carboxyl end and amino end
what shapes do secondary structure of proteins create?
alpha helixes or beta sheets
tertiary structure of proteins
folding created by interactions between R groups
quaternary structure of proteins
some separate amino acid polymers bind together using non-peptide bonds to make a functional “protein” unit
disulfide bond
bonds between 2 sulfur atoms, can occur in tertiary and quaternary structure of proteins
denaturation
loss of secondary/tertiary/quaternary structure but not primary structure; non-peptide bonds are sensitive to things like temperature, pH, salt
competitive inhibitor
the blocking of an enzyme’s active site to prohibit its function
allosteric inhibitor
changing the shape of the enzyme’s active site by binding to a separate part of the enzyme to inhibit its activity
homeostasis
trying to maintain balance
negative feedback
the processes that create certain products also regulate them through competitive and allosteric inhibition often