introduction to bilogical macromolecules Flashcards
what do variations in carbon skeletons allow for?
molecular diversity
carbon can form large molecules known as
macromolecules
polymers
chain like macromolecules of similar or identical repeating units that are covalently bonded together
monomers
the repeating units that make up polymers
dehydration reaction
bonds two monomers with the loss of H2O
the OH of one monomer bonds with the H of another monomer forming H2O, which is released
A+B—>AB+H2O
hydrolysis
breaks the bonds in a polymer by adding H2O
one H of the H2o bonds to one monomer and the remaining OH of the H2O attaches to the other monomer
AB+H2O—>A+B
carbohydrates include blank and blank of sugars
sugars
polymers
what groups do carbohydrates contain?
a carbonyl group and many hydroxyl groups
comprised of C, H, and O
monosaccharides
simple sugars
molecular formulas with multiples of the unit CH2O
most common is glucose
can serve as building blocks for amino acids, or as monomers for di and polysaccharides
disaccharides
two monosaccharides joined together by covalent bonds
most common is sucrose
polysaccharides
polymer with many sugars joined via dehydration reactions
storage polysaccharides
plants store starch (polymer of glucose monomers); allows plants to store excess glucose
animals store glycogen (polymer of glucose); stored in liver and muscle cells
structural polysaccharides
cellulose: tough substance that forms plant cell walls
chitin: forms exoskeleton of arthtropods
formation of a protein
amino acid—>peptide—>polypeptide—>protein
protein
molecule consisting of polypeptides (polymers of amino acids) folded in a 3D shape
comprised of C, H, O, N, and S
shape determines function
amino acids
molecules that have an amino group and a carbonyl group
general structure of protein
amino group, carbonyl group, and variable side chain (R)
unique aspects of the AA are based on what?
the side chain’s physical and chemical properties
side chains can be grouped as
nonpolar (hydrophobic)
polar (hydrophilic)
charged/ionic (hydrophilic)
side chains interact, which determine the blank and blank of the protein
shape
function
to form a peptide bond, the blank group of one AA must be positioned next to the blank group of another AA
carboxyl
amino
polypeptides
many amino acids linked by peptide bonds
each polypeptide has unique sequence of AAs and directionality