chp. 3 Flashcards
- carbohydrates - monosaccharides - energy, structure(cell wall) - glucose
- lipids - fatty acids - high energy storage, cell membrane - butter, vegetable oil, cholesterol
- proteins - amino acids - structure, enzymatic - amylase
- nucleic acids - nucleotides - hereditary code, energy carrier - dna, ATP
4 main classes of macromolecules
when a large number of monomers are bonded together.
polymer
Process of linking monomers together is
polymerization.
amino acid generalized structure
Central Carbon then: H-hydrogen/NH v 2 –amino functional group/ COOH-carboxyl functional group/ distinctive r group (side chain).
When a water molecules is removed in the condensation reaction the ______ group is converted to a ________ functional group (C=O) in the resulting polymer, and the amino group is reduced to an N-H (peptide bond). Peptide bond is in the center of the two combined.
carboxyl, carbonyl
which amino acids have oxygen
polar
Nonpolar side chains lack charged or highly electronegative atoms capable of forming hydrogen bonds with water. this makes them____
hyrdophobic
Instead of dissolving hydrophobic side chains tend to coalesce in aqueous solution
Polar or charged side chains interact readily with water and are _______
hydrophilic. (Hydrophilic side chains dissolve in water easily)
sequence with the free amino group (starts)
n terminus or amino terminus
sequence with the free carboxyl (end)
c terminus or carboxyl terminus.
unique sequence of amino acids stabilized by peptide bonds.
primary
created in part by hydrogen bonding between components of the peptide bonded backbone. Distinctively shaped sections of proteins that are stabilized largely by hydrogen bonding that occurs between he oxygen on the C=O group of one amino acid residue and the hydrogen on the N-H groups of another. Alpha helix/beta sheets. Highly stable because there are a lot of weak hydrogen bonds. (Look like curled ribbon or folded paper).
secondary
shape results from interactions between r groups or between r groups and the backbone. Because each contact between r groups causes the peptide bonded back bone to bend and fold each contributes to the distinctive three d shape of a polypeptide. Hydrogen bonding, hydrophobic interactions, van der waals interactions, covalent bonding, ionic bonding. Can have ribbons and beta sheets, can have multiple a helixes, or folded beta sheets, or lots of disulfide bonds which look like jax.
tertiary
combination of polypeptides referred to as subunits gives a protein this structure. Individual polypeptides are held together by same five bonds as tertiary. This is the level with multiple proteins.
quarternary
_____ perform more types of cell functions than any other type of molecule does. Catalyze, defense, movement, signaling, structure, transport.
Proteins
