Macromolecules Flashcards
Glycogen: animal storage
stored as granules in muscle or liver. very branched, dosen’t last long
how are starch and cellulose different?
the different placement of the hydroxyl groups in glucose results in different shapes (
Polysaccharide
long chains of carbohydrate molecules composed of several smaller monosaccharides
-saccharide
group that incorporates starch, cellulose, and sugar
Lipids
hydrophobic molecules
- fats
- phospholipids
- steroids
Fat: triglyceride
glyceride backbone, 3 tails called fatty acids (storage contain a lot of energy)
Saturated v unsaturated
saturated:
no double bonds
max # of H+ are attached to carbons
NO kinks in chain
ex. butter
unsaturated:
one or more double bonds (creates kinks)
chain has kinks, makes it more fluid
ex. olive oil
Phospholipids
two fatty acid tails + a phosphate head
makes phosphate polar (hydrophobic head, hydrophilic tail)
very important to cell membrane
Steroids
whole class of chemical messengers
4 lipid rings fused together
hydrogenated
means add more hydrogens
ex. hydrogenated vegetable oil –> is solid at rom temp because more hydrogens have been added leading to less tail kinks (stack better)
Enzymes
speed up reactions
storage
source of amino acids for use later
Transport
facilitate movement of a substance within body and or cells
Receptors
recognize other molecules (pick up signaling between nerve cells)
Proteins!
Enzymes
storage
defense
transport
hormones
receptors
movement
structure
what is a protein?
polymer of amino acids, linked by peptide bonds to form polypeptide
polypeptide
many amino acids connected
peptide bond
covalent bond between carboxyl group and amine group
Amino acids
20 of them, they differ by their R group
protein structure
properties of amino acids in the polypeptide bond lead to different shapes of proteins
- fold according to charges in chemical reactions
- shape os critical to function
Primary structure
sequence of amino acids. dictates secondary and tertiary structure
Secondary structure
regions stabilized by hydrogen bonds between the polypeptide chain
- different regions within the polypeptide fold differently due to hydrogen bonding
two types:
alpha helix - a coiled structure
beta helix - chains lying side by side (sheet)
Tertiary structure
3D shape by interacting interactions with side chains
- may cluster according to polarity: hydrophobic or hydrophilic
Reinforced by…
- hydrogen bonding
- ionic bonds
- disulfide bridges ( type of covalent bond )
Quaternary structure
overall 3-D protein structure of multiple polypeptide subunits
Breaking proteins
pH
salt concentration
temperature
other environmental factors
- damage is reversible as long as it isn’t to the primary structure!!
Denature
when a protein loses its particular shape, it will not function properly
- breaks weak bonds (hydrogen bonds) causing the proteins shape to start to fall apart
Nucleic Acids
polymers of nucleotides
2 types –> DNA and RNA
what is a nucleotide?
- nitrogenous base (contains nitrogen)
- 5 carbon sugar (pentose)
- one or more phosphate groups
Nitrogenous bases
Pyrimidines: C,T (in DNA), U (in RNA)
Purines: A, G
Mutations
result in changes in protein expression, raw material evolution
