simple sugars (most common
glucose) often ending with the
suffix -ose
aldose: has an aldehyde
ketose: has a ketone
disaccharides
lactose
sucrose
maltose
polysaccharides
starch
amylose
amylopectin
branched
glycogen
storage form of glucose usually in
the liver and muscles of humans/vertebates
whenever blood glucose levels
decrease, glycogen is broken down
to release glucose
cellulose
most abundant biopolymer
cell wall of plants and wood
cannot be digested by humans, only by
some herbivores due to protists
alternating positions of glycosidic bonds, need enzyme
cellulase to be broken down
chitin
major component of arthropod exoskeletons and fungal cell walls
N-acetyl-β-d-glucosamine
short term energy storage and
structural molecules
n(CH2O)
BENEFITS
immediate source of energy (4.3 Kcal)
insoluble part (fiber) helps bowel movement and remove excess cholesterol
Lipids
Ester bond
bond between glycerol
and fatty acid
insoluble in water and contain
CHO (just lower number than
carbs)
long term energy storage,
insulation, structural and protection
BENEFITS
essential fats
help reduce the risk of heart attacks, reduce triglyceride levels in the blood, lower blood pressure
and prevent thrombosis by inhibiting blood clotting.
Omega-6
Omega-3
many vitamins are fat soluble
A, D, E, K
fatty acids
waxes
long chain fatty acids bond with alcohol
solid at normal temperature due to high melting point
prevents water loss and helps protection
steroids
hydrocarbons with the carbons arranged in a set of 4 linked rings
cholesterol
hormones
phospholipids
main component of cell membrane
glycerol with 2 fatty acids attached and a phosphate head
hydrophilic head and hydrophobic tail
triglycerides
fats
solid at room temperature and come from animals
saturated
more hydrogen atoms
straight chains
oils
liquid at room temperature and come from plants
unsaturated
have double bonds with carbon
crooked chains
Proteins
Peptide bond
bonds between amino acids
carboxyl group + amino acid combine to relase water
chain of amino acids
polypeptide
amino acids
monomers that make up proteins
has a central carbon atom, bonded to amino
group (and R), carboxyl group, and hydrogen atom
the side chain (R) determines if
acidic, basic, polar, or non-polar
sequence and number of amino acids
determine protein shape and function
20 types of amino acids
10 essential amino acids
consists of 4 elements: Carbon, Oxygen, Hydrogen
and Nitrogen with some proteins having Sulfur
protein refers to a polypeptide or polypeptides
that have combined together
BENEFITS
the most important type of macromolecule
support
collagen in skin, keratin in hair, crystallin in eye
enzymes
all metabolic transformations are done by enzynes
transport
oxygen in the blood is carried by hemoglobin
nutrition
insulin, egg yolk, contractile, antibodies
organized by levels of increasing complexity
primary
unique sequence of amino acids in a polypeptide chain
secondary
local folding of polypeptide in some regions
a-helix
due to hydrogen bonds that form between the O and
CO and another four amino acids farther along the
chain
twirling figure
b-pleated sheet
pleats are formed by hydrogen bonding with atoms on backbone of chain
parallel and antiparallel pleated segments
folded paper figure
tertiary
interactions among R-groups
Interaction between cysteine side chains forms disulfide
linkages in the presence of oxygen (covalent bonding).
hydrophobic interactions
hydrophobic R groups of non-polarity lay interior whereas
hydrophilic lay outside
quarternary
weak interactions of subunits
some proteins are formed from
several polypeptides or more than one amino acid chain
Nucleic Acids
Phosphate ester bond and hydrogen bond
bond between phosphate
and pentose sugar + bond
between nitrogenous bases
nucleotides
organic compounds composed of a pentose sugar, nitrogenous base, and a phosphate group