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lipids
organic molecules that are not water soluble.
no specific functional group
4 basic categories of lipids
fats and waxes, complex lipids, steroids; prostaglandins, leukotrienes, thromboxanes
fats and waxes
fatty acids, 12-20 carbon monocarboxylic acids
unsaturated fatty acids
have double bonds, can undergo chemistry to metabolize easier.
melting points are lower than saturated fat melting points.
all natural unsaturated fatty acids are
cis unsaturated fatty acids
have a lower melting point
polyunsaturated fats
more desirable because lower melting point and more reactive
means its easier to metabolize
triglycerides
glycerol backbone with 3 fatty acids
soap
glycerol and the sodium salts of fatty acids.
created when a triglyceride reacts with a base such as NaOH
linoleic and linolenic fats
essential fats
alpha and omega fatty acids
need from outside sources
complex lipids
phospholipids and glycolipids
phospholipids
have a glycerol or sphyngocine backbone
both include a phosphate group
Phosphate group adds dual solubility
glycolipids
have a sphingocine backbone and a sugar group
also possesses dual solubility
steroids
4 rings: 3 six membered rings, 1 five membered ring
ex. cholesterol
Cholesterol
liver breaks down HDL into bile salts.
building block of steroids and sex hormones
bile salts
amphipathic molecules that act as detergents
prostaglandins
mediate fever and pain
leukotrienes
trigger inflammation, bronchioconstrictors (athsma)
thromboxanes
promote blood clotting, vasoconstrictor
proteins
polyamides, come from a carboxylic acid reacting with an amine (dehydration rxn)
Amino acids
20 common
all are water soluble and have a high melting point
react with itself due to zwitteronic forces
amino acid structure
alpha carbon, amine group, carboxyl group, and R group
primary structure of protein
amino acid sequence, amide bonding through dehydration
2º structure
folding patterns: alpha helix or beta pleated sheet
occur through hydrogen bonding between two amino acids in the backbone
3º structure of proteins
interactions with the R group
ionic bond
hydrophobic interactions
hydrogen bonding
disulfide linkage
metal ion coordination
4º structure of protein
consists of more than one amino acid chain
ex. hemoglobin
protein function
enzymes
immunoglobulins
transport proteins
regulatory proteins (insulin)
structural proteins
movement
receptor proteins
denaturing proteins
ruining a proteins shape, done by denaturing bonds in the 2º or 3º structures.
denaturing methods
adding an acid or base
[O] or [H]
adding salts or metals
physically mixing it
heat
adding organic compounds or solvents
enzymes
proteins found in the cell that are responsible for catalyzing chemical reactions
super specific, usually 1 enzyme for a given chemical reaction.
make reactions faster by 108 - 1020
remain unchanged
each cell contains > 3000 enzymes
lock and key method
reactant is the substrate and the active site on the enzyme is what it’s interacting with
induced fit model
the enzyme is always moving but it accommodates the substrate as the substrate approaches.
What can alter the active site
pH and temp.
most enzymes optimal pH is 5-8.
if not at optimum, the enzymes will denature and no longer work
cofactors
inorganic enzyme helpers that make for proper enzyme activity.
minerals
coenzymes
organic helpers for proper enzymatic activity
ex. vitamins
competitive enzyme inhibition
the inhibitor blocks the active site, not allowing the substrate access to it, thus no reaction.
adding more substrate can override and increase the rate of reaction
non-competitive inhibition
interact at a different spot on the enzyme, changes the shape of the active site.
substrate cannot interact and no reaction occurs
adding more substrate does not increase the rate of reaction.
allosteric/non-competitive regulation
inhibitor
proenzyme/zymogen
group on/group off inactive group preventing enzyme from working
feedback control
one of the products acts as an inhibitor.