Biochemistry Handouts GOOD FATS vs.
BAD FATS
LIPIDS
Lipids is an organic compound found in living
organisms that is insoluble in water but soluble in
nonpolar organic solvents.
- Building blocks are fatty acids and glycerol.
- Water solubility decreases as carbon chain
length increases.
- Short-chain fatty acid have a slight solubility
in water.
- Long -chain fatty acids are insoluble in water.
- Melting points are influenced by both carbon
chain length and degree of unsaturation.
- As carbon chain length increases, melting
point increases.
- The greater the degree of unsaturation, the
greater the reduction in melting points.
Saturated fatty acids have higher melting points than
unsaturated fatty acid.
Long-chain SFA tends to be solid at room
temperature.
Examples: beef, pork, poultry, full-fat dairy products,
coconut & palm oil
Polyunsaturated fatty acids: fish oil, corn, sunflower,
soybean, walnut
Long-chain MUFA tends to be liquid at room
temperature
Examples: olive, peanut, canola, avocados,
almonds, hazelnuts, sesame seeds
LIPIDS ARE DIVIDED BASED ON THEIR
FUNCTION:
a. Energy-storage lipids (triacylglycerols)
b. Membrane lipids (phospholipids,
sphingoglycolipids, and cholesterol)
c. Emulsification lipids (bile acids)
d. Messenger lipids (steroid hormones and
eicosanoids)
e. Protective-coating lipids (biological waxes)
TYPES OF FATTY ACIDS:
Saturated fatty acid is a fatty acid with a carbon chain
in which all carbon-carbon bonds are single bonds.
Monounsaturated fatty acid is a fatty acid with
carbon chain in which one carbon-carbon double is
present.
Polyunsaturated fatty acid is a fatty acid with a
carbon chain in which two or more carbon-carbon
double bonds are present.
Δ, delta followed by one or more superscript
numbers is used to specify the double-bond
positioning within the carbon chain of unsaturated
fatty acid.
Ω, omega is used to specify the double-bond
position relative to the methyl end of the fatty acid
carbon chain.
Saturated fats are bad fats
Monounsaturated fats are good fats
Polyunsaturated fats can be both good fat and bad
fat.
CHEMICAL REACTION OF TRIACYLGLYCEROLS
Hydrolysis is reaction wherein it breaks large
molecules into smaller molecules. In triacylglycerol
hydrolysis, it is carried out in a laboratory setting
which require the presence of acid or base. Under
acidic conditions, the product of triacylglycerols are
fatty acids and glycerol. Under basic condition, it
produces glycerols and fatty acids salts.
Saponification is a reaction carried out in an alkaline
solution that produces glycerol and fatty acids salts
from fats and oils.
Hydrogenation is a chemical reaction that involves
addition of hydrogen across carbon-carbon multiple
bonds, which increases the degree of saturation.
With this change, there is also an increase in melting
point of the substance.
Oxidation breaks the carbon-carbon bonds in the
presence of air as oxidizing agent, which yields
aldehyde and carboxylic acid products.
PROTEINS
Proteins are naturally occurring, unbranched
polymer in which the monomer units are amino
acids.
Characteristics of Protein
• Most abundant substances in all cells.
• It contains, hydrogen, oxygen, nitrogen, and
sulfur
• The presence of nitrogen in proteins sets
them apart from carbohydrates and lipids.
AMINO ACIDS: THE BUILDING BLOCKS FOR
PROTEINS
Amino acid is an organic compound that contains
both an amino group (-NH2) and a carboxyl group (-
COOH)
AMINO ACIDS ARE GROUPED ACCORDING TO
SIDE-CHAIN POLARITY:
• Non polar amino acid is an amino acid that
contains one amino group, one carboxyl
group and a nonpolar side chain.
• Polar neutral amino acid is an amino acid that
contains one amino group, one carboxyl
group, and a side chain that is polar but
neutral.
• Polar acidic amino acid is an amino acid that
contains one amino group and two carboxyl
groups, the second carboxyl group is part of
the side chain.
• Polar basic amino acid is an amino acid that
contains two amino groups and one carboxyl
group, the second amino group is part of the
side chain.
 glycine 5.97-6.06 tryptophan 5.88

histidine 7.59-7.64 tyrosine 5.63-5.66

isoleucine 6.02-6.04 valine 5.97-6.02

▪ The “no net charge” pH value for an amino acid

solution is called “isoelectric points”.
▪ At isoelectric point, almost all amino acid
molecules in a solution are present in their
zwitterion form.
▪ In an electric field, a charged molecule is
attracted to the electrode of the opposite charge.
▪ At a high pH, an amino acid has a net negative
charge and migrates toward the positive
electrode.
▪ At a low pH, an amino acid has positive charge
and migrate towards negative electrode.
▪ At isoelectric point, migration does not occur
because zwitterions present have no net charge.
▪ Electrophoresis is the process of separating
charged molecules on the basis of their migration
toward charged electrodes associated with an
ACID-BASE PROPERTIES OF AMINO ACIDS: electric field.
PEPTIDES:
Peptide is an unbranched chain of amino acids, each
joined to the next by a peptide bond.
They are classified by the number of amino acids
present in the chain.
• Dipeptide
In neutral solution, carboxyl group lose protons (H+), • Tripeptide
producing negatively charge (COO-), while amino • Oligopeptide (with 10-20 amino acids)
group accept the protons (H+), producing positive • Polypeptide (long unbranched chain of amino
charge molecule (+NH3). The molecule formed here acids)
is zwitterion. It is a molecule that has a positive NATURE OF PEPTIDE BOND
charge on one atom and negative charge on another • Carboxylic acid and an amine can react to
atom, but which has no net charge. produce an amide.
In acidic solution (at low pH), the zwitterion accepts
proton (H+) to form a positively charge ion.
In basic solution (at high pH), the +NH3 of the
zwitterion loses a proton producing a negatively
charge molecule.
ISOELECTRIC POINTS & ELECTROPHORESIS:
Name Isoelectric Name Isoelectric
point point
• Two amino acids combine in similar way –
alanine 6.01-6.11 leucine 5.98-6.04
products are a molecule of water and a
arginine 10.76 lysine 9.47 molecule containing the two amino acids linked
asparagine 5.41-5.43 methionine 5.71-5.74
by an amide bond.

Aspartic 2.77-2.98 phenylalani 5.48-5.76

acid ne

cysteine 5.07-5.15 Proline 6.3-6.48

Glutamic 3.08-3.22 serine 5.68-5.7

acid

glutamine 5.65 threonine 5.87-5.6

• N-terminal end with free H3N+ group of the
peptide is always written on the left while C-
terminal end with free COO- is on the right.
Steps in writing the structural formula of a certain
peptide:
Example: Ala-Gly-Val
1. The N-terminal end of the peptide should be
written first. (Ala)
2. The structure of the next amino acid (Gly) should
be written right to Ala structure, and a peptide
bond is formed between two amino acids
producing one molecule of water and one
molecule containing the two amino acids linked
by an amide bond.
3. To the right, draw the structure of Val, then repeat
step 2 to form the desired peptide.

IUPAC rules for naming small peptides are as

follows:
1. The C-terminal amino acid keeps its full amino
acid name.
2. All of the other amino acids have names that
end in -yl which replaces the -ine or -ic acid,
except for tryptophan (tryptophyl), cysteine
(cysteinyl), glutamine (glutaminyl), and
asparagine (asparaginyl).
3. The amino acid naming sequence begins at N-
terminal amino acid.
Example: Glu-Ser-Ala (Glutamylserylalanine)