CARBOXYL GROUP can dissociate.

▪ Amino Acids
Can become a carboxylate ion (-COO-) +
hydrogen ion (H+)
▪ The building blocks of protein
▪ Proton Donor
▪ N-terminal end amino group (-NH2)
▪ Carboxyl group is the ACIDIC part of
▪ C-terminal end carboxyl group (- the amino acid.
COOH)

▪ These groups bond to the alpha

STEREOCHEMISTRY OF AMINO ACIDS
carbon with the amino group of one R and S Forms
amino acid linking with the carboxyl
group of another = peptide bond

BASIC STRUCTURE OF AMINO

ACIDS
HYDROGEN

NOTE: The higher atomic mass gets the

Amino highest priority. S>O>N>C>H
group
HYDROGEN IS ALWAYS THE LEAST
PRIORITY BECAUSE OF ITS ATOMIC
R GROUP/SIDE MASS WHICH IS 1.
CARBOXYL
GROUP

CHAINS
R GROUP OR SIDE CHAIN
▪ functional groups that are the major
determinants of the conformation
and function of proteins, as well as
the electric charge on the molecule
▪ Properties of each amino acid are
dependent on its side chain
AMINO GROUP can accept a Hydrogen
ion (H+)/a proton.
If the priorities of these other groups go
in a clockwise rotation, the chiralty is
“R’.
If the priorities of these other groups go
counterclockwise, the chiralty is “S”.
▪ What is a CHIRAL CARBON?
This is carbon to which you have 4 different
groups attached.
Also called ASYMMETRIC CARBON
Glycine is not classified as chiral because of
its side chain: H
Why? Remember that the definition of a
chiral carbon, is you have 4 different groups
attached to the alpha carbon.

▪ When you add another Hydrogen, it

becomes positively charged
▪ NH2 will become NH3+
▪ Proton Acceptor
L (Levorotatory) and D (Dextrorotatory)
Amino group is the BASIC part of the amino
acid. configuration

▪ All protein amino acids share the
absolute configuration of L-
ALPHA AMINO ACIDS.
Amino group is on the LEFT of
alpha-carbon = L-Amino Acid
All amino acids is the body are L-
Amino Acids
Amino group is on the RIGHT of
alpha-carbon = D-Amino Acid
There are only 2 D-Amino Acids in
the body:
D-ASPARTATE AND D-SERINE-
Found in the brain
FORMS OF AMINO ACID
▪ UNIONIZED FORM
Carboxyl GroupNOT NEGATIVE (Didn’t
donate any proton)
Amino GroupNOT POSITIVE (Didn’t
accept any proton)
Purpose of this form is only for writing the
formula of the amino acids
▪ DIPOLAR IONS or ZWITTERION
Forms that exist in the body
Dipolar Ions (ZWITTERION)
Amino Group POSITIVELY CHARGED
Carboxyl Group NEGATIVELY
CHARGED
Equal amounts of positive charge and
negative charge = ELECTRICALLY
NEUTRAL (ZERO NET CHARGE)
▪ FULLY PROTONATED
Fully protonated means all hydrogen ions
are attached –
Carboxyl Group gained
You have another hydrogen attached to the
Amino GroupPOSITIVELY CHARGED
Fully protonated forms are ALWAYS
POSITIVE
pH 1  ACIDIC MEDIUM
▪ FULLY DISSOCIATED FORM
Fully dissociated means all hydrogen ions
are removed - Carboxyl Group is
NEGATIVELY CHARGED
- Amino Group Not positively charged
Fully dissociated forms are ALWAYS
NEGATIVE
pH 11 and above is ALKALINIC MEDIUM
Zwitterions and Isoelectric Points
A zwitterion
has an equal number of —NH3+ and COO–
groups forms when the H from —COOH in
an amino acid transfers to the —NH2

Isoelectric Point (pI)

The isoelectric points (pI)
are the pH at which zwitterions have an overall
zero net charge of nonpolar and polar (neutral)
amino acids exist at pH values from 5.1 to 6.3

Zwitterions in Acidic Solutions

In solutions that are more acidic than the pI,
the COO– in the zwitterion accepts a proton
the amino acid has a positive charge

▪ Polar (Hydrophilic) usually exposed

on the surface of proteins

▪
Zwitterions in Basic Solutions
In solutions that are more basic than the pI, 3 types of Polar Amino Acids:
the NH3+ in the zwitterion loses a proton
the amino acid has a negative charge ▪ Uncharged

pI, pH, and Charge

▪ Classification of R group

▪ Non- Polar (Hydrophobic)

▪ usually buried in the hydrophobic

interior of a protein and are out of
contact with water
▪ Positively charged Polar R groups
(Basic)

▪
 ▪ Acidic – with more -COOH than -NH2
group (aspartic acid, glutamic acid)

▪ Neutral amino acids - with one -COOH

and one NH2 (glycine, alanine)

Nutritionally Essential MUST BE PRESENT in the DIET

Arginine (1)
Histidine (1)
Isoleucine
▪ Negatively charged Polar R groups
Leucine
Lysine
(Acidic)
Methionine
Phenylalanine
Threonine
Tryptophan
Valine

Nutritionally Non Essential

( 12)
Alanine
Asparagine
▪ Classification of R group Aspartate
Cysteine
▪ Structure Glutamate
Glutamine
▪ Aliphatic amino acid - carbon atoms Glycine
are arranged in a straight chain Hydroxyproline(2)
(lysine, arginine, glutamic acid, Hydroxylysl (2)
aspargine, glutamine) Proline
▪ Branched amino acid - branching of
Serine
Tyrosine
side chain. (leucine, isoleucine, valine)

▪ Aromatic amino acid - contains the FORMATION OF PEPTIDE BOND

benzene ring (phenylalanine, tyrosine,
tryptophan)

▪ Heterocyclic amino acid - cyclic side

chain containing C atoms and other
elements (tryptophan, histidine, proline,
hydroxyproline)

▪ Sulfur-containing – contains S
(cysteine, cysteine, methionine)

▪ Hydroxy-containing - contains -OH The amino acids shown above is at a form of

group (threonine, serine)
▪ Amidic- containing – asparginine,
glutamine
▪ Basic – with more -NH2 than -COOH
group (lysine, arginine, histidine)
zwitterion.
A reaction should be between 1 carboxyl group
and 1 amino group.
An amino acids cannot just join by holding
hands, they have to actually give up something
in order to live their lives together. In our
dipeptide R1 gives up an atom of 1 oxygen (from
the carboxyl group) while R2 losses an atom of
2 hydrogen (from the amino group). Together
they release a molecule called H2O.
DEHYDRATION SYNTHESIS REACTION- loss
of H2O to form a bond.

CO-NH Linkage = amide linkage known as the

PEPTIDE BOND

Guys, take note. Hindi sa lahat ng pagkakataon

nasa physiological pH ang amino acids.
Depende pa din sa environment yan pag acidic,
neutral, or basic. 