AMINO ACIDS AND

PROTEINS
Elizabeth C. Bills, RMT
OBJECTIVES:

Enumerate Enumerate the different amino acid and its groups.

Discuss Discuss the process of forming proteins through their structure.

Elaborate Elaborate the different functions and structures of protein.

AMINO ACIDS
• Building blocks of proteins
• Structure includes an amino group and a
carboxyl group
• α-carbon bears a side chain (R-group)
• R-group varies depending on each amino
acid

• 20 amino acids (standard amino acids)

• 19 of 20 amino acids are chiral
• 1 amino acid is achiral
• Glycine has H ion as R side chain
Importance of r-side
chains

• The side chains

determine
• the polarity of the
amino acids
• Their acidic or
basic property
Nonpolar (Hydrophobic) vs Polar (Hydrophilic)
Non Polar Polar

Neutral Acidic Basic

Alkyl Aromatic (oxygen and sulfur
(carboxylic acid side
chain)
(nitrogen atom
attachments) attachments)

Glycine
Serine
Alanine
Threonine
Valine Aspartic Acid Histidine
Phenylalanine Asparagine
Methionine Glutamic acid Lysine
Tryptophan Glutamine
Leucine Arginine
Cysteine
Isoleucine
Tyrosine
Proline
 Essential vs Non essential Amino acids

ESSENTIAL NON ESSENTIAL

AMINO ACIDS AMINO ACIDS
Can be produced by the body
Cannot be produced by the body
Not needed to be obtained from the
Taken from diet
diet
 ESSENTIAL NON ESSENTIAL
AMINO ACIDS AMINO ACIDS
Threonine
Tyrosine
Valine

Phenylalanine
Isoleucine The rest
Leucine
Lysine

Methionine
Histidine
 Under physiologic conditions, pH is neutral

Amino acids
When pH is neutral, amino acids are also
can act as neutrally charged.

both acids and

bases Carboxyl group is negatively charged while
amino group is positively charged

When ions are neutrally charged (meaning

they both have positive and negative
charges), they exist as a zwitterion
PEPTIDE BOND
• Individual amino acids can be
linked by forming covalent bonds

• Alpha carboxyl group of one amino

acid attaches to alpha amino group
of another amino acid

• Water is eliminated in the process

(condensation reaction/
dehydration synthesis)

• The bond formed is called a

peptide bond
 Peptides - compounds formed by
linking small numbers of amino
acids, ranging from two to several
dozen

Polypeptide chain – many amino

PEPTIDE BOND acids linked together by peptide
bonds

Amide – another name for the

compound formed between the
reaction of a carboxyl and amino
group
 PEPTIDE BOND

• Dipeptide - simplest possible covalently bonded combination of amino acids

example: carnosine (found in muscle tissue), aspartame (200 times sweeter
than sugar)
• Tripeptide – three amino acids linked by two peptide bonds
example: Glutathione (an oxidizing agent)
• Pentapeptides – five amino acids
example: enkephalins (naturally occurring pain reliever or analgesic)
PROTEINS
 • Greek word “Proties” – meaning
‘first rank of importance’

• Composed of CHON

• Polymers consisting of amino acids

linked by covalent peptide bonds
Proteins • Synthesized by the liver and
secreted by the hepatocyte into the
circulation

• AMPHOTERIC – composed of acidic

and basic amino acids
PROTEIN SYNTHESIS

The alpha amino acids contain a special carbon called

_____________.

This carbon contains four (4) specific components:

One R group
An amino group A Carboxyl group One Hydrogen
_________________
PROTEIN SYNTHESIS

• These 4 components of the alpha carbon are responsible for the specific
property of each kind of amino acid.

• One property that it imparts is _____________.

PROTEIN SYNTHESIS
• Chirality
• The mirror image of amino acids
• Has two kinds
• ____________________- right turning
• ____________________ - left turning
TAKE NOTE:
ALL BIOLOGICALLY ACTIVE proteins occur in the _______________ position.
PROTEIN SYNTHESIS

• Proteins a.k.a ______________, are formed when any two amino acids are
joined together via _______________.

• Proteins are now made by the attachment of many amino acids to form one
long chain of amino acids called ________________.
Levels of Protein
Structure

01
 Levels of Protein Structure
01 02

Primary Secondary
Linear sequence of amino Repetitive organization of the
acids in a polypeptide chain peptide backbone

03 04

Tertiary Quaternary
Complete 3D arrangement of Arrangement of monomer subunits with
all atoms respect to each other
Primary structure
• Formed by the
POLYMERIZATION of amino
acids
• Bridge formation between
Cysteine residues
Secondary structure
• FOLDING of polypeptide chains
• Two main structures are formed
• _______ helices
• _______ sheets
• ALPHA HELIX • BETA-PLEATED SHEETS
• Coil of amino acid is in • Polypeptide chains lie ______
________ turn to one another
• There are about ___ amino • may be parallel or
antiparallel
acids per turn
Tertiary structure
• THREE-DIMENSIONAL
shape formation of
polypeptides by folding
further.

Quaternary structure
• Proteins in the ACTIVE
STATE are usually
quaternary proteins
 PROTEIN
FOLDING
STRUCTURE

PRIMARY Linear structure; no folding

STRUCTURE

SECONDARY Folding via hydrogen bonds produces

STRUCTURE alpha helix or beta sheets

TERTIARY Folding of alpha helix and beta sheets

STRUCTURE

QUATERNARY Folding of tertiary structures

STRUCTURE
 PROTEIN FOLDING

• PROTEIN FOLDING - a process by which a polypeptide chain folds to

become a biologically active protein in its native 3D structure

• Folding of proteins into their correct native structure is key to their

function
• Defects in protein folding can cause various diseases
 Temperature – in high temperature,
proteins can unfold or denature

Factors pH – extreme pH can also cause

denaturation
Affecting
Protein Chemicals – chemical denaturants
Folding can also denature pH

Gene defect or mutations

Protein Folding Disorders

• Cystic fibrosis – lack of

cystic
fibrosis transmembrane
conductance regulator
(CFTR) protein
• Tay-Sachs disease – lack of
hexosaminidase A
• Alzheimer’s disease –
accumulation of beta-
amyloid protein in the
brain
• Parkinson’s disease –
accumulation of clumps
of protein called Lewy
bodies in the brain
Classification of
Proteins by
Simple Proteins
Structure
&

02
Conjugated Proteins
 SIMPLE PROTEINS
FIBROUS PROTEINS GLOBULAR PROTEINS

● Elongated, asymmetrical ● Symmetrical, compactly

polypeptide folded polypeptide

● Water insoluble ● Water soluble

● Ex. Fibrinogen, Troponin, ● Ex. Hemoglobin, Enzymes,

Collagen Albumin
MYOGLOBIN

• Single heme group

• One molecule of myoglobin
binds one oxygen molecule
• Function: Oxygen storage in
muscles
• Must bind strongly to
oxygen at very low
pressures
HEMOGLOBIN

• Each chain has 1 heme group;

hemoglobin can bind up to 4
molecules of O2
• Function: Oxygen transport
• Must be able to both bind
strongly to oxygen and to
release oxygen easily
 CONJUGATED PROTEINS
• Glycoproteins
• Attached to 10 – 40% CHO 4. Metalloproteins
• Ex. Haptoglobin ○ CHON attached to
• Mucoproteins metal
• Attached to >40% CHO ○ Ex. Ceruloplasmin
• Ex. Mucin
• Lipoproteins 5. Nucleoproteins
• CHON with lipid prosthetic group ○ CHON attached to
• Ex. Cholesterol, Triglycerides DNA or RNA
○ Ex. Chromatins
Classification of
Proteins by
Function
Simple Proteins
&

03
Conjugated Proteins
Classification of Proteins by Function

• Enzymes
• Protiens that catalyze chemical reactions
• Ex. Creatinine kinase

• Hormones
• Chemical messengers that control the actions of specific cells or organs
• Ex. Insulin, Glucagon
• Transport Proteins
• Proteins that transport ions, small molecules or macromolecules
– such as hormones, vitamins, minerals, and lipids across a
biologic membrane
• Ex. Bilirubin, Albumin, Transferrin

• Immunoglobulins (Antibodies)
• Proteins produced by B-cells in the bone marrow that mediate
the humoral immune response to identify and neutralize foreign
objects
• Structural Proteins
• Fibrous proteins that are the structures of cells and tissues – such
as muscle, tendons, and bone matrix

• Storage Proteins
• serve as reserves of metal ions and amino acids that can be
released and used later w/o harm occurring to cells during the time
of storage
• Ex. Ferritin
• Energy Source
• serve as a reserve source of energy for tissues and

muscles

• Osmotic Force
• Function in the distribution of water throughout

the compartments of the body