Amino Acids

Amino Acids and Proteins
Prepared by:
Nelven M. Gallego, RMT, MLS(ASCPi), MSMT cand.
Our Lady of Fatima University – Pampanga
College of Medical Laboratory Science
Biochemistry (CHM 123)
Nelven M. Gallego, RMT, MLS(ASCPi)

Characteristics of Proteins:
• Naturally-occurring, unbranched polymer in which
the monomer units are amino acids
•
• Carbon, Hydrogen, Nitrogen, Oxygen, & Sulfur
• 15.4% by mass (average nitrogen content)
•

• A protein is a peptide in which at least
40 amino acid residues are present:

 Common proteins contain 400–500 AA residues
 Small proteins contain 40–100 AA residues

• More than one polypeptide chain may be present:
– Monomeric: Contains one polypeptide chain
–

Chemical Composition
Simple proteins:
• A protein in which only amino acid residues are present:
Albuminoids - keratin in skin, hair, nails;

collagen in cartilage
Albumins - egg albumin, serum albumin
Globulins -
Histones -

Chemical Composition
Conjugated proteins:
• Protein that has one or more non-amino acid entities
(prosthetic groups) present in its structure:

Based on Shape
Fibrous proteins:
•
• Long, rod-shaped or string-like molecules
•
• Structural functions

Based on Shape
Globular proteins:
• Folded into spherical or globular shapes
•
• Polar amino acids are on the surface
•
•

Based on Shape

Based on Function
• Play crucial roles in most biochemical processes.
• The diversity of functions exhibited by proteins far
exceeds the role of other biochemical molecules
• The functional versatility of proteins stems from:
–
–
–

Based on Function
Major Categories
1. Catalytic proteins: Enzymes are best
known for their catalytic role.
2. Defense proteins: Immunoglobulin or
antibodies are central to functioning of
the body’s immune system.

Based on Function
Major Categories
3. Transport proteins: Bind small biomolecules, e.g.,
oxygen and other ligands, and transport them to other
locations in the body and release them on demand.
4. Messenger proteins: Transmit signals to coordinate
biochemical processes between different cells, tissues,
and organs.
–
–

Based on Function
Major Categories
5. Contractile proteins:
– Muscles contain filament-like contractile proteins
–
6. Structural proteins:
– Collagen is a component of cartilage
–

Based on Function
Major Categories
7. Transmembrane proteins:
– Help molecules to enter and exist the cell.
–
8. Storage proteins:
– Ferritin - an iron-storage protein
–

Based on Function
Major Categories
9. Regulatory proteins:
– Often the molecules that bind to enzymes (catalytic
proteins), thereby turning them “on” and “off,” and
thus controlling enzymatic action.
10. Nutrient proteins: .
– Casein (milk) and ovalalbumin (egg white)
–

Amino Acids:
Building Blocks for Proteins
• The position of carbon atom is Alpha ()
•
• COOH group is attached at alpha () carbon atom.
•

Amino Acids:
Nomenclature
• Three letter abbreviations
– First letter of amino acid name is compulsory and
capitalized followed by next two letters not
capitalized except in the case of Asparagine (Asn),
Glutamine (Gln) and tryptophan (Trp).
• One letter symbols
–
–

Amino Acids:
• All amino acids differ from one another by their R-groups
–
• Standard amino acids are divided into four groups based
on the properties of R-groups
• Non-polar amino acids: R-groups are non-polar
–
–
– When present in proteins, they are located in the
interior of protein where there is no polarity

Amino Acids:
Non-Polar Amino Acids

21
Amino Acids:
• Polar amino acids: R-groups are polar
– Polar neutral; Polar acidic; and Polar basic
• Polar-neutral: contains polar but neutral side chains
–
• Polar acidic: Contain carboxyl group
– Two amino acids belong to this category
• Polar basic: Contain amino group
–

Amino Acids:
Polar Neutral Amino Acids

Amino Acids:
Polar Acidic Amino Acids:
Polar Basic Amino Acids:

Amino Acids:
Derived Amino Acids
•
• Formed by an enzyme-facilitated reaction on a common
amino acid after that amino acid has been incorporated
into a protein structure
•
• Hydroxyproline, and hydroxylysine found in collagen
•

Amino Acids:
Essential Amino Acids
• Essential amino acid: a standard amino acid
needed for protein synthesis that must be obtained
from dietary sources

Arginine Methionine
Phenylalanine
Isoleucine
Tryptophan
Lysine

Amino Acids:
• Complete protein

• Incomplete protein
 Low in one or more of the essential amino acids,
usually lysine, tryptophan, or methionine


Amino Acids:
• Complementary proteins
 Incomplete proteins which when served together,
complement each other and provide all the essential
amino acids

Chirality and Amino Acids:
• Four different groups are attached to the
a-carbon atom in all of the standard amino
acids except glycine
•

Chirality and Amino Acids:
• Molecules with chiral centers exhibit enantiomerism
• Amino acids found in nature as well as in proteins
are L isomers

Amino Acids:
Acid-Base Properties
• In pure form amino acids are white crystalline solids
•
• Not very soluble in water
• Under physiological conditions exists as Zwitterions:

Amino Acids:
•
•

Amino Acids:
Isoelectric point (pl)
• Amino acids in solution exist in three different species
(zwitterions, positive ion, and negative ion)

Amino Acids:
Isoelectric point (pl)
• pH at which the concentration of Zwitterion is maximum
– net charge is zero
–
–

Amino Acids:
• At pH values lower than pI, the carboxylate end of the
zwitterion picks up a proton from solution, the amino
acid acquires a net + charge, and migrate to the
negative electrode in an electric field.

Amino Acids:
• At pH values higher than pI, a proton is removed from
the ammonium end of the zwitterion, the amino acid
acquires a net negative(-) charge and migrate to the
negative electrode

Amino acids and Proteins 1
Prepared by:
Nelven M. Gallego, RMT, MLS(ASCPi), MSMT cand.
Our Lady of Fatima University – Pampanga Campus
College of Medical Laboratory Science
Biochemistry (CHM 123)
NELVEN M. GALLEGO, RMT, MLS(ASCPi)

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Amino Acids and Proteins

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Albuminoids - keratin in skin, hair, nails;

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Polar Basic Amino Acids:

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Essential Amino Acids

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

Nelven M. Gallego, RMT, MLS(ASCPi)

NELVEN M. GALLEGO, RMT, MLS(ASCPi)

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