AMINO ACIDS

-Building blocks/stones of proteins

-Fundamental sub-units of proteins

AMINO ACID STRUCTURE

AMINO GROUP- BASIC PROPERTIES

CARBOXYL GROUP- ACIDIC POPERTIES

CHIRAL C – ASSYMETRIC CARBON

PEPTIDE BOND

PHYSICAL ANG CHEMICAL

-PHYSICAL PROPERTIES

1. WHITE CRYTALLINE substances

2. SOLUBLE IN COLD WATER, except cysteine and tyrosine

3. INSOLUBLE IN ALCOHOL AND ETHER, except proline and hydroxyproline

4. ALL AMINO ACIDS except proline are PRECIPITATED OFF FROM THEIR
SOLUTIONS by alcohol but not by (NH4)2SO4 or NaCI

5. MOST OF THEM ARE SWEET like glycine,alanine, serine and proline, others like
leucine are tasteless; while some are bitter like arginine

-CHEMICAL PROPERTIES

1. Amino acids are AMPHOTERIC.

2. Form ESTERS with alcohol- by FRACTIONAL, DISTILLATION

3. Amino acids can be ACETYLATED, BENZYLATED OR METHYLATED in the

presence of acetic acid, benzoic acid or methyl group, respectively. These
reactions occur in the body during detoxification processes.

4. All amino acids REACT WITH NITROUS ACID with the liberation of nitrogen gas,
except proline and hydroxyproline. This is the principle involved in VAN SLYKE
method of determining amino groups in proteins , blood and other biological
substances.

-Reaction with Alcohols (Esterification)

- the amino acids is reacted with alcohol to form, “Ester”. The esters are volatile
in contrast to the form of amino acids

5. FORMALDEHYDE REACTION: When an excess of neutral formaldehyde is added

to neutral amino acid solution, a distinctly acid mixture is produced. The hydrogen
atoms of the amine group are replaced by a methylene group thus destroying the
basic property and allowing the carboxyl to assert itself freely . Basis of SORENSEN
FORMOL TEST

6. Amino acids from ACYL HALIDES. The amino group is previously protected by
acetylation. The protecting (-CO-CH3) group may be subsequently be REMOVED
BY USING HCL.
7. By heating with barium hydroxide, primary amines are formed due to the
breaking off the carboxyl group with formation of CO2.

8. when amino acids are dehydrated, they unite with each other forming a ring,
diketopiperazine. On boiling with HCI, diketopiperazine yields dipeptide

CHARACTERISTICS

1. OPTICALLY ACTIVE

-All the amino acids except glycine have handedness (chiral)

-Amino acids exist as D or L form that are non superimposable mirror image of
one another. L form naturally occurs in proteins.

-destrorotatory (+)- plane polarized lights shifted to the right

-levorotary(+)- plane polarized light shifted to the left

2. AMPHOPETRIC / AMPHOLYTE

3. ZWITTERION / DIPOLAR ION

-Possesses both a positive or negative ion Acidity is due to r2 (pie r) electron

delocalization. The OH bond in COOH weakens so it is easily given off or lost as a
proton and is accepted by the lone pair in NH3

4.ISOELECTRIC POINT

-The ph value at which zwitterion state exists at a maximum

-Amino aids & proteins assume a zero net charge

-Amino acids & proteins are least soluble (precipitate form)

Above pl : favors anionic state

Below pl : favors cationic state (pl)

3 importane of pl:

1. Used in BUFFER SYSTEMS

2. For SEPARATION & IDENTIFICATION PURPOSES --- since each amino acid has its
distint pl.

3. Show STRUCTURAL CHANGES in globular CHON--- the expalanation of

structures of biological reactions.

5. ACID – BASE PROPERTY

ACIDIC BASIC

CLASSIFICATIONS OF AMINO ACIDS

Names,3 letter code, 1 letter code

CLASSIFICATION
 TYROSINE

Tyr, Y

AROMATIC

METABOLISM

LEUCINE, LYSINE, PHENYLALANINE, ISOLEUCINE, THREONINE, TRYPTOPHAN,

TYROSINE, ETC.

ACCORDING TO R-GROUP
A. NEUTRAL OR STRAIGHT CHAIN AMINO ACIDS: (POLAR) GLYCINE(GLY),
ALANINE(ALA)

B. BANCHED CHAIN AMINO ACIDS VALIE(VAL),

LEUCINE(LEU),

ISOLEUCINE(ILE)

C. ACIDIC AMINO ACIDS: (POLAR) ASPARTIC

ACID(ASP),

GLUTAMIC
ACID(GLU)

D. BASIC AMINO ACIDS: (POLAR) LYSINE(LYS),

HISTIDINE(HIS),

ARGININE (ARG)

E. AROMATIC AMINO ACIDS: (NON POLAR)

PHENYLALANINE(PHE),

TYROSINE(TYR)

TRYPTOPHAN(TRP)
F. SULFUR-CONTAINING AMINO ACIDS
METHIONINE(METH)

CYSTEINE(CYS
OR CYS1),

CYSTINE (CYS OR
CYS2)

G. HYDROXY-CONTAINING AMINO ACIDS SERINE,

THREONINE

H. IMINO ACIDS- not an amino acids because of the PROLINE(PRO)

,

absence of NH2 but only NH

HYDROXYPROLINE(HPR)

I. ALIPHATIC R-GROUP (NON POLAR) GLYCINE,

ALANINE ,

PROLINE, VALINE, LEUCINE,

ISOLEUCINE, METHIONINE

INDIVIDUAL AMINO ACIDS

-GROUP A: Nonpolar side chains- Ala, Val, Leu, Ile, Pro, Phe, Trp, Met.

- Ala, Val, Leu, Ile, Pro- contain aliphatic hydrocarbon group. Pro has cyclic
structure.

-Trp- Indole ring side chain, aromatic.

-Met- Sulfur atom in side chain.

AMINO ACIDS (CONT’D)

-GROUP C: Acidic Side Chain: Glu, Asp

-Both have a carboxyl group inside a chain

-Can lose a proton, forming a carboxylate ion

-These amino acids are negatively charged at neutral pH

-GROUP D: Basic side chains: His, Lys, Arg

-Side chains are positively charged at pH 7

-Arg-side chain is a guanidino group

-His-side chain is an imidazole group

-Lys-side chain NH3 group is attached to an aliphatic hydrocarbon chain

CLASSIFICATIONS OF AMINO ACIDS

ACCORDING TO IMPORTANCE

ACCORDING TO IMPORTANCE

ESSENTIAL / INDASPANSABLE AMINO ACIDS

NON- ESSENTIAL AMINO ACIDS

CONDITIONALY ESSENTIAL AMINO ACIDS

ESSENTIAL / INDISPENSABLE AMINO ACIDS

-Those which cannot be synthesized in the body

-Must be provided in the diet

-Primarily essential or semiessential

Papa Vincent Teach Me To Live Like A Hero

Papa Phenylalanine

Vincent Valine, Isoleucine

Teach Tryptophan

Me Methionine

To Threonine

Live Leucine

Like Lysine

A Arginine

Hero Histidine

NON ESSENTIAL /DISPENSABLE AMINO ACIDS

-Those which can be produced in the body

AMINO ACIDS THAT ARE NOT PART OF PAPA VINCENT IS CONSIDERED NON-
ESSENTIAL :

GLYCINE NORLEUCINE

GLUTAMIC ACID CITRULINE

ALANINE TYROSINE
HYDROXYGLUTAMICACID
PROLINE SERINE

CYSTEINE ASPARTIC ACID

HYDROXYPROLINE

CONDITIONALLY ESSENTIAL AMINO ACIDS

-Those amino acids that are essential in the presence of physiological stress

NORMALLY NON-ESSENTIAL BUT BECOMES ESSENTIAL IN THE PRESENCE OF

PHYSIOLOGICAL STRESS

ARGININE GLYCINE

CYSTEINE TYROSINE

PROLINE GLUTAMINE

TAURINE

ACCORDING TO METABOLISM

PURELY KETOGENIC

KETOGENIC AND GLUCOGENIC

PURELY GLUCOGENIC

PURELY KETOGENIC

-Converted to Ketone Bodies

LEUCINE AND LYSINE

KETOGENIC AND GLUCOGENIC

-Partially Ketogenic and Partially Glucogenic

ISOLEUCINE, PHENYLALANINE, THREONINE, TYROSINE, TRYPTOPHAN

PURELY GLUCOGENIC

-Substrate the gluconeogenesis

ALL THE REMAINING 14 AMINO ACIDS

OTHERS

Arginine, Glutamic Acid, Glycine, Inhibitory Amino Acid Neurotransmitters and

Excitatory Amino Acid Neurotransmitters

SESSION 6

PROTEIN

-Greek word “PROTEIOS” meaning “pre-eminence” or of first importance

> Most important macromolecule

> Macromolecular

> Made up of C,H,O,N

> Litmus paper: red-blue

CLASSIFICATIONS OF PROTEIN

ACCORDING TO HYDROLYSIS PRODUCTS

ACCORDING TO BIOLOGICAL SUBSTANCE

ACCORDING TO CONFORMATION/SHAPE

ACCORDING TO HYDROLYSIS PRODUCTS

SIMPLE PROTEINS

 These are TRUE PROTEINS found abundantly in both plants

and animals
 On hydrolysis with enzymes they yield a-amino acids and their
derivatives

-ALBUMINS

> SOLUBLE in water and DILUTE neutral salt solutions

> They are conjugated by heat and precipitated by full saturation with (NH4)2 SO4
but not with NACI except in the presence of acid

-GLOBULINS

> Soluble in neutral dilute salt solutions but not water

> Coagulated by heat and can be precipitated from their solutions by half
saturation with (NH4)2SO4 and complete saturation with NACI

-GLUTEINS

> Soluble in dilute acids and alkalies but insoluble in neutral solvents

-PROLAMINES

> Soluble in 70% alcohol at about neutral point, insoluble in ordinary solvent

-HISTONES

> Soluble in water, dilute acids and alkaliesbut not in dilute ammonia

-PROTAMINES

>Soluble in water and dilute acids and alkalies

-SCLEROPROTEINS (ALBUMINOIDS)
> Soluble in water and neutral solvents

Conjugated Proteins

 Made up of protein molecules combined with non-protein

groups

Derived Proteins

 Include substances formed from simple and conjugated

proteins

2 DIVISIONS

1. PRIMARY PROTEIN DERIVATIVES

2. SECONDARY PROTEIN DERIVATIVES

PRIMARY PROTEIN DERIVATIVES

 Have undergone slight intramolecular rearrangement through

the hydrolytic action of certain physical and chemical agents
 Synonymous with DENATURED PROTEIN

EXAMPLES

PROTEANS- are insoluble substances resulting from the preliminary action of

water, dilute acids or enzymes

METAPROTEANS- are products of further hydrolysis

-soluble in weak acids and alkalies but insoluble in neutral

salt solution
SECONDARY PROTEIN DERIVATIVES

-products of more extensive hydrolysis

-PRIMARY PROTEOSES

-Soluble in water

- Precipitated by con. HNO3 and by half saturation with (NH4)2SO4 or ZnSO4

-Not Coagulated by heat

-SECONDARY PROTEOSES

-Precipitated only by complete saturation with ammonium sulfate but not with nitric acid o
picric acid

-PEPTONES

-Soluble in water

-Not coagulated by heat and not precipitated by saturation with ammonium

sulfate but by certain alkaloidal reagents such as phosphotungstic and tannic
acids

-PEPTIDES

-Are combinations of two or more amino acids, the carboxyl group of one being
united with the amino group of the other

-Examples are: di, tri, tetra, penta, and poly peptides

ACCORDING TO BIOLOGICAL SIGNIICANCE

-TRANSPORT PROTEINS – carry/circulate small molecule ions

> Hemoglobin – carries O2 from lungs to other tissues

> Serumalbin – distribute fatty acids between fat tissue and other organs
-STORAGE PROTEINS - store small molecules ions

> Ovalbumin – used to store amino acids used as nutrients by chicken embryos
found in eggs

> Ferretin – “liver protein”

-CONTRACTILE PROTEIN – conductin of nerve impulses

-muscular motion and coordination of motion

EXAMPLES:

> Myosin + Muscle Protein

-STRUCTURAL PROTEIN – provide mechanical support and structure

EXAMPLES:

> Collagen – for mechanical strength of bones

> Keratin - hair

-PROTECTION PROTEIN – “natural defense proteins”

EXAMPLES:

>Antibodies

-CATALYTIC PROTEIN – used to catalyzed biochemical reactions

EXAMPLES:

> ENZYMES

-CHEMICAL MESSENGER – hormonal action

EXAMPLES:

> HORMONES

ACCORDING TO CONFORMATION/SHAPE

FIBROUS

 Polypeptide chains are arranged tightly parallel fibers and

sheets
 Forms the structural framework of the body
 EXAMPLES: Collagen most important protein in human
connective tissue, Elastin similar to collagen but not cannot be
converted to gelatin, Keratin – insoluble, indigestible, fibrous
proteins. Most component of hair, nails and feathers

GLOBULAR

 Polypeptides are arranged in compact spherical forms

 Soluble in water
 e,g. Antibodies, Enzymes

MIXED

 Resembles fibrous protein in terms of strength

SESSION 7

PEPTIDE BONDS

- ARE CHAINS OF AMINO ACIDS

- When a few amino acids are joined in this fashion, the structure is called
an oligopeptide. When many amino acids are joined the product is called a
polypeptide
FORMATION OF PEPTIDE LINKAGES

NAMING OF PEPTIDE

Change the ending of the 1st succeeding amino acids into –yl but retain the name
of the last amino acids

Glycine – glycyl Glutamic acid – glutamyl tryptophan –tryptophyl

Alanine – alanyl Lysine – lysyl Methionine –methionine

Valine – valyl Histidine – histidyl Cysteine – cysteyl

Leucine – leucyl Arginine – arginyl Cystine – cystyl

Isoleucine – isoleucyl Phenylalanine – phenylalanyl Serine – seryl

Aspartic acid – aspartyl Tyrosine – tyrosyl Threonine – threonyl

CHARACTERISTICS OF PEPTIDE BOND

- The peptide bond is a partial double bond

- The C-N bond is ‘trans’ in nature and there is no freedom of roration
- The angles of rotation, known as Ramachandran angles, therefore
determine the spatial orientation of the peptide chain

PROPERTIES OF PROTEINS
PHYSICAL

- Generally CHON are odorless and tasteless except proten hydrolyzates

CHEMICAL PROPERTIES

- Observed when there ae changes in chemical composition

a. Amphoteric / ampholyte

- possess both a positive and negative ion

b. Proteins

LEVELS OF ORGANIZATION OF CHON

PRIMARILY STRUCTURE 1o

- Linear arrangement of amino acid in a polypepide chain joined together by

means of peptide linkages

CHARACTERISTICS OF PEPTIDE LINK

- A STRONG BOND
 Due to the eletron delocalization towards the arbonyl group
- EXHIBIT GEOMETRIC ISOMERISM
 CIS ISOMER – both above or both below; both ;left or both
right
 TRANS ISOMER – 1 above and 1 below; 1 left and 1 right due to
the restricted rotation in the double bon, groups attached to C
and N may be projected on the same side
1.SECONDARY STRUCTUR 2O

- Involves folding of polypeptide hains due to it

- Refers to particularly stable arrangements of amino acids

2 TYPES OF SECONDARY STRUCTURE

ALPHA HELIX

- Formed due to intramolecular H-bonding

- INTRAMOLECULAR – within the molecules/peptides

BETA- PLEATED SHEAT

- Due to intermolecular H-bonding

- INTERMOLECULAR – between different peptide

2. TERTIARY STRUCTURE

- unfolding of polypeptide chains due to formation of bonds like H-bond

-DOMAIN – is the term used to denote a compact globula functional unit of

protein

3. QUATERNARY STRUCTURE

- Most complex aspect of protein strand

DENATURATION OF PROTEINS

-Denaturation of the secondary, tertiary, and quaternary structures of CHON

leading to changes in its physical, chemical biological characteristics.
SESSION 8

MALNUTRITION

- Caused by a deficiency or excess in one or more essential nutrients in the

diet

TYPES OF UNDERWEIGHT:

UNDERWEIGHT- underweight for one’s age (weight for age)

STUNTED- a chronic malnutrition manifested by being too short for one’s age
(height for age)

WASTED- an acute malnutrition manifested by being dangerously thin (weight for

height)

TWO MAJOR TYPES OF MALNUTRITION

Protein-energy malnutrition

Micronutrient deficiency disease

KWASHIORKOR
 A form of malnutrition due to a diet deficient in protein and
energy-producing foods
 SYMPTOMS: Generalize edema, breaking down of skin,
preservation of subcutaneous fat, gross enlargement of the
liver, loss of appetite, diarrhea, general discomfort, apathy,
gastrointestinal infection(in some)
MARASMUS

 Severe lack of protein intake and other nutrients THE “DRY-

FORM” OF PEM
 SYMPTOMS: No edema, muscle and fat are wasted, liver is
shrink, looks “old”, pallid, apathetic

SYMPTOMS

-No edema

-Muscle ad fath are wasted

-Liver is shrunk

-Scaling of skin

MALNUTRITION

-ATROPHY

> also known as “”muscle wasting”; due to aging or protein deficiency

> cells are more likely to shrink because no energy is sustaining them

> the body assumes a “kin-bone” appearance or like that of a living mummy

-SICKLE – CELL DISORDER

-AKA DEPRANOCYTOSIS-

> Heriditary blood disease caused by a deficiency in protein globulin foun in RBC