Vinay A

Iyer
XII A
Chemistry Project Vinay A Iyer

Help is but one of the basic necessities of life. Akin to an infant who cannot set forth to meet the
world unless with his hand held by someone else, no endeavor can seek completion without
support and encouragement meted out by many hands. So, it becomes my fond duty to thank
those who made this project possible.

After offering our humblest gratitude to the Lord Almighty we wish to offer our gracious thanks
to the CBSE for providing a means of practically applying what is learnt in school and hence
understand the subject better.

We are also indebted to our Principal, Mrs. Deepa Sridhar and the staff of our institution who
have never gone back in providing any kind of assistance and support to us.

Also, we are eternally grateful to our Chemistry teacher, Mrs.Shubha as also the exceedingly
helpful lab assistants led by Mr. Prakash for enriching the experience of working on this project
by their expertise and skill.

Lastly our acknowledgements are due to our kin and friends for all the help that they have
selflessly provided.

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Chemistry Project Vinay A Iyer

This is to certify that

Vinay A Iyer
of class XII A
has successfully completed the
project
Estimation of free amino acids
in
food samples
in
Chemistry
as prescribed by the CBSE board
for the year 2009-10 in
the laboratory of
Sri Kumaran Children’s Home
 Signature of the external examiner Signature of internal examiner
Date: Date:

Chemistry Project Vinay A Iyer

3
Chemistry Project Vinay A Iyer

Sl No Topic Page No
1. Introduction 5
2. Amino acids 6

3. Free amino acids 7

4. Classification& 11
Reactions
5. Function & 13
Occurrence
6. Colorimeter 14

7. Application 16

8. Experiment 17

9. Observations & 20
Graph
10. Conclusion 22

11. Bibliography 23
 Proteins are large molecules composed of one or more chains of amino acids in a specific order
that is determined by the base sequence of nucleotides in the coding for the protein. Proteins are
very useful structurally and metabolically and each protein has unique functions. They result due
to the formation of peptide linkages between free amino acid molecules via a dehydration
reaction of –COOH and –NH2 groups.

The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning.
Protein is generally used to refer to the complete biological molecule in a stable conformation,
whereas peptide is generally reserved for a short amino acid oligomer often lacking a stable
three-dimensional structure.

Amino acids may be defined as a group of organic molecules that consist of a basic amino group
(−NH2), an acidic carboxyl group (−COOH), and an organic R group (or side chain) that is unique to each
amino acid. The term is usually understood to mean α-Amino acids with the general formula:

Proteins and amino acids are of primary importance to the continuing functioning of life on
Earth. Proteins catalyze the vast majority of chemical reactions that occur in the cell. They
provide many of the structural elements of a cell, and they help to bind cells together into tissues.
Some proteins act as contractile elements to make movement possible. Others are responsible for
the transport of vital materials from the outside of the cell (“extracellular”) to its inside
(“intracellular”). Proteins, in the form of antibodies, protect animals from disease and, in the
form of interferon, mount an intracellular attack against viruses that have eluded destruction by
the antibodies and other immune system defenses. Many hormones are proteins. Last but
certainly not least, proteins control the activity of genes (“gene expression”).

Hence amino acids as building blocks of proteins find great application in nutrition. They help in
repairing muscle tissues, food flavoring et al. However free amino acids that are consumed in
diet are also of immense use since they synthesize a variety of standard and non standard
biomolecules and contribute to the urea cycle.

Also, in recent years the free amino acid content in naturally occurring substances has been
exploited to produce biocompatible materials. For example, changing the amino acid structure of
keratin can help develop the compound used for biodegradable plastic.

Thus, in account of the above it becomes very important to analyze the content of amino acids in
various food stuffs.

Chemistry Project Vinay A Iyer 5

 Amino acids or more specifically Proteinogenic amino acids are 22 (including proline where the
amino group is secondary due to cyclization and hence an imino acid) amino acids that are
found in proteins and that are coded for in the standard genetic code. Proteinogenic literally
means protein building. Proteinogenic amino acids are assembled into a polypeptide (the
subunit of a protein) through a process known as translation

The precise amino acid content, and the sequence of those amino acids, of a specific protein, is
determined by the sequence of the bases in the gene that encodes that protein. The chemical
properties of the amino acids of proteins determine the biological activity of the protein.

The amino acids are usually distinguished by the R group on the α Carbon and all the standard
amino acids are known to exist stereochemically in the L form, though D-alanine has been discovered in
some bacterial cell walls and gycine is not chiral. Amino acids also differ by the polarity of the
molecules.

Nonstandard amino acids refer to those amino acids that have been chemically modified after they have
been incorporated into a protein (termed a “post-translational modification”) and those amino acids that
occur in living organisms but are not found in proteins.

Another important feature of free amino acids is the existence of both a basic and an acidic group at the α-
carbon. Compounds such as amino acids that can act as either an acid or a base are called amphoteric. The
basic amino group typically has a pKa between 9 and 10, while the acidic α-carboxyl group has a pKa
that is usually close to 2. The pKa of a group is the pH value at which the concentration of the protonated
group equals that of the unprotonated group. Thus, at physiological pH (about 7–7.4), the free amino
acids exist largely as dipolar ions or zwitter ions. There is a pH called the isoelectric point at which the
molecule has a net zero charge.

Free amino acids combine

with each other through
polypeptide bonds to form
proteins. This is the principal
use of amino acids.

Chemistry Project Vinay A Iyer 6

 Amino acid Abbreviation Symbol Structure
Alanine ala A CH3-CH(NH2)-COOH
Arginine arg R HN=C(NH2)-NH-(CH2)3-CH(NH2)-COOH
Asparagine asn N H2N-CO-CH2-CH(NH2)-COOH
Aspartic Acid asp D HOOC-CH2-CH(NH2)-COOH
Cysteine cys C HS-CH2-CH(NH2)-COOH
Glutamic Acid glu E HOOC-(CH2)2-CH(NH2)-COOH
Glutamine gln Q H2N-CO-(CH2)2-CH(NH2)-COOH
Glycine gly G NH2-CH2-COOH
Histidine his H NH-CH=N-CH=C-CH2-CH(NH2)-COOH
Isoleucine ile I CH3-CH2-CH(CH3)-CH(NH2)-COOH
Leucine leu L (CH3)2-CH-CH2-CH(NH2)-COOH
Lysine lys K H2N-(CH2)4-CH(NH2)-COOH
Methionine met M CH3-S-(CH2)2-CH(NH2)-COOH
Phenylalanine phe F Ph-CH2-CH(NH2)-COOH
Proline pro P NH-(CH2)3-CH-COOH
Serine ser S HO-CH2-CH(NH2)-COOH
Threonine thr T CH3-CH(OH)-CH(NH2)-COOH
Tryptophan trp W Ph-NH-CH=C-CH2-CH(NH2)-COOH
Tyrosine tyr Y HO-Ph-CH2-CH(NH2)-COOH
Valine val V (CH3)2-CH-CH(NH2)-COOH

Apart from these 20 classical standard proteinogenic amino acids two others namely;
Selenocysteine (Sec / U) with CH2SeH as R group and Pyrrolysine (Pyl / O) with C4H8-NH-CO-
3-CH3-3,4-dihydro-2H-pyrrol-2-yl as the R group are recommended by the IUPAC and
IUBMB as recent additions to the group.

The 3D structure of Asparagine, one of

the proteinogenic amino acids

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Chemistry Project Vinay A Iyer

Essential amino acids:

 HISTIDINE

Has been used in the treatment of arthritis and anemia; is essential for the growth and repair of tissues; is
needed for the production blood cells; protects the body from radiation damage; lowers blood pressure.

 ISOLEUCINE

Is needed for hemoglobin formation; stabilizes and regulates blood sugar and energy levels; is
valuable to athletes because it aids in the healing and repair of muscle tissue, skin and
bones.

 LEUCINE

Works with Isoleucine and Valine to promote the healing of muscle tissue, skin, and bones lowers
blood sugar levels; aids in increasing growth hormone production.

 LYSINE
Participates in hydrogen bonding and as a general base in catalysis; treatment of cancer; beneficial for
those with herpes simplex infections.

 METHIONINE

A powerful anti-oxidant and a good source of sulfur, which prevents disorders of the hair, skin, and
nails; detoxifies harmful agents such as lead and other heavy metals; helps diminish
muscle weakness.

 PHENYLALANINE

Used by the brain to produce norepinephrine, a chemical that transmits signals between nerve cells
in the brain; promotes alertness and vitality; elevates mood; decreases pain; aids memory
and learning.

 THREONINE

Helps maintain proper protein balance in the body; is important for the formation of collagen,
elastin and tooth enamel; assists metabolism and assimilation.

 TRYPTOPHAN
 A natural relaxant, helps alleviate insomnia by inducing normal sleep; reduces anxiety and
depression and stabilizes mood; enhances the release of growth hormones; helps control
hyperactivity in children.

 VALINE

Needed for muscle metabolism and coordination, tissue repair and for the maintenance of proper nitrogen
balance in the body. Sickle cell disease results when Valine substitutes Glutamic acid reducing folding.

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Chemistry Project Vinay A Iyer

Non-Essential amino acids:

 ALANINE

Plays a major role in the transfer of nitrogen from peripheral tissue to the liver; aids in the
metabolism of glucose; guards against the buildup of toxic substances; strengthens
the immune system.

 ARGININE

Retards the growth of tumors; aids in liver detoxification by neutralizing ammonia; used
in treating sterility in men ; facilitates an increase in muscle mass and a reduction of body
fat; assists the growth.

 ASPARAGINE

Used in baking; the nervous system requires Asparagine; plays an important role in the synthesis
of ammonia.

 ASPARTIC ACID

Increases stamina; rejuvenates cellular activity, cell formation and metabolism; protects the liver
by aiding the expulsion of ammonia.
 CYSTINE

Functions as a powerful anti-oxidant in detoxifying harmful toxins; protects the body from radiation
damage; protects the liver and brain from damage due to alcohol.

 GLUTAMIC ACID

Is an excitatory neurotransmitter; important in the metabolism of sugars and fats; aids in the
transportation of potassium; acts as fuel for the brain; helps correct personality disorders.
  GLUTAMINE

The most abundant amino acid found in muscles; helps build and maintain muscle tissue; increases
mental activity; assists in maintaining the proper acid/alkaline balance in the body;

 GLYCINE

Retards muscle degeneration; improves glycogen storage, thus freeing up glucose for energy needs;
promotes a healthy central nervous system, and immune system; useful for repairing
damaged tissue.

 PROLINE

Improves skin texture by aiding the production of collagen; helps in the healing of cartilage and
the strengthening of joints, tendons, and heart muscle

Chemistry Project Vinay A Iyer

 SERINE

Needed for the proper metabolism of fats and fatty acids, the growth of muscle, and the
maintenance of a healthy immune system; is a component of the protective myelin sheaths
that cover nerve fibers

 TYROSINE

Is important for overall metabolism; regulates mood and stimulates metabolism and the
nervous system; helps reduce body fat; aids in the production of melanin

 SELENOCYSTEINE

Used to prepare selenoproteins and as a source of selenium.

 PYRROLYSINE

Catalyses methyltransferases; incorporated during translation

Use of dietary amino acids in
humans. The classification of
essential and non essential
amino acids as made above is
strictly for humans.

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Chemistry Project Vinay A Iyer

 Based on the polarity:

Amino acids like alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine and tryptophan
are non polar. The R groups of these amino acids have either aliphatic or aromatic groups. This makes
them hydrophobic (“water fearing”). In aqueous solutions, globular proteins will fold into a three-
dimensional shape to bury these hydrophobic side chains in the protein interior.

On the other hand amino acids such as glycine, serine, cysteine, threonine, tyrosine, asparagine, and
glutamine are polar and uncharged . The side chains in this group possess a spectrum of functional
groups. However, most have at least one atom (nitrogen, oxygen, or sulfur) with electron pairs available
for hydrogen bonding to water and other molecules. They are hydrophilic. The carbonyl group can
function as a hydrogen bond acceptor, and the amino group (NH2) can function as a hydrogen bond
donor.
Non polar amino acids form
globular proteins with
hydrophobic part inwards

 Based on acidic nature:

Both aspartic acid and glutamic acid have a carboxylic acid on their side chain that gives them acidic
(proton-donating) properties. In an aqueous solution at physiological pH, all three functional groups on
these amino acids will ionize, thus giving an overall charge of −1.

Arginine, histidine, and lysine are called basic amino acids. Each side chain is basic (i.e., can accept a
proton). Lysine and arginine both exist with an overall charge of +1 at physiological pH. The guanidino
group in arginine’s side chain is the most basic of all R groups (a fact reflected in its pKa value of 12.5).

Both acidic and basic amino acids are generally hydrophilic.

 Hydrophilic Character:
Polar amino acids are hydrophilic and neutral ones are hydrophobic.

The nature of constituent amino acids decides nature of proteins. For example, soluble proteins have
surfaces rich with polar amino acids like serine and threonine, while integral membrane proteins tend to
have outer rings of hydrophobic amino acids that anchor them into the lipid bilayer. In the case part-way
between these two extremes, peripheral membrane proteins have a patch of hydrophobic amino acids on
their surface that locks onto the membrane.

Hydrophilic amino acids

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Chemistry Project Vinay A Iyer

Amino acids via their various chemical functionalities (carboxyls, amino, and R groups) can undergo
numerous chemical reactions. However, two reactions (peptide bond and cysteine oxidation) are of
particular importance because of their effect on protein structure.

Peptide bond formation:

Amino acids can be linked by a condensation reaction in which an −OH is lost from the carboxyl group of
one amino acid along with a hydrogen from the amino group of a second, forming a molecule of water
and leaving the two amino acids linked via an amide—called, in this case, a peptide bond.

In cells, this reaction does not occur directly; instead the amino acid is first activated by attachment to a
transfer RNA molecule through an ester bond.

Small polymers of amino acids (fewer than 50) are termed oligopeptides, while larger ones (more than
50) are referred to as polypeptides. Hence, a protein molecule is a polypeptide chain composed of many
amino acid residues, with each residue joined to the next by a peptide bond. The lengths for different
proteins range from a few dozen to thousands of amino acids, and each protein contains different relative
proportions of the 20 standard amino acids, each linked via peptide bond formation.

Other reactions:

Amino acids can undergo other reactions like nucleophilic addition, imine formation, esterification and
decarboxylation reactions due to the amino and carboxylic acid groups as also other reactions due to side
chains.

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Chemistry Project Vinay A Iyer

Amino acids are useful components in a variety of metabolisms. Even though, some roles can be
highlighted as a function of an amino acid, it is important to be aware that they are part of complex
pathways and biological systems. The function and use of an amino acid is dependent on other amino
acids, mineral elements, carbohydrate and fatty acids and has indirect effects that are manifested in
myriad metabolisms. They are one of the chief constituents of cell protoplasm

No biosynthesis can happen without the help of amino acids. 20 of them are required for effective human
biosynthesis. While essential amino acids are to be supplemented in diet so as to aid in effective human
biosynthesis. There are also semi-essential amino acids that are needed by lactating mothers and growing
children, like Arginine and Histidine.

Apart from protein synthesis amino acids are also important in forming parts of coenzymes or as
precursors for biosynthesis. Note that the human body, minus water, is 75% amino acids.

Non standard amino acids have their own uses. For example, they determine the localization of the
protein, e.g., the addition of long hydrophobic groups can cause a protein to bind to a phospholipid
membrane.

Humans consume many foods that contain free amino acids. Foods from animal sources are typically rich
in essential amino acids. These include chicken, fish, eggs, dairy products, beef, and pork. Plant sources
include dried beans (black, kidney, red, and white beans), peas, soy, nuts, and seeds. Although plant
sources generally lack one or more of the essential amino acids, when combined with whole grains such
as rice, or by eating nuts or seeds with legumes all the amino acids can be obtained. A large quantity of
dissolved free amino acids has been reported in ocean water as well. But it is to be remembered that the
major source of amino acids remain breaking down of dietary protein.

Glycine and alanine have a sweet taste, valine and leucine have a bitter taste, and aspartic acid and
glutamate have sour tastes. Though called a bitter amino acid, valine has a slightly sweet taste as well.
The sweetness of glycine and alanine is lighter than that of sugar. Combination of amino acids with their
respective tastes is a key determinant for the taste of food.

Amino acids are also present in hormones, enzymes and other bio-fluids.

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Chemistry Project Vinay A Iyer

Colorimetry can be defined as the procedure for quantitative chemical analysis, based on comparison of
the color developed in a solution of the test material with that in a standard solution; the two solutions
being observed simultaneously in a colorimeter and quantitated on the basis of the absorption of light.

Most of the species in water do not have any color, meaning that the species do not absorb light in the
visible region. To measure the absorbance of the colorless molecules, a reaction must be found which will
produce a color that can be measured. Thus we react the species with a reagent to produce a new
compound which has one or more chromophores. Following this we may analyze its color with respect to
a standard or blank.

Laws used in colorimetric analysis are:

 Beer’s Law: It states that for a parallel beam of monochromatic radiation passing through
homogeneous solutions of equal path length the absorbance is proportional to the concentration.
Alternatively, the rate of decrease of intensity is exponential as the concentration of absorbing
substance increases arithmetically.

 Lambert’s Law: It states that for a parallel beam of monochromatic radiation passing through
homogeneous solutions of equal concentration the absorbance is proportional to the path length.
Alternatively, the rate of decrease of intensity with thickness is proportional to the intensity of
light.

 Beer-Lambert’s Law: It states that there is a logarithmic dependence between the transmission
(or transmissivity), T, of light through a substance and the product of the absorption coefficient of
the substance, α, and the distance the light travels through the material (i.e. the path length), ℓ.
Mathematically;

where A’ is transmission, N is concentration and I 0 and I are the intensity of the incident
light and the transmitted light, respectively

A colorimeter- instrument Depiction of the Beer-

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used for colorimetric analysis. Lamber’s law
Chemistry Project Vinay A Iyer

The essential parts of a colorimeter are:

 a light source (often an ordinary low-voltage filament lamp)

 an adjustable aperture

 a set of colored filters

 a cuvette to hold the working solution

 a detector (usually a photoresistor) to measure the transmitted light

 a meter to display the output from the detector

(1) Wavelength selection, (2) Printer button,

(3) Concentration factor adjustment, (4) UV
mode selector (Deuterium lamp), (5) Readout,
(6) Sample compartment, (7) Zero control
(100% T), (8) Sensitivity switch.

Filters

Changeable optics filters are used in the colorimeter to select the wavelength of light which the solute
absorbs the most, in order to maximize accuracy. The usual wavelength range is from 400 to 700
nanometres (nm).

The choice of the correct wavelength for testing is important. It is interesting to note that the wavelength
that gives the most sensitivity (lower detection limit) for a test factor is the complementary color of the
test sample.

A spectrophotometer is a similar type of instrument that can measure intensity as a function of the color,
or more specifically, the wavelength of light.
15
Chemistry Project Vinay A Iyer

Over the years, the study of amino acids has gained a variety of applications in science and technology.
For example, Ninhydrin is most commonly used to detect fingerprints, as amino acids left over from
peptides and proteins sloughed off in fingerprints react with Ninhydrin. The method employed in this
process is similar in principal to the one in this project.

Though the content of free amino acids in various food stuffs is not necessarily an indicator of the level of
proteins; and hence the amount of amino acids that can be obtained on hydrolysis during digestion, it
certainly gives a fair idea of the ‘protein- richness’ of a particular material. Hence in the background of
the efforts being made by international nutrition experts in isolating the ‘perfect diet’ for each individual,
this becomes a small step in that direction.

Amino acids became popular as dietary supplements by the end of the twentieth century for various uses,
including fitness training, weight loss, and certain chronic diseases. Claims exist in holistic medicine that
indicate amino acid supplements taken in the proper dosage can aid also in fighting depression, allergies,
heart disease, gastrointestinal problems, high cholesterol, muscle weakness, blood sugar problems,
arthritis, insomnia, bipolar illness, epilepsy, chronic fatigue syndrome, autism, attention-deficit
hyperactivity disorder (ADHD), and mental exhaustion. Thus, in the next decade the importance of amino
acids will increase manifold and it will be detrimental for us to increase our knowledge about them.

Also this project has given us a fair view of the processes involved in chemical qualitative and
quantitative analysis and has increased our interest in the same.

Forensic investigations
involving fingerprints are
largely dependent on amino
acid analysis.

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 EXPERIMENT

ESTIMATION OF FREE AMINO ACID

CONTENT
IN VARIOUS FOOD SAMPLES

Chemistry Project Vinay A Iyer 17

AIM:
To estimate the percentage of free amino acids in various food samples.

REQUIREMENTS:
Food samples, Ninhydrin, Glycerin, Sodium Hydroxide solution, Citric Acid, Stannous Chloride crystals,
Ethanol, Distilled Water, Digital Colorimeter, Chemical balance, Test Tubes, Beakers, Measuring Cylinder,
hot water trough & Propanol.

PRINCIPLE:
Free Amino acids undergo special unique reaction with Ninhydrin (Triketohydrindene hydrate).
Among the products is a purple colour imino derivative, which provides as a useful colour test.

Ninhydr

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Chemistry Project Vinay A Iyer

REAGENTS:

Ninhydrin Reagent : 1 gm Ninhydrin dissolved in 50 ml Glycerin

Citrate Buffer : 2 gm citric acid crystals dissolved in 200ml of 0.1 N NaOH

made up to 500 ml.

Stannous Chloride- Citrate Buffer : 80 mg stannous chloride dissolved in 50 ml citrate buffer

Ninhydrin-SnCl2 Citrate Buffer : Ninhydrin solution and stannous chloride-Citrate Buffer mixed
in equal volumes.

Propanol-Water : Propanol and Distilled Water mixed in equal volumes.

PROCEDURE:

• Prepare 5% homogenate (5 g in 100 ml) of sample in ethanol.

• Centrifuge till supernatant is clear.
• Blank: Add 1 ml of Ninhydrin-SnCl2 Citrate Buffer and 3 ml of Propanol Water to
1 ml of Ethanol.
• Sample: Add 1 ml of Ninhydrin-SnCl2 Citrate Buffer to 1 ml of supernatant and
heat for 10 mints. Cool the solution and add 3 ml of Propanol water.
• Record Optical Density of sample against that of Blank.
• Record your observations.

CALCULATIONS:

• Wavelength of Light (Colorimeter) = 540mm

• 0.3 OD of Sample = 0.4 mg of Amino Acids
• Percentage of Amino Acids: (M x 100/5 g)
M: g (Amino Acids)

PRECAUTIONS:

• Ninhydrin is Carcinogenic and a strong Oxidizing agent. Hence proper caution should be
Taken and excessive contact is unadvisable.
• Heating of supernatant and Ninhydrin-SbCL2 citrate Buffer mixture should not be
Direct: a water bath should be used.
• All reagents should be prepared freshly if possible; for best results Ninhydrin and
Stannous Chloride-Citrate Buffer should be refrigerated and mixed only at time of analysis.

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Chemistry Project Vinay A Iyer

Sl OD(540 Quantity of free amino Percentage of free amino

Sample
No nm) acids(mg) acids

1. Rice 0.06 0.08 1.60%

2.
Wheat 0.04 0.053 1.06%

3. Corn 0.19 0.253 5.06%

4.
Ragi 0.03 0.04 0.80%

5. Maida 0.16 0.213 4.26%

6.
Pea 0.14 0.187 3.74%

7. Urad Dal 0.40 0.533 10.66%

8.
Black eye pea 0.20 0.267 5.34%

9. Rajma 0.31 0.413 8.26%

10.
Green gram 0.09 0.12 2.40%

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Chemistry Project Vinay A Iyer

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Chemistry Project Vinay A Iyer

 Among the 10 food samples analyzed, white lentils were found to possess the highest amount of
free amino acid content followed by rajma. This is expected due to the common knowledge that
lentils are a very good source of proteins.

 As a general trend, the free amino acid content in cereals is shown to be abysmally low when
seen in the light of lentils and peas. This indicates that for a well rounded diet the latter is an
absolute necessity, more so on the Indian platter which is largely composed of cereals.

 Among cereals, though it is known that ragi is richer in proteins when compared to rice or wheat,
the experiment seems to suggest otherwise. This may be due to the fact that the amount of free
amino acids is not directly related to the amount of proteins. This statement is true even for wheat
and maida.

 Though green pea and black eye pea are expected to have a similar amount of free amino acids,
the latter has a higher content of free amino acids. This may be attributed to the fact that the latter
is usually marketed in processed form which may reduce the free amino acid content.

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Chemistry Project Vinay A Iyer

 Encyclopedia Britannica

 Wikipedia- The free encyclopedia

 The Biology Project- University of Arizona

 West Virginia University - Online archives

 About.com: Chemistry

 IUBMB – Online articles

 PeptideGuide.com

 Links for Chemists- www virtual library

 Austin Nutritional Research

 Organic Chemistry By Robert Thornton Morrison & Robert Neilson Boyd

 IIT JEE Organic Chemistry By Dr Jagdamba Singh

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