PROTEIN-AND-AMINO-ACIDS-PPT.p df

Amino Acid
Amino Acid
Amino acids are the monomers
that make up proteins. Specifically,
a protein is made up of one or
more linear chains of amino acids,
each of which is called a
polypeptide.
Amino Acid

AMINO ACID
Amino acids are a group of organic
compounds containing two functional
groups— amino and carboxyl. The
amino group (—NH2) is basic while the
carboxyl group (—COOH) is acidic in
nature.
General structure of amino
acids
The amino acids are termed as D-
amino acids, if both the carboxyl and
amino groups are attached to the
same carbon atom.
Optical isomers of amino acids If a carbon atom is
attached to four different groups, it is asymmetric
and therefore exhibits optical isomerism. The
amino acids (except glycine) possess four distinct
groups (R, H, COO–, NH3 + ) held by D-carbon.
Thus all the amino acids (except glycine where R
= H) have optical isomers.

AMINO ACID
Amino acid classification
based on the structure : A
comprehensive classification
of amino acids is based on
their structure and chemical
nature. Each amino acid is
assigned a 3 letter or 1
letter symbol. These
symbols are commonly used
to represent the amino acids
in protein structure. The 20
amino acids found in
proteins are divided into
seven distinct groups.

Amino Acid
Amino Acid
CHARACTERISTIC OF AMINO
ACID CLASSIFICATION OF AMINO ACIDS BASED ON POLARITY :
Amino acids are classified into 4 groups based on their polarity.
Polarity is important for protein structure.
1. Non-polar amino acids : These amino acids are also referred to as
hydrophobic (water hating). They have no charge on the ‘R’ group. The
amino acids included in this group are — alanine, leucine, isoleucine,
valine, methionine, phenylalanine, tryptophan and proline.
2. Polar amino acids with no charge on ‘R’ group : These amino acids,
as such, carry no charge on the ‘R’ group. They however possess groups
such as hydroxyl, sulfhydryl and amide and participate in hydrogen
bonding of protein structure. The simple amino acid glycine (where R =
H) is also considered in this category. The amino acids in this group are
— glycine, serine, threonine, cysteine, glutamine, asparagine and
tyrosine.

Amino Acid
Amino Acid
ACID
3. POLAR AMINO ACIDS WITH POSITIVE ‘R’ GROUP : THE THREE
AMINO ACIDS LYSINE, ARGININE AND HISTIDINE ARE INCLUDED IN THIS
GROUP.
4. POLAR AMINO ACIDS WITH NEGATIVE ‘R’ GROUP : THE
DICARBOXYLIC MONOAMINO ACIDS— ASPARTIC ACID AND GLUTAMIC
ACID ARE CONSIDERED IN THIS GROUP.
Amino acids are organic compounds that are the building blocks of proteins. They contain
both an amino group (-NH2) and a carboxyl group (-COOH), which are attached to a
central carbon atom. The remaining side chain of each amino acid is unique and determines
its properties 1234.
There are 20 different types of amino acids that can be found in proteins. They can be
classified based on the nature of their side chains into three categories: nonpolar, polar, and
charged 24. Nonpolar amino acids have hydrophobic side chains, while polar amino acids
have hydrophilic side chains. Charged amino acids have either a positive or negative charge
on their side chains 24.
The properties of amino acids are determined by the nature of their side chains. For
example, nonpolar amino acids tend to be hydrophobic and are often found in the interior of
proteins, while polar and charged amino acids tend to be hydrophilic and are often found on
the surface of proteins 24.

Amino Acid
Amino Acid
ACID

AMINO ACID
1. Amino acids with aliphatic side chains : These are monoamino monocarboxylic acids. This
group consists of the most simple amino acids—glycine, alanine, valine, leucine and
isoleucine. The last three amino acids (Leu, Ile, Val) contain branched aliphatic side chains,
hence they are referred to as branched chain amino acids.
2. Hydroxyl group containing amino acids : Serine, threonine and tyrosine are hydroxyl
group containing amino acids. Tyrosine—being aromatic in nature—is usually considered
under aromatic amino acids.
3. Sulfur containing amino acids : Cysteine with sulfhydryl group and methionine with
thioether group are the two amino acids incorporated during the course of protein
synthesis. Cystine, another importa nt sulfur containing amino acid, is formed by
condensation of two molecules of cysteine.

AMINO ACID
4. Acidic amino acids and their amides : Aspartic acid and glutamic acids are dicarboxylic
monoamino acids while asparagine and glutamine are their respective amide derivatives. All
these four amino acids possess distinct codons for their incorporation into proteins.
5. Basic amino acids : The three amino acids lysine, arginine (with guanidino group) and
histidine (with imidazole ring) are dibasic monocarboxylic acids. They are highly basic in
character.
6. Aromatic amino acids : Phenylalanine, tyrosine and tryptophan (with indole ring are
aromatic amino acids. Besides these, histidine may also be considered under this category.
7. Imino acids : Proline containing pyrrolidine ring is a unique amino acid. It has an imino group
( NH), instead of an amino group ( NH2) found in other amino acids. Therefore, proline is an D-
imino acid. Heterocyclic amino acids : Histidine, tryptophan and proline.

20 AMINO ACIDS THAT ARE FOUND IN
ALL NATURALLY OCCURRING PROTEINS

Each amino acid consists of a
central carbon atom connected to
a side chain (R), a hydrogen, a
nitrogen-containing amino group (-
NH2) , a carboxyl group (-COOH)—
hence the name “amino acid.”
Amino acids differ from each
other by which specific side chain
(or the R group) is bonded to the
carbon center.

5
Your nonessential amino acids are the amino acids
your body can create on its own as a byproduct of
normal functioning. There are 11 of these amino
acids, and they include the following:
Alanine (ala)
Arginine (arg)
Asparagine (asn)
Aspartic acid (asp)
Cysteine (cys)
Glutamic acid (glu)
Glutamine (gln)
Glycine (gly)
Proline (pro)
NONESSENTIAL
Your essential amino acids are the ones you need
but cannot produce yourself, and so must be
gained either from your diet or via
supplementation. These amino acids include the
following:
Histidine (his)
Isoleucine (ile)
Leucine (leu)
Lysine (lys)
Methionine (met)
Phenylalanine (phe)
Threonine (thr)
Tryptophan (typ)
Valine (val)
ESSENTIAL
NUTRITIONAL CLASSIFICATION

5
Amino acids can classified according to the
properties of their side chains, that is,
whether they are nonpolar (have an even
distribution of electrons) or polar (have an
uneven distribution of electrons, such as
acids and bases
CLASSIFICATION
OF AMINO ACIDS
Nonpolar (hydrophobic) and uncharged
1.
Polar (hydrophilic) and uncharged
2.
Acidic (polar and charged)
3.
Basic (polar and charged)
4.
AMINO
ACID
Proteins

Each of these amino acids has a
nonpolar side chain that does not
gain or lose protons or participate
in hydrogen or ionic bonds.
The side chains of these amino
acids can be thought of as "oily" or
lipid-like, a property that promotes
hydrophobic interaction (water
fearing or repelling).
Nonpolar (hydrophobic) and
uncharged

In proteins found in aqueous solutions (a polar
environment), the side chains of the nonpolar amino acids
tend to cluster together in the interior of the protein due to
the hydrophobic effect or nature of the nonpolar side chains
(R-groups).
Nonpolar amino acids are commonly found in the
transmembrane domains of integral membrane proteins,
where they help anchor the protein in the lipid bilayer.
These amino acids play a critical role in maintaining the
structural integrity of proteins and providing stability to
protein cores or to its structure.
Location of nonpolar amino acids in proteins:

Unlike nonpolar amino acids, polar unchanged amino have hydrophilic (water loving) side chains,
which allows them to interact with water and form hydrogen bonds.
Serine, threonine, and tyrosine each contain a polar hydroxyl group that can participate in
hydrogen bond formation.
Asparagine and glutamine each contain a carbonyl group and an amide group, both of which can
also participate in hydrogen bonding.
Found on the surface of proteins
These amino acids can form hydrogen bonds and engage in interactions with water molecules,
making them important for the solubility, protein-protein, and protein-solvent interactions.
Polar (hydrophilic) and uncharged

Acidic (polar and
charged)
The amino acids aspartic and glutamic
acid are proton donors.
At physiologic pH, the side chains of these
acidic amino acids are fully ionized,
forming a negatively charged carboxylate
group (-COO-).
These amino acids are often involved in
the ionic interactions and binding of metal
ions within proteins.
They also play essential roles in enzyme
catalysis, signal transduction, and protein-
protein interactions.

The side chains of the basic amino
acids accept protons.
At physiologic pH, the basic amino
acids, lysine, arginine, and histidine,
contain side chains with amino groups
that are positively charged.
Their positive charges enable them to
interact with negatively charged
molecules and surfaces, influencing
various biochemical processes (vise
versa.)
These amino acids are essential for
variousbiological functions, including
DNA binding, enzyme catalysis, and
maintaining the overall charge
balance within proteins.
Basic (polar
and charged)

PROPERTIES OF AMINO ACID
Two types of isomerism are shown by amino acids basically
due to the presence of asymmetric carbon atom. Glycine has
no asymmetric carbon atom in its structure hence is optically
inactive
A. Isomerism:

•Stereoisomerism means that the molecules have the same
molecular formula and the same structural formula but have a
different three dimensional arrangement in space.
STEREOISOMERISM:

•The optical isomers are called enantiomers
•Enantiomers are any pair of stereoisomers that are non-
superimposable mirror images of each other.
• Enantiomers are said to be Chiral.
OPTICAL ISOMERISM

Means something can act as both an acid and a base
depending on the situation. For example, amino acids can
donate or accept protons depending on the pH of the solution
they're in.
AMPHOTERIC NATURE:

Proteins are colourless and usually tasteless.
Shape and Size.
A. Globular proteins: Round proteins mainly found in plants, like
in seeds and leaf cells.
B. Fibrillar proteins: Thread-like or oval-shaped proteins mostly
found in animal muscles.
PHYSICAL PROPERTIES:

PHYSICAL PROPERTIES: SHAPE AND SIZE

Types of Chemical Reactions given by
Amino Acids
Chemical Reactions due to...
-COOH group
-NH2 group
-COOH group
-NH2 group

Amino Acids
-COOH group
-COOH group
Amino acids forms salts (-COONa) with bases and esters (-COOR’) with alcohols.
1
1.
.Amino acids forms salts (-COONa) with bases and esters (-COOR’) with alcohols.
1.
A. Formation of Salts with Bases:
Amino acids contain both acidic (carboxyl group, -COOH) and basic (amino group, -
NH2) functional groups. The acidic -COOH group can react with a base to form a salt.
The amino acid donates a proton (H+) from the -COOH group, forming a carboxylate
ion (-COO⁻). The base accepts the proton to become a positively charged ion.
The resulting salt is formed between the carboxylate ion of the amino acid and the
positively charged ion of the base.
A. Formation of Salts with Bases:
Amino acids contain both acidic (carboxyl group, -COOH) and basic (amino group, -
NH2) functional groups. The acidic -COOH group can react with a base to form a salt.
The amino acid donates a proton (H+) from the -COOH group, forming a carboxylate
ion (-COO⁻). The base accepts the proton to become a positively charged ion.
The resulting salt is formed between the carboxylate ion of the amino acid and the
positively charged ion of the base.

Amino Acids
-COOH group
-COOH group
Amino acids forms salts (-COONa) with bases and esters (-COOR’) with alcohols.
1
1.
.Amino acids forms salts (-COONa) with bases and esters (-COOR’) with alcohols.
1.
B. Formation of Esters with Alcohols:
The -COOH group of an amino acid can also react with an alcohol to form an ester.
In this reaction, the -OH group of the alcohol reacts with the -COOH group of the
amino acid in the presence of an acid catalyst. This reaction is known as
esterification.
The result is the formation of an ester and water, as the -COOH group loses a
hydroxyl (-OH) group, and the -OH group of the alcohol loses a hydrogen atom.
B. Formation of Esters with Alcohols:
The -COOH group of an amino acid can also react with an alcohol to form an ester.
In this reaction, the -OH group of the alcohol reacts with the -COOH group of the
amino acid in the presence of an acid catalyst. This reaction is known as
esterification.
The result is the formation of an ester and water, as the -COOH group loses a
hydroxyl (-OH) group, and the -OH group of the alcohol loses a hydrogen atom.

Amino Acids
-COOH group
-COOH group
2. Decarboxylation: Amino acids undergo decarboxylation to produce corresponding
amines.
2. Decarboxylation: Amino acids undergo decarboxylation to produce corresponding
amines.
The -COOH group undergo decarboxylation, wherein it loses a carbon dioxide
molecule. This results to the formation of a new functional group.
The -COOH group undergo decarboxylation, wherein it loses a carbon dioxide
molecule. This results to the formation of a new functional group.

Amino Acids
-COOH group
-COOH group
3. Reaction with ammonia: The carboxyl group of dicarboxylic amino acids react with
NH3 to form amide.
3. Reaction with ammonia: The carboxyl group of dicarboxylic amino acids react with
NH3 to form amide.
The amino acid and ammonia engage in a reaction known as deamination. In this
interaction, the amino group of the amino acid bids farewell. It doesn't just vanish;
instead, it combines with the ammonia, forming an ammonium ion.
The amino acid and ammonia engage in a reaction known as deamination. In this
interaction, the amino group of the amino acid bids farewell. It doesn't just vanish;
instead, it combines with the ammonia, forming an ammonium ion.

Amino Acids
-NH2 group
-NH2 group
Amino Groups behave as bases and combine with acids to form salts.
1
1.
. Amino Groups behave as bases and combine with acids to form salts.
1.
The amino group has a lone pair of electrons on the nitrogen atom, which can
accept a proton(H+) from an acid through a process called protonation.
The amino group has a lone pair of electrons on the nitrogen atom, which can
accept a proton(H+) from an acid through a process called protonation.

Amino Acids
-NH2 group
-NH2 group
2. Reaction with ninhydrin: The amino acifs react with ninhydrin to form a purple, blue
or pink color complex(Ruhemann’s purple).
2. Reaction with ninhydrin: The amino acifs react with ninhydrin to form a purple, blue
or pink color complex(Ruhemann’s purple).
The mechanism of the reaction involves the interaction of ninhydrin with the amino
group of amino acids, leading to the formation of a colored product. The specific
color can vary, but typically, a purple or blue color is observed.
The mechanism of the reaction involves the interaction of ninhydrin with the amino
group of amino acids, leading to the formation of a colored product. The specific
color can vary, but typically, a purple or blue color is observed.

Amino Acids
-NH2 group
-NH2 group
3. Transamination: The transfer of an amino group from an amino acid to a keto acid to
form a new amino acid.
3. Transamination: The transfer of an amino group from an amino acid to a keto acid to
form a new amino acid.
Transamination is a biochemical process where an amino group (NH2) is
transferred from one amino acid to another, facilitated by enzymes called
transaminases. This leads to the creation of a new amino acid and a new keto acid. It
plays a crucial role in amino acid metabolism, allowing for the synthesis and
breakdown of amino acids..
Transamination is a biochemical process where an amino group (NH2) is
transferred from one amino acid to another, facilitated by enzymes called
transaminases. This leads to the creation of a new amino acid and a new keto acid. It
plays a crucial role in amino acid metabolism, allowing for the synthesis and
breakdown of amino acids..

Amino Acids
-NH2 group
-NH2 group
4. Oxidative deamination: Amino acids undergo oxidative deamination to liberate
ammonia.
4. Oxidative deamination: Amino acids undergo oxidative deamination to liberate
ammonia.
Oxidative deamination is a process where an amino group (NH2) is removed from
an amino acid, resulting in the formation of a keto acid. This reaction is catalyzed by
enzymes, and ammonia (NH3) is released as a byproduct. Oxidative deamination is a
key step in the breakdown of amino acids and is important for eliminating excess
nitrogen from the body.
Oxidative deamination is a process where an amino group (NH2) is removed from
an amino acid, resulting in the formation of a keto acid. This reaction is catalyzed by
enzymes, and ammonia (NH3) is released as a byproduct. Oxidative deamination is a
key step in the breakdown of amino acids and is important for eliminating excess
nitrogen from the body.

Methods of Protein Seperation
Methods of Protein Seperation depends on their characterestics.
These characterestics are;
Methods of Protein Seperation depends on their characterestics.
These characterestics are;
Solubility
Ionic Charge
Polarity
Molecular Size
Binding Specificity
Solubility
Ionic Charge
Polarity
Molecular Size
Binding Specificity

Salting In:
1
1.
.
Prepare Protein Solution:
Start with a protein solution in water, where the proteins are surrounded by water
molecules.
Gradual Salt Addition:
Add a neutral salt (e.g., ammonium sulfate) gradually to the protein solution.
Monitor Solubility:
As salt is added, the ionic strength of the solution increases.
Ion Shielding:
The salt ions shield the charges on the surface of the proteins, reducing repulsive forces
between proteins.
Salting In:
1.
Start with a protein solution in water, where the proteins are surrounded by water
molecules.
Monitor Solubility:
As salt is added, the ionic strength of the solution increases.
Ion Shielding:
The salt ions shield the charges on the surface of the proteins, reducing repulsive forces
between proteins.
Depending On Solubility

Salting In:
1
1.
.
Complete Solubilization:
The shielding effect of ions allows hydrophobic interactions between proteins to dominate,
leading to increased solubility.
Further Processing:
Solubilized proteins can undergo additional processing steps, such as chromatography, to
isolate and purify specific proteins.
Salting In:
1.
Complete Solubilization:
The shielding effect of ions allows hydrophobic interactions between proteins to dominate,
leading to increased solubility.
Further Processing:
Solubilized proteins can undergo additional processing steps, such as chromatography, to
isolate and purify specific proteins.

2. Salting Out:
Begin with a protein solution in water, where the proteins are surrounded by water
molecules.
Monitor Precipitation:
As salt concentration increases, water molecules are disrupted, and the water structure
around proteins is disturbed.
2. Salting Out:
Begin with a protein solution in water, where the proteins are surrounded by water
molecules.
Monitor Precipitation:
As salt concentration increases, water molecules are disrupted, and the water structure
around proteins is disturbed.

2. Salting Out:
Complete Precipitation:
Proteins, now less solvated due to disrupted water structure, aggregate and precipitate out
of the solution.
Centrifugation:
Centrifuge the solution to separate the precipitated proteins from the liquid phase.
Resuspend and Further Processing:
Resuspend the protein pellet in a chosen buffer. Additional processing steps may include
purification techniques.
2. Salting Out:
Complete Precipitation:
Proteins, now less solvated due to disrupted water structure, aggregate and precipitate out
of the solution.
Centrifugation:
Centrifuge the solution to separate the precipitated proteins from the liquid phase.
Resuspend and Further Processing:
Resuspend the protein pellet in a chosen buffer. Additional processing steps may include
purification techniques.

4. Electrophoresis:
Gel Preparation:
Prepare a gel (agarose or polyacrylamide) with wells for sample loading.
Sample Loading:
Load protein or nucleic acid samples into the wells.
Electrophoresis:
Apply an electric field. Charged molecules migrate through the gel based on size and charge.
Visualization:
Stain or label molecules for visualization under UV light or specific dyes.
Separation:
Molecules are separated based on size and charge.
4. Electrophoresis:
Gel Preparation:
Sample Loading:
Electrophoresis:
Apply an electric field. Charged molecules migrate through the gel based on size and charge.
Visualization:
Separation:
Molecules are separated based on size and charge.
Depending On Ionic Charge

5. Isoelectric Focusing:
Prepare Gel:
Set up a gel with a pH gradient.
Sample Loading:
Load the protein mixture.
Isoelectric Focusing:
Apply an electric field. Proteins migrate to their isoelectric point (pI).
Visualization:
Stain or label proteins for visualization.
Separation:
Proteins are separated based on their pI.
5. Isoelectric Focusing:
Prepare Gel:
Set up a gel with a pH gradient.
Sample Loading:
Load the protein mixture.
Isoelectric Focusing:
Apply an electric field. Proteins migrate to their isoelectric point (pI).
Visualization:
Separation:
Proteins are separated based on their pI.

6. Adsorption Chromatography:
Prepare Column:
Set up a column with a solid matrix coated with an adsorbent.
Sample Loading:
Load the protein mixture onto the column.
Adsorption:
Proteins bind to the adsorbent based on interactions like hydrogen bonding or hydrophobicity.
Elution:
Elute proteins by changing conditions like pH or salt concentration.
Separation:
Proteins are separated based on their affinity for the adsorbent.
6. Adsorption Chromatography:
Prepare Column:
Set up a column with a solid matrix coated with an adsorbent.
Sample Loading:
Adsorption:
Proteins bind to the adsorbent based on interactions like hydrogen bonding or hydrophobicity.
Elution:
Elute proteins by changing conditions like pH or salt concentration.
Separation:
Proteins are separated based on their affinity for the adsorbent.
Depending On Polarity

7. Paper Chromatography:
Prepare Paper:
Apply a small spot of the protein sample on chromatography paper.
Solvent Migration:
Allow a solvent to migrate through the paper.
Separation:
Different proteins move at different rates based on their affinities for the paper and solvent.
Visualization:
7. Paper Chromatography:
Prepare Paper:
Apply a small spot of the protein sample on chromatography paper.
Solvent Migration:
Allow a solvent to migrate through the paper.
Separation:
Different proteins move at different rates based on their affinities for the paper and solvent.
Visualization:

8. Reverse-Phase Chromatography:
Prepare Column:
Use a column with a hydrophobic stationary phase.
Sample Loading:
Elution:
Elute proteins by changing the polarity of the mobile phase.
Separation:
Proteins are separated based on hydrophobic interactions.
8. Reverse-Phase Chromatography:
Prepare Column:
Use a column with a hydrophobic stationary phase.
Sample Loading:
Elution:
Elute proteins by changing the polarity of the mobile phase.
Separation:
Proteins are separated based on hydrophobic interactions.

9. Hydrophobic Interaction Chromatography (HIC):
Prepare Column:
Use a column with a material that dislikes water (hydrophobic).
Sample Loading:
Put proteins into the column.
Hydrophobic Interaction:
Proteins with hydrophobic parts stick to the material in the column.
Elution:
Change the solution to release proteins; less hydrophobic ones come out first.
Separation:
Proteins separate based on how much they dislike water.
9. Hydrophobic Interaction Chromatography (HIC):
Prepare Column:
Use a column with a material that dislikes water (hydrophobic).
Sample Loading:
Put proteins into the column.
Hydrophobic Interaction:
Proteins with hydrophobic parts stick to the material in the column.
Elution:
Change the solution to release proteins; less hydrophobic ones come out first.
Separation:
Proteins separate based on how much they dislike water.

10. Dialysis and Ultrafiltration:
Sample Containment:
Place the protein sample in a dialysis bag or ultrafiltration device.
Solvent Exchange:
Dialyze or ultrafilter the sample against a buffer to exchange solvents.
Concentration:
Concentrate the sample by removing excess solvent.
Separation:
Larger molecules are retained, while smaller molecules pass through.
10. Dialysis and Ultrafiltration:
Sample Containment:
Place the protein sample in a dialysis bag or ultrafiltration device.
Solvent Exchange:
Dialyze or ultrafilter the sample against a buffer to exchange solvents.
Concentration:
Concentrate the sample by removing excess solvent.
Separation:
Larger molecules are retained, while smaller molecules pass through.
Depending On Molecular Size

11. Gel Electrophoresis:
Gel Preparation:
Sample Loading:
Electrophoresis:
Apply an electric field. Charged molecules migrate through the gel based on size.
Visualization:
Separation:
Molecules are separated based on size.
11. Gel Electrophoresis:
Gel Preparation:
Sample Loading:
Electrophoresis:
Apply an electric field. Charged molecules migrate through the gel based on size.
Visualization:
Separation:
Molecules are separated based on size.

12. Gel Filtration Chromatography:
Prepare Column:
Set up a column with a porous gel matrix.
Sample Loading:
Elution:
Elute proteins based on their size. Larger molecules pass through the gel more quickly.
Separation:
Proteins are separated based on their size.
12. Gel Filtration Chromatography:
Prepare Column:
Set up a column with a porous gel matrix.
Sample Loading:
Elution:
Elute proteins based on their size. Larger molecules pass through the gel more quickly.
Separation:
Proteins are separated based on their size.

13. Ultracentrifugation:
Sample Loading:
Load the protein sample into ultracentrifuge tubes.
Centrifugation:
Centrifuge at high speeds to separate components based on density.
Separation:
Components separate into layers or pellets based on their densities.
13. Ultracentrifugation:
Sample Loading:
Load the protein sample into ultracentrifuge tubes.
Centrifugation:
Centrifuge at high speeds to separate components based on density.
Separation:
Components separate into layers or pellets based on their densities.

14. Affinity Chromatography:
Prepare Column:
Set up a column with a matrix containing ligands specific to the target protein.
Sample Loading:
Affinity Binding:
Target proteins selectively bind to the ligands.
Elution:
Elute the target proteins by changing conditions like pH or adding a competitive ligand.
Separation:
Target proteins are separated based on their affinity for the ligands.
14. Affinity Chromatography:
Prepare Column:
Set up a column with a matrix containing ligands specific to the target protein.
Sample Loading:
Affinity Binding:
Target proteins selectively bind to the ligands.
Elution:
Elute the target proteins by changing conditions like pH or adding a competitive ligand.
Separation:
Target proteins are separated based on their affinity for the ligands.
Depending On Binding Specificity
Depending On Binding Specificity

Determination of Peptide
Structure

WHAT ARE PEPTIDES?
A Combination of Amino Acids
Peptides makes proteins like
Collagen, Elastin & Keratin.
Crucial for maintaining the texture,
firmness, & elasticity of our skin.

Dipeptide
-A dipeptide contains 2 amino acid molecules linked by a single
peptide bond.
-Dipeptides help to maintain the pH of cells or act as
antioxidants.
-Some examples of dipeptides include carnosine, anserine, and
homoanserine.

Dipeptide
Amino acid Amino acid

Tripeptide
-Tripeptides contain 3 amino acid molecules linked by
2 peptide bonds .
-Tripeptide helps improve muscle growth and strength, as well
as to reduce fatigue and improve overall health.
-Example of tripeptides are Glutathione

Tripeptide
Amino acid Amino acid Amino acid

Oligopeptide Structure
-Oligopeptides are protein sequences ranging from 2 to 20
amino acids.
-Oligopeptide has been found to help improve digestion, reduce
inflammation, boost the immune system, and even help with
weight loss.

Polypeptide
-A polypeptide contains more than 20 amino acid molecules, and
up to 100 residues.
-Some examples of polypeptides are natriuretic peptides (a component
of snake venom), some antibiotics, and peptide hormones.

Group 5
Thank you
for listening!

PROTEIN-AND-AMINO-ACIDS-PPT.p df

Recommended

Recommended

More Related Content

Similar to PROTEIN-AND-AMINO-ACIDS-PPT.p df

Similar to PROTEIN-AND-AMINO-ACIDS-PPT.p df (20)

More from ChyeOdchigue

More from ChyeOdchigue (10)

Recently uploaded

Recently uploaded (20)

PROTEIN-AND-AMINO-ACIDS-PPT.p df