TANUJ SANJAY MAHALE

FYBSc (FORENSIC SCIENCE)

ROLL NO.:- IFBS154

SEAT NO:-25360023

SUBJECT:- INTRODUCTION TO FORENSIC BIOLOGY

TOPIC:- AMINO ACID – DEFINITION,STRUCTURE,CLASSSIFICATION AND ISOELECTRIC POINT

ASSIGNMENT
AMINO ACID DEFINATION:-

Amino acids serve as fundamental building blocks of proteins being organic compounds
crucial for various bodily functions essentially everywhere. A central alpha carbon atom
bonded four key groups characterizes them and an amino group acts as base quite
effectively.- A carboxyl group (–COOH): This group acts as an acid.

- A hydrogen atom (–H): A standard component in creating the molecular structure.

- A unique side chain (R-group): This variable group differentiates one amino acid from
another and largely determines its chemical behavior.

A carboxyl group denoted by –COOH acts somewhat acidly. A hydrogen atom denoted –H
serves as standard component pretty much always in molecular structure creation
endeavors basically. A unique side chain known as R-group differentiates one amino acid
from another largely determining its chemical behavior quite variably. Amino acids join
together through dehydration synthesis forming peptide bonds and creating rather lengthy
polypeptides suddenly.

STRUCTURE OF AMINO ACID:-

Amino acids possess a fundamental structure consisting of a central carbon atom bonded
rather tightly to four quite distinct groups. Characteristic structure manifests thus: H₂N — C
— COOH flanked by H above and R below with amino group –NH₂ serving as base donating
electron pair freely.

Representation involves H stuck between H₂N — C — COOH and R somehow.

Each part breaks down differently with –NH₂ acting very basically and quite freely donating
an electron pair meanwhile somehow staying attached. Presence of it renders amino acid
able to form peptide bonds quite readily with myriad other amino acid molecules.-

Carboxyl Group (–COOH):

Acting as an acid, this group contributes to the acid-base properties of the amino acid.
Acting as an acid this group contributes heavily to acid-base properties of amino acid fairly
significantly somehow.-
Hydrogen Atom (–H):

A single hydrogen atom is bonded to the alpha carbon, which, along with the other groups,
contributes to the overall structure.

Side Chain (R Group):

This variable group is what differentiates one amino acid from another. It can readily
surrender a proton H⁺ during various complex biochemical reactions occurring inside cells
under specific conditions normally. A single hydrogen atom bonds to alpha carbon and
contributes heavily alongside other groups to overall molecular structure. A variable group
known as side chain or R group differentiates one amino acid quite significantly from
another. Side chains range from incredibly simple hydrogen atoms found in glycine
molecules to fairly complex aromatic rings similar to those found in phenylalanine. Chemical
nature of R group dictates amino acid polarity charge and reactivity profoundly influencing
proteins' 3D structure and functional roles somewhat irregularly. Chirality plays a crucial
role in amino acid structure often manifesting quite subtly yet profoundly affecting overall
molecular configuration.

CLASSIFICATION OF AMINO ACID:-

Amino acids get categorized variously and grasping such classifications proves pivotal in
biology for appreciating their multifaceted roles somewhat effectively. Two main
approaches exist generally nowadays. Amino acid chemical properties largely depend on
nature of side chain or R group attached quite irregularly to central α carbon. Nonpolar
amino acids contain mostly aliphatic or sometimes aromatic side chains generally not
interacting very well with water. They cluster tightly together inside proteins stabilizing
folded structure deeply.**Examples:** Glycine (Gly), Alanine (Ala), Valine (Val), Leucine
(Leu), Isoleucine (Ile), Proline (Pro), Phenylalanine (Phe), and Tryptophan (Trp).

Polar (Hydrophilic) Amino Acids:

These amino acids have side chains that can form hydrogen bonds with water, and they
often tend to be found on the protein surface. Glycine abbreviated as Gly and Alanine
dubbed Ala are accompanied by Valine or Val Leucine nicknamed Leu and Isoleucine tagged
Ile.**Examples:** Serine (Ser), Threonine (Thr), Cysteine (Cys), Asparagine (Asn), Glutamine
(Gln), and Tyrosine (Tyr).

Charged Amino Acids:

Their side chains bear either a positive or negative charge at physiological pH, which plays
critical roles in enzyme activity and substrate binding.

Acidic (Negatively Charged):

Examples: Aspartic acid (Asp) and Glutamic acid (Glu).

Basic (Positively Charged):

Examples: Lysine (Lys), Arginine (Arg), and Histidine (His).

2. Polar hydrophilic amino acids have side chains that form hydrogen bonds readily with
water and tend often to reside on protein surfaces. Uncharged polar amino acids have side
chains that remain polar yet harbour no net charge at physiological pH basically.-

Non-Essential Amino Acids:

The body can produce these amino acids internally, so they do not necessarily need to come
from the diet. Examples include Serine or Ser Asparagine aka Asn and Tyrosine known as Tyr
quite frequently in various biochemical contexts obviously
Conditional Amino Acids:

Under normal conditions these amino acids are synthesizable by the body; however, during
periods of stress, illness, or rapid growth, their synthesis might not meet the body’s
demand. Amino acids bearing charges have side chains with either positive or negative
electrical properties at physiological pH playing crucial roles in enzyme activity.---

Why These Classifications Matter

Functional Implications: The chemical properties derived from the side chain
(hydrophobicity, charge, size, etc.) influence protein folding, structure, and function.
Negatively charged acidic examples include aspartic acid and glutamic acid often denoted by
abbreviations Asp and Glu respectively.-

Nutritional Considerations: Understanding which amino acids are essential helps guide
dietary choices to support proper health and metabolism, especially since proteins are
critical for tissue repair, enzymatic reactions, and overall cellular function.

Biochemical Pathways: The classification also informs us about metabolic pathways—for

example, how amino acids are converted into energy, or how they contribute to
synthesizing neurotransmitters and other biomolecules.

Basic positively charged amino acids include Lysine abbreviated as Lys and Arginine often
denoted Arg and Histidine frequently shortened to His.
ISOELECTRIC POINT OF AMINO ACID:-

Amino acid molecules bear no net electrical charge whatsoever at a specific pH known
rather obscurely as their isoelectric point or pI. At this specific pH positive charges and
negative charges on amino acid balance out and it exists predominantly as a zwitterion with
overall neutrality.---

How pI Is Determined

For amino acids without ionizable side chains:

Most amino acids have two main ionizable groups:

1. Carboxyl Group (-COOH):

- Typically has a pKa in the range of 2.0–2.5.

2. Amino Group (-NH₃⁺):

- Typically has a pKa in the range of 9.0–9.8.

The isoelectric point is calculated by taking the arithmetic mean of the pKa values of these
two groups:

Example with Glycine:

- pKa (COOH) ≈ 2.34

- pKa (NH₃⁺) ≈ 9.60

For amino acids with ionizable side chains:

Some amino acids have extra ionizable groups in their side chains. pI determination occurs
mostly for amino acids lacking ionizable side chains and having just two main ionizable
groups ordinarily present. Typically carboxyl group denoted as -COOH has a pKa somewhere
around 2.0 to 2.5 roughly.- **Acidic Amino Acids (e.g., Aspartic Acid):**

- Groups:

- α-COOH (pKa ≈ 2.1)

- Side chain COOH (pKa ≈ 3.9)

- α-NH₃⁺ (pKa ≈ 9.8)

- pI is calculated by averaging the two lowest pKa values (since deprotonation of the acidic
groups leads to neutrality):

Basic Amino Acids (e.g., Lysine):

- Groups:

- α-COOH (pKa ≈ 2.2)

- α-NH₃⁺ (pKa ≈ 8.9)

- Side chain NH₃⁺ (pKa ≈ 10.5)

- pI is calculated by averaging the two highest pKa values (since the basic groups remain
protonated until a higher pH):

At the isoelectric point, despite the presence of ionizable groups, their charges cancel each
other, making the net charge zero. Amino group -NH₃⁺ ordinarily exhibits pKa values ranging
roughly from 9.0 to 9.8 pretty much everywhere.

Isoelectric point gets calculated by averaging pKa values of COOH group and NH₃⁺ group
pretty simply.

pI equals roughly half sum of pKa COOH and pKa NH₃⁺.

Glycine has pKa COOH around 2.34 and pKa NH₃⁺ around 9.60.

pI of glycine approximately equals average of 2.34 and 9.60 which is roughly 5.97.

Amino acids having ionizable side chains possess extra ionizable groups within their side
chains normally

Visualizing the Concept

Below is a simple ASCII infographic to summarize the concept:
At the isoelectric point, despite the presence of ionizable groups, their charges cancel each
other, making the net charge zero. This property is key in protein biochemistry—for
instance, it affects protein solubility and movement in an electric field during techniques like
isoelectric focusing.