all about protiens there types there application and so on.....

1. What are proteins?
Proteins are complex macromolecules that are essential for a wide
variety of biological processes. Here are 15 points to explain what
proteins are:
1.Proteins are large molecules made up of one or more polypeptide
chains, which are long chains of amino acids linked together by
peptide bonds.
2.There are 20 different types of amino acids that can be
incorporated into a polypeptide chain, each with a different side
chain that determines its unique properties.
3.The sequence of amino acids in a polypeptide chain is determined
by the genetic code, which specifies the order of nucleotides in DNA
or RNA.
4.The primary structure of a protein refers to the linear sequence of
amino acids in a polypeptide chain.
5.The secondary structure of a protein refers to the regular patterns

2. 6.The tertiary structure of a protein refers to the overall three-dimensional shape of a polypeptide chain, which is critical to
its function.
7.The quaternary structure of a protein refers to the arrangement of multiple polypeptide chains into a larger protein
complex.
8.Proteins can have a wide variety of functions, including catalyzing chemical reactions, providing structural support, and
transporting molecules.
9.Enzymes are a type of protein that catalyze chemical reactions by lowering the activation energy required for the
reaction to occur.
10,Antibodies are a type of protein that play a critical role in the immune system by recognizing and binding to foreign
molecules.
11.Hormones are a type of protein that regulate a wide variety of physiological processes, including growth and
development, metabolism, and reproduction.
12.Proteins can be synthesized by cells using the process of translation, which involves the ribosome reading the genetic
code and assembling a polypeptide chain from amino acids.
13.Proteins can also be modified after they are synthesized, for example through the addition of sugar molecules or lipid
groups.
14.Misfolding of proteins can result in a variety of diseases, including Alzheimer's disease, Parkinson's disease, and prion
diseases.

3. 15
min
Importance of protein in chemical engineering
Proteins are important in chemical engineering due to their unique properties and functions. Here are
10 points explaining the importance of proteins in chemical engineering:
1.Protein engineering: Chemical engineers can engineer proteins to have specific properties or
functions that are useful for a variety of applications, such as creating new biocatalysts or drug
delivery systems.
2.Biocatalysis: Proteins, such as enzymes, can be used as catalysts in various chemical reactions,
allowing for more sustainable and efficient processes.
3.Bioreactor design: Chemical engineers can design bioreactors to cultivate cells and
microorganisms that produce specific proteins, which can then be harvested and purified for various
applications.
4.Biosensors: Proteins can be used in biosensors to detect specific molecules or conditions, such as
glucose levels in blood or environmental pollutants.
5.Protein purification: Chemical engineers can develop and optimize methods for purifying proteins,
which is essential for many applications, such as the production of biologics.

4. 15
min
Importance of protein in chemical engineering
6.Protein stability: Chemical engineers can study protein stability in different environments, such as
extreme temperatures or pH conditions, to optimize their function and stability for specific
applications.
7.Protein-protein interactions: Understanding protein-protein interactions is critical for many
applications, such as drug discovery and development.
8.Protein-based materials: Chemical engineers can develop protein-based materials, such as
scaffolds for tissue engineering or biodegradable packaging.
9.Protein expression systems: Chemical engineers can optimize protein expression systems to
produce high yields of recombinant proteins for various applications.
10.Protein-based therapeutics: Many protein-based drugs have been developed for various
diseases, such as monoclonal antibodies for cancer treatment, highlighting the importance of
proteins in chemical engineering for pharmaceutical development.

5. Classifacition of protiens
Classification of protiens
Primary structure Secondary structure Tertiary structure Quaternary structure
Primary structure
refers to the linear
sequence of amino
acids in a protein chain.
The order of amino
acids is determined by
the genetic code, which
specifies the sequence
of nucleotides in DNA.
Secondary structure
refers to the local
folding patterns that
occur within a protein
chain, such as alpha-
helices and beta-
sheets. These
structures are stabilized
by hydrogen bonds
between the amino
acid residues.
Quaternary structure
refers to the
arrangement of
multiple protein
subunits into a larger,
functional protein
complex. Examples of
quaternary structures
include hemoglobin,
which is composed of
four subunits, and
antibodies, which are
composed of two
heavy chains and two
light chains.
Tertiary structure refers
to the overall 3D shape
of a protein, which is
determined by
interactions between
the amino acid side
chains. These
interactions can include
hydrogen bonds,
disulfide bonds,
hydrophobic
interactions, and
electrostatic
interactions.

6. 1.PRIMARY PROTIENS
Primary proteins are the most basic level of protein structure,
referring to the sequence of amino acids in a polypeptide
chain. Here are 10 points on primary proteins:
1.Primary proteins are also known as the first level of protein
structure, as they represent the linear sequence of amino
acids.
2.The sequence of amino acids in a protein determines the
folding and shape of the protein, which ultimately determines
its function
3.There are 20 different types of amino acids that can be
combined in any order to form a protein's primary structure.
4.The sequence of amino acids in a protein is determined by
the sequence of nucleotides in the DNA that codes for the
protein.
5.Errors or mutations in the DNA sequence can result in
changes in the amino acid sequence, leading to altered
protein function or disease.

7. 1.PRIMARY PROTIENS
6. The primary structure of a protein is critical to its function,
as even minor changes to the amino acid sequence can lead
to altered protein function or loss of function.
7. The primary structure of a protein can be determined
experimentally using techniques such as X-ray
crystallography, NMR spectroscopy, or mass spectrometry.
8. The primary structure of a protein can also be predicted
computationally based on the protein's amino acid sequence
and knowledge of protein folding patterns.
9.Post-translational modifications can also affect the primary
structure of a protein, such as the addition or removal of
amino acid residues.
10.Understanding the primary structure of a protein is a
critical first step in understanding its structure, function, and
potential roles in disease or therapeutic development.

8. 2. SECONDARY PROTIENS
Secondary proteins are the second level of protein structure, referring to
the regular patterns of folding and coiling that occur in a polypeptide
chain. Here are 10 points on secondary proteins:
1.Secondary proteins are formed by the folding of the polypeptide chain
into regular, repeating patterns.
2.The two most common types of secondary structures are alpha helices
and beta sheets.
3.Alpha helices are formed by the coiling of the polypeptide chain into a
helical structure stabilized by hydrogen bonding between nearby amino
acids.
4.Beta sheets are formed by the folding of the polypeptide chain into a
sheet-like structure stabilized by hydrogen bonding between adjacent
strands.
5.Other types of secondary structures include beta turns and loop
regions.

9. 2. SECONDARY PROTIENS
6.The formation of secondary structures is driven by the interactions
between amino acid side chains and the backbone of the
polypeptide chain.
7.The secondary structure of a protein can be predicted
computationally based on the protein's amino acid sequence and
knowledge of protein folding patterns.
8.The secondary structure of a protein can also be determined
experimentally using techniques such as X-ray crystallography,
NMR spectroscopy, or circular dichroism.
9.The secondary structure of a protein can affect its function and
stability, as well as its interactions with other molecules.
10.Understanding the secondary structure of a protein is important
for understanding its overall three-dimensional structure, function,
and potential roles in disease or therapeutic development.

10. 2. TERTIARY PROTIENS
Tertiary proteins are the third level of protein structure, referring to the overall three-
dimensional structure of a polypeptide chain. Here are 10 points on tertiary proteins:
1.Tertiary proteins are formed by the folding of the polypeptide chain into a compact,
three-dimensional structure.
2.The folding of a protein is driven by a combination of interactions between the amino
acid side chains and the backbone of the polypeptide chain, as well as interactions
with the surrounding environment.
3.The overall shape of a protein is critical to its function, as it determines the way that
the protein interacts with other molecules.
4.The tertiary structure of a protein can be predicted computationally based on the
protein's amino acid sequence and knowledge of protein folding patterns.
5.The tertiary structure of a protein can also be determined experimentally using
techniques such as X-ray crystallography, NMR spectroscopy, or cryo-electron
microscopy.

11. 2. TERTIARY PROTIENS
6.The tertiary structure of a protein can be stabilized by a variety of
interactions, including hydrogen bonds, van der Waals interactions,
hydrophobic interactions, and disulfide bonds.
7.Proteins with similar amino acid sequences often have similar tertiary
structures, although there can be significant variation in structure even
between closely related proteins.
8.Changes to the amino acid sequence of a protein can result in changes
to the protein's tertiary structure, which can affect its function.
9.Misfolding of proteins can result in a variety of diseases, including
Alzheimer's disease, Parkinson's disease, and prion diseases.
10.Understanding the tertiary structure of a protein is critical to
understanding its function, potential roles in disease or therapeutic
development, and interactions with other molecules.

12. 2. Quaternary proteins are the fourth level of protein structure, referring to
the arrangement of multiple polypeptide chains into a larger protein
complex. Here are 10 points on quaternary proteins:
1.Quaternary proteins are formed by the association of two or more
polypeptide chains into a larger protein complex.
2.The individual polypeptide chains, or subunits, can be identical or
different, and may be held together by a variety of interactions.
3.The interactions between subunits can include hydrogen bonds, van
der Waals interactions, hydrophobic interactions, and disulfide bonds.
4.The quaternary structure of a protein can significantly impact its
function and stability, as well as its interactions with other molecules.
5.The quaternary structure of a protein can be predicted computationally
based on the amino acid sequences of the individual subunits and
knowledge of protein folding patterns.
Quaternary proteins

13. Quaternary proteins
6.The quaternary structure of a protein can also be determined
experimentally using techniques such as X-ray crystallography, NMR
spectroscopy, or cryo-electron microscopy.
7.Changes to the amino acid sequence of one subunit can affect the
interactions between subunits and alter the quaternary structure of a
protein.
8.Many proteins have quaternary structures, including enzymes,
antibodies, and transport proteins.
9.Protein complexes with multiple subunits can provide a higher degree of
regulation and specificity in their interactions with other molecules.
10.Understanding the quaternary structure of a protein is important for
understanding its function, potential roles in disease or therapeutic
development, and interactions with other molecules.

14. Types of protien
1.Enzymes
2.Transport proteins
3.Hormones
4.Antibodies
5.Signaling proteins
6.Regulatory proteins
7.Motor proteins
8.Storage proteins

15. Types of protien
Enzymes
These proteins catalyze chemical reactions in
the body, such as breaking down food
molecules or building new molecules.
Examples include amylase, lactase, and
protease.
These proteins move molecules or ions
across cell membranes or throughout the
body. Examples include hemoglobin, which
carries oxygen in the blood, and ion channels,
which allow ions to pass through cell
membranes.
These proteins act as signaling
molecules that regulate various
physiological processes. Examples
include insulin, growth hormone, and
thyroid hormone.
Hormones:
Transport proteins Antibodies:
These proteins are produced by the immune
system to help identify and neutralize foreign
invaders, such as viruses or bacteria

16. Types of protien
Motor proteins
These proteins generate movement and
force within cells. Examples include
myosin and actin, which are involved in
muscle contraction, and kinesin and
dynein, which transport materials within
cells.
these proteins regulate various cellular
processes by transmitting signals between
cells. Examples include receptors, growth
factors, and cytokines.
These proteins store nutrients, such as
amino acids or iron, for later use by the
body. Examples include ferritin, which stores
iron, and casein, which is a major protein in
milk.
Storage proteins
Signaling proteins: Regulatory
proteins:
These proteins control gene expression
or other cellular processes. Examples
include transcription factors and histones.

17. 15
min
5. Activity – Evil scientist’s council
Tools
Device with LifeLiqe – “HIV virus” 3D model, Internet connection.
Instructions
Open Lifeliqe “HIV virus” model and show it to the class. If you have a tablet, use it as your
“picture” through role play of an evil scientist. Talk about HIV as your virus which will rule the
world, structuring text on the ideas from the bulletins in a following point. It should look like:
Glad to see everyone on the evil council. I present to you my HIV virus. Its symptoms diversifies
from person to person, but mostly in the first stage people become acutely ill, having flu-like
symptoms (fever, sore throat, headaches). However, the virus cannot be destroyed, even if the
first acute illnesses diminish. It prevails silently in the second stage making its host look
healthy and then, in the last stage, virus unleashes a full attack, destroying the victim’s
immune system. From now on, it keeps victim’s defense very weak so even the ordinary
curable illnesses can become a serious threat, even fatal. The Infected host then becomes a
medium to transfer the virus through sexual intercourse, sharing injections when taking drugs
or even through blood transfusions. People with a weaker immune system are more likely to
get it. There is no cure for it yet, but many supportive treatments can cause it to rapidly slow
down the evolution process and keep its host relatively healthy and long-living. Pretty evil,
don’t you think?
Click to open in Lifeliqe

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