This document provides an introduction and overview of protein classification and properties. It discusses how proteins are classified based on their source, shape, composition and solubility, as well as their biological functions. Key points include that proteins are composed of amino acids and can have globular or fibrous shapes. Conjugated proteins are linked to non-protein groups. Insulin is an important protein hormone that regulates blood sugar levels and was the first to be fully sequenced. The document also examines general protein properties like molecular weight and reactions involving amino acid groups.
I have given the content as much as easy as possible. the title and content of the ppt is INTRODUCTION AND PROPERTIES OF PROTEIN which involves the physical, chemical and physio-chemical and other properties of protein.
I have given the content as much as easy as possible. the title and content of the ppt is INTRODUCTION AND PROPERTIES OF PROTEIN which involves the physical, chemical and physio-chemical and other properties of protein.
the presentation contain ways used to estimate proteins, this presentation prepared by TONNYBITE, a student from KILIMANJARO CHRISTIAN MEDICAL UNIVERSITY COLLEGE, TANZANIA
The loss of native conformation brings about changes in specific properties characterizing the identity of proteins.
Bring changes in the proteins.
It makes peptide bonds more readily available for hydrolysis by proteolytic enzymes.
Protein solubility decreased (hydrophobic groups exposed out).
Biological properties (catalytic, hormonal) are lost.
Viscosity and optical rotation increases.
the presentation contain ways used to estimate proteins, this presentation prepared by TONNYBITE, a student from KILIMANJARO CHRISTIAN MEDICAL UNIVERSITY COLLEGE, TANZANIA
The loss of native conformation brings about changes in specific properties characterizing the identity of proteins.
Bring changes in the proteins.
It makes peptide bonds more readily available for hydrolysis by proteolytic enzymes.
Protein solubility decreased (hydrophobic groups exposed out).
Biological properties (catalytic, hormonal) are lost.
Viscosity and optical rotation increases.
Proteins are naturally occurring polymers made up of amino acids and linked together by peptide bonds.
Proteins are the most abundant organic molecules in the living system.
The term "protein" is derived from the Greek word proteios, meaning holding the first place.
These are nitrogenous organic compounds that have large molecules weight of one or more long chains of amino acids.
Proteins are made from 20 ɑ-amino acids. (chains of amino acids)
A single unit of amino acid is known as a monomer. When many monomers combine together, they form polymers.
Proteins are the most abundant organic molecules of the living system.
They occur in every part of the cell and constitute about 50% of the cellular dry weight.
Proteins form the fundamental basis of structure and function of life.
Amino acids are the monomers that make up proteins
• Description: In this video the viewers will come to know about different mode of classification of proteins. Proteins are classified based on their Solubility and composition, Function, Shape & size.
Portion explained:
Classification based on solubility and composition
Simple proteins
1. Albumins
2. Globulins
3. Prolamins
4. Glutelins
5. Histones
6. Protamines
7. Albuminoids
ii. Conjugated or compound proteins
1. Nucleoproteins
2. Mucoproteins
3. Chromoproteins
4. Lipoproteins
5. Metalloproteins
6. Phosphoproteins
B. Classification of proteins based on function
1. Catalytic proteins – Enzymes
2. Regulatory proteins – Hormones
3. Protective proteins – Antibodies
4. Storage proteins
5. Transport proteins
6. Toxic proteins
7. Structural proteins
8. Contractile proteins
9. Secretary proteins
10. Exotic proteins
C. Classification based on size and shape
Cancer cell metabolism: special Reference to Lactate PathwayAADYARAJPANDEY1
Normal Cell Metabolism:
Cellular respiration describes the series of steps that cells use to break down sugar and other chemicals to get the energy we need to function.
Energy is stored in the bonds of glucose and when glucose is broken down, much of that energy is released.
Cell utilize energy in the form of ATP.
The first step of respiration is called glycolysis. In a series of steps, glycolysis breaks glucose into two smaller molecules - a chemical called pyruvate. A small amount of ATP is formed during this process.
Most healthy cells continue the breakdown in a second process, called the Kreb's cycle. The Kreb's cycle allows cells to “burn” the pyruvates made in glycolysis to get more ATP.
The last step in the breakdown of glucose is called oxidative phosphorylation (Ox-Phos).
It takes place in specialized cell structures called mitochondria. This process produces a large amount of ATP. Importantly, cells need oxygen to complete oxidative phosphorylation.
If a cell completes only glycolysis, only 2 molecules of ATP are made per glucose. However, if the cell completes the entire respiration process (glycolysis - Kreb's - oxidative phosphorylation), about 36 molecules of ATP are created, giving it much more energy to use.
IN CANCER CELL:
Unlike healthy cells that "burn" the entire molecule of sugar to capture a large amount of energy as ATP, cancer cells are wasteful.
Cancer cells only partially break down sugar molecules. They overuse the first step of respiration, glycolysis. They frequently do not complete the second step, oxidative phosphorylation.
This results in only 2 molecules of ATP per each glucose molecule instead of the 36 or so ATPs healthy cells gain. As a result, cancer cells need to use a lot more sugar molecules to get enough energy to survive.
Unlike healthy cells that "burn" the entire molecule of sugar to capture a large amount of energy as ATP, cancer cells are wasteful.
Cancer cells only partially break down sugar molecules. They overuse the first step of respiration, glycolysis. They frequently do not complete the second step, oxidative phosphorylation.
This results in only 2 molecules of ATP per each glucose molecule instead of the 36 or so ATPs healthy cells gain. As a result, cancer cells need to use a lot more sugar molecules to get enough energy to survive.
introduction to WARBERG PHENOMENA:
WARBURG EFFECT Usually, cancer cells are highly glycolytic (glucose addiction) and take up more glucose than do normal cells from outside.
Otto Heinrich Warburg (; 8 October 1883 – 1 August 1970) In 1931 was awarded the Nobel Prize in Physiology for his "discovery of the nature and mode of action of the respiratory enzyme.
WARNBURG EFFECT : cancer cells under aerobic (well-oxygenated) conditions to metabolize glucose to lactate (aerobic glycolysis) is known as the Warburg effect. Warburg made the observation that tumor slices consume glucose and secrete lactate at a higher rate than normal tissues.
Richard's entangled aventures in wonderlandRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
Seminar of U.V. Spectroscopy by SAMIR PANDASAMIR PANDA
Spectroscopy is a branch of science dealing the study of interaction of electromagnetic radiation with matter.
Ultraviolet-visible spectroscopy refers to absorption spectroscopy or reflect spectroscopy in the UV-VIS spectral region.
Ultraviolet-visible spectroscopy is an analytical method that can measure the amount of light received by the analyte.
A brief information about the SCOP protein database used in bioinformatics.
The Structural Classification of Proteins (SCOP) database is a comprehensive and authoritative resource for the structural and evolutionary relationships of proteins. It provides a detailed and curated classification of protein structures, grouping them into families, superfamilies, and folds based on their structural and sequence similarities.
Slide 1: Title Slide
Extrachromosomal Inheritance
Slide 2: Introduction to Extrachromosomal Inheritance
Definition: Extrachromosomal inheritance refers to the transmission of genetic material that is not found within the nucleus.
Key Components: Involves genes located in mitochondria, chloroplasts, and plasmids.
Slide 3: Mitochondrial Inheritance
Mitochondria: Organelles responsible for energy production.
Mitochondrial DNA (mtDNA): Circular DNA molecule found in mitochondria.
Inheritance Pattern: Maternally inherited, meaning it is passed from mothers to all their offspring.
Diseases: Examples include Leber’s hereditary optic neuropathy (LHON) and mitochondrial myopathy.
Slide 4: Chloroplast Inheritance
Chloroplasts: Organelles responsible for photosynthesis in plants.
Chloroplast DNA (cpDNA): Circular DNA molecule found in chloroplasts.
Inheritance Pattern: Often maternally inherited in most plants, but can vary in some species.
Examples: Variegation in plants, where leaf color patterns are determined by chloroplast DNA.
Slide 5: Plasmid Inheritance
Plasmids: Small, circular DNA molecules found in bacteria and some eukaryotes.
Features: Can carry antibiotic resistance genes and can be transferred between cells through processes like conjugation.
Significance: Important in biotechnology for gene cloning and genetic engineering.
Slide 6: Mechanisms of Extrachromosomal Inheritance
Non-Mendelian Patterns: Do not follow Mendel’s laws of inheritance.
Cytoplasmic Segregation: During cell division, organelles like mitochondria and chloroplasts are randomly distributed to daughter cells.
Heteroplasmy: Presence of more than one type of organellar genome within a cell, leading to variation in expression.
Slide 7: Examples of Extrachromosomal Inheritance
Four O’clock Plant (Mirabilis jalapa): Shows variegated leaves due to different cpDNA in leaf cells.
Petite Mutants in Yeast: Result from mutations in mitochondrial DNA affecting respiration.
Slide 8: Importance of Extrachromosomal Inheritance
Evolution: Provides insight into the evolution of eukaryotic cells.
Medicine: Understanding mitochondrial inheritance helps in diagnosing and treating mitochondrial diseases.
Agriculture: Chloroplast inheritance can be used in plant breeding and genetic modification.
Slide 9: Recent Research and Advances
Gene Editing: Techniques like CRISPR-Cas9 are being used to edit mitochondrial and chloroplast DNA.
Therapies: Development of mitochondrial replacement therapy (MRT) for preventing mitochondrial diseases.
Slide 10: Conclusion
Summary: Extrachromosomal inheritance involves the transmission of genetic material outside the nucleus and plays a crucial role in genetics, medicine, and biotechnology.
Future Directions: Continued research and technological advancements hold promise for new treatments and applications.
Slide 11: Questions and Discussion
Invite Audience: Open the floor for any questions or further discussion on the topic.
Professional air quality monitoring systems provide immediate, on-site data for analysis, compliance, and decision-making.
Monitor common gases, weather parameters, particulates.
2. INTRODUCTION
• Protein name is derived from a
Greek word PROTOS which
mean “ the first or supreme”.
• Protein are extremely
complicated .
• 20 amino acids which have been
found to occur in all proteins,
known as standard amino acid.
• 21st amino acid; Selenocysteine
• 22nd amino acid; Pyrrolysine
4. CLASSIFICATION BASED ON THE
SOURCE OF PROTEIN MOLECULE
• Animal proteins are the proteins derived from animal sources such as eggs,
milk, meat and fish. They are usually called higher-quality proteins.
• On the other hand, plant proteins are called lower-quality proteins.
• The four most common limiting amino acids are methionine, lysine,
threonine and tryptophan.
5. CLASSIFICATION BASED ON THE SHAPE OF
PROTEIN MOLECULE
Globular protein or Corpuscular Proteins :-
• These have an axial ratio (length : width) of less than 10 (usually not over 3 or 4) and,
henceforth, possess a relatively spherical or ovoid shape.
• These are usually soluble in water.
How can we remember the examples:- GHARMII
• G Globin (protein part of Haemoglobin)
• H Histone (Eukaryotic DNA)
• A Albumin (Maintain BCOP*)
• R Rubisco ( Enzyme in Calvin cycle)
• M Myoglobin ( Pigment in muscle for O2 transport)
• I Insulin (Pancreatic hormone)
• I Immunoglobulin's (Antibodies)
• (BCOP*= Blood colloidal osmotic pressure)
6. Fibrous Proteins or Fibrillar Proteins:-
• These have axial ratios greater than 10 and, henceforth, resemble long ribbons
or fiber in shape.
• These are mainly of animal origin and are insoluble in all common solvents
such as water, dilute acids, alkalies and salts and also in organic solvents.
• The fibrous proteins are extremely strong and possess two important properties
which are characteristic of the elastomers. These are
A. They can stretch and later recoil to their original length.
B. They have a tendency to creep
Fibrous proteins
• Collagens.
• Elastins
• Keratins
• Fibroin.
7. CLASSIFICATION BASED ON COMPOSITIONAND
SOLUBILITY
Simple Proteins
These are of globular
type. This group
includes proteins
containing only amino
acids.
• Protamines (Arginine
rich)and
histones(Arginine and
lysine)
• Albumins; water soluble
• Globulins; insoluble in
water
• Globins; rich in histidine
• Prolamines; present in
sperm cells
• Scleroproteins or
Albuminoids
Conjugated Proteins
These are the proteins
linked with a separable
nonprotein portion
called prosthetic group.
• Metalloproteins
• Chromoproteins.
• Glycoproteins and
Mucoprotein
• Phosphoproteins
• Lipoproteins
• Nucleoproteins
Derived Proteins
Protein derived from
simple and conjugated
protein by chemical and
physical treatment.
I. Primary derived
proteins.(insoluble in
water)
• Metaproteins or
Infraproteins
• Coagulated Proteins
II. Secondary derived
proteins.(soluble in water)
• Proteoses
• Polypeptides
8.
9. Conjugated proteins Protein part Prosthetic group
Haemoglobin
(transfer of oxygen in
body from lungs to the
tissue)
Globin Heme
(bone marrow and liver)
Nucleoprotein
( transcription, translation,
regulating gene
expression)
Histones DNA
Rhodopsin
( the primary
photoreceptor molecule
of vission)
Opsin 11-cis-retinal
(Vit. A aldehyde)
Ferritin
(store iron inside the cell)
Aproferritin Iron
Lipoprotein
(they carry cholesterol
through the blood stream
to the cell)
Protein Lipid (Fats)
13. EGG PROTEINS:-
The eggs and milk are consumed as food by an appreciable portion of the
global population. Hence, the egg and milk proteins deserve a special mention.
Eggs contain 2 types of proteins : the egg white protein and egg yolk protein.
Egg yolk contains 2 phosphoproteins, lipovitellin and lipovitellenin.
Egg yolk also contains water-soluble protein that does not precipitate on dilution
of the yolk. This fraction is called livetin.
Whole egg is an excellent food because it is a very rich source not only of
protein and lipid but also of most of the vitamins (except vitamin C) and most of
the required minerals (except calcium).
14. General Properties
1) Colour and Taste.
2) Shape and Size.
3) Molecular Weight.
4) Colloidal Nature.
5) Amphoteric Nature.
6) Solubility.
PHYSICAL CHEMICAL
A. Hydrolysis.
B. Reactions Involving
COOH Group.
C. Reactions Involving NH2
Group.
D. Reactions Involving Both
COOH And NH2 Groups.
E. Reactions Involving R
Group Or Side Chain.
15.
16.
17. Chemical properties
A. HYDROLYSIS:- (using acidic group)
B. REACTIONS INVOLVING COOH GROUP
• Reaction with alkalies (Salt formation)
• Reaction with alcohols (Esterification)
18. • Reaction with amine:-
C. REACTIONS INVOLVING NH2 GROUP:-
• Reaction with mineral acids (Salt formation)
D. REACTIONS INVOLVING BOTH COOH AND NH2 GROUPS:-
• Reaction with phosgene
19. PHYSICALAGENTS:-
Heat, UV, high pressure.
CHEMICALAGENTS:-
Acids, alkalis, heavy metals, detergents(SDS), urea etc.
EXAMPLE OF DENATURATION:- PANEER
EXAMPLE OF RENATURATION:- SDS denaturation can be reversed
20. E. REACTIONS INVOLVING R GROUP OR SIDE CHAIN:-
• Colour reactions for specific amino acids
21. INSULIN:-
• Insulin ( from Latin insula, 'island').
• It is considered to be the main anabolic hormone of the body.
• Porcine insulin is especially close to the human version, and was
widely used to treat type 1 diabetics before human insulin could be
produced in large quantities by recombinant DNA technologies.
• Frederick Sanger sequenced the amino acid structure in 1951,
which made insulin the first protein to be fully sequenced.
• Insulin is also the first protein to be chemically synthesized and
produced by DNA recombinant technology.
• Researchers have succeeded in introducing the gene for human
insulin into plants as another method of producing insulin
("biopharming") in safflower. This technique is anticipated to reduce
production costs.