The document summarizes a biochemistry group project on proteins. The group, led by Mohammad Raes, discussed the definition, chemistry, structure, classification, properties, and functions of proteins. Key points included that proteins are polymers of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. Proteins perform important roles such as enzymes, hormones, antibodies, and structure.
20.1 Characteristics of Proteins
20.2 Amino Acids: The Building Blocks for Proteins
20.3 Essential Amino Acids
20.4 Chirality and Amino Acids
20.5 Acid–Base Properties of Amino Acids
20.6 Cysteine: A Chemically Unique Amino Acid
20.7 Peptides
20.8 Biochemically Important Small Peptides
20.9 General Structural Characteristics of Proteins
20.10 Primary Structure of Proteins
20.11 Secondary Structure of Proteins
20.12 Tertiary Structure of Proteins
20.13 Quaternary Structure of Proteins
20.14 Protein Hydrolysis
20.15 Protein Denaturation
20.16 Protein Classification Based on Shape
20.17 Protein Classification Based on Function
20.18 Glycoproteins
20.19 Lipoproteins
Amino acids have properties that are well-suited to carry out a variety of biological functions
Capacity to polymerize
Useful acid-base properties
Varied physical properties
Varied chemical functionality
What are Peptides Difference between Peptides and ProteineMatt Stan
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Cofactor of Enzymes
Mohammed Haddad
PHD Student
Prof . Dr. Emine Karaku
A cofactor is a non-protein chemical compound that is required for the protein's biological activity. These proteins are commonly enzymes, and cofactors can be considered "helper molecules" that assist in biochemical transformations.
20.1 Characteristics of Proteins
20.2 Amino Acids: The Building Blocks for Proteins
20.3 Essential Amino Acids
20.4 Chirality and Amino Acids
20.5 Acid–Base Properties of Amino Acids
20.6 Cysteine: A Chemically Unique Amino Acid
20.7 Peptides
20.8 Biochemically Important Small Peptides
20.9 General Structural Characteristics of Proteins
20.10 Primary Structure of Proteins
20.11 Secondary Structure of Proteins
20.12 Tertiary Structure of Proteins
20.13 Quaternary Structure of Proteins
20.14 Protein Hydrolysis
20.15 Protein Denaturation
20.16 Protein Classification Based on Shape
20.17 Protein Classification Based on Function
20.18 Glycoproteins
20.19 Lipoproteins
Amino acids have properties that are well-suited to carry out a variety of biological functions
Capacity to polymerize
Useful acid-base properties
Varied physical properties
Varied chemical functionality
What are Peptides Difference between Peptides and ProteineMatt Stan
At Peptides 411 you get the entire scoop. What are peptides? The difference between Peptides and Proteins. Where to buy peptides and how to get the lowest prices.
Cofactor of Enzymes
Mohammed Haddad
PHD Student
Prof . Dr. Emine Karaku
A cofactor is a non-protein chemical compound that is required for the protein's biological activity. These proteins are commonly enzymes, and cofactors can be considered "helper molecules" that assist in biochemical transformations.
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
essential topic on bio molecule:
They are naturally occurring polypeptides that contain more than 50 amino acid units. therefore a protein is a hetero polymer.
Most abundant organic molecules of the living system.
They form about 50% of the dry weight of the cell.
They are most important for the architecture and functioning
of the cell.
Proteins on complete hydrolysis yields Amino Acids
There are 20 standard amino acids which are repeatedly found in the structure of proteins – animal, plant or microbial.
Collagen is the most abundant animal protein and Rubisco is the most abundant plant protein
Protein Synthesis is controlled by DNA.
They are substituted methane (CH4)
Amino acids are group of organic compounds having 2 functional groups (-NH2) and (-COOH)
(-NH2) group is basic whereas (-COOH) is acidic
R- can be H in glycine, CH3 in alanine, Hydroxymethyl in serine
in others it can be hydrocarbon chain or a cyclic group
All amino acids contain C, H, O and N but some of them additionally contain S
Physical and chemical properties of amino acids are due to amino, carboxyl and R functional groups
Quantitative estimation of protein Likhith KLIKHITHK1
Proteins are polypeptide structures consisting of one or more long chains of amino acid residues. They carry out a wide variety of organism functions, including DNA replication, transporting molecules, catalyzing metabolic reactions, and providing structural support to cells. A protein can be identified based on each level of its structure. Every protein at least contains a primary, secondary, and tertiary structure. Only some proteins have a quaternary structure as well. The primary structure is comprised of a linear chain of amino acids. The secondary structure contains regions of amino acid chains that are stabilized by hydrogen bonds from the polypeptide backbone. These hydrogen bonds create alpha-helix and beta-pleated sheets of the secondary structure. The three-dimensional shape of a protein, its tertiary structure, is determined by the interactions of side chains from the polypeptide backbone. The quaternary structure also influences the three-dimensional shape of the protein and is formed through the side-chain interactions between two or more polypeptides. Each protein at least contains a primary, secondary, and tertiary structure. Only some proteins have a quaternary structure as well.
Accurate protein quantitation is essential to protein studies in a multitude of research topics. A wide array of different methods have been developed to quantitate both complex mixtures of proteins as well as a single type of protein.
Total protein quantitation methods comprise traditional methods such as the measurement of UV absorbance at 280 nm, Bicinchoninic acid (BCA) and Bradford assays, as well as alternative methods like Lowry or novel assays developed by commercial suppliers, which often provide a well-designed, convenient kit for each type of the assay. Individual protein quantitation methods include enzyme-linked immunosorbent assay (ELISA), western blot analysis, and more recently, mass spectrometry, among others. Accurate protein quantitation is essential to all experiments related to proteins studies in a multitude of research topics. Different wide array of different methods have been developed to quantitate both complex mixtures of proteins in a given assay for total protein content and as well as for a single type of protein.
Lung Cancer: Artificial Intelligence, Synergetics, Complex System Analysis, S...Oleg Kshivets
RESULTS: Overall life span (LS) was 2252.1±1742.5 days and cumulative 5-year survival (5YS) reached 73.2%, 10 years – 64.8%, 20 years – 42.5%. 513 LCP lived more than 5 years (LS=3124.6±1525.6 days), 148 LCP – more than 10 years (LS=5054.4±1504.1 days).199 LCP died because of LC (LS=562.7±374.5 days). 5YS of LCP after bi/lobectomies was significantly superior in comparison with LCP after pneumonectomies (78.1% vs.63.7%, P=0.00001 by log-rank test). AT significantly improved 5YS (66.3% vs. 34.8%) (P=0.00000 by log-rank test) only for LCP with N1-2. Cox modeling displayed that 5YS of LCP significantly depended on: phase transition (PT) early-invasive LC in terms of synergetics, PT N0—N12, cell ratio factors (ratio between cancer cells- CC and blood cells subpopulations), G1-3, histology, glucose, AT, blood cell circuit, prothrombin index, heparin tolerance, recalcification time (P=0.000-0.038). Neural networks, genetic algorithm selection and bootstrap simulation revealed relationships between 5YS and PT early-invasive LC (rank=1), PT N0—N12 (rank=2), thrombocytes/CC (3), erythrocytes/CC (4), eosinophils/CC (5), healthy cells/CC (6), lymphocytes/CC (7), segmented neutrophils/CC (8), stick neutrophils/CC (9), monocytes/CC (10); leucocytes/CC (11). Correct prediction of 5YS was 100% by neural networks computing (area under ROC curve=1.0; error=0.0).
CONCLUSIONS: 5YS of LCP after radical procedures significantly depended on: 1) PT early-invasive cancer; 2) PT N0--N12; 3) cell ratio factors; 4) blood cell circuit; 5) biochemical factors; 6) hemostasis system; 7) AT; 8) LC characteristics; 9) LC cell dynamics; 10) surgery type: lobectomy/pneumonectomy; 11) anthropometric data. Optimal diagnosis and treatment strategies for LC are: 1) screening and early detection of LC; 2) availability of experienced thoracic surgeons because of complexity of radical procedures; 3) aggressive en block surgery and adequate lymph node dissection for completeness; 4) precise prediction; 5) adjuvant chemoimmunoradiotherapy for LCP with unfavorable prognosis.
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Ethanol (CH3CH2OH), or beverage alcohol, is a two-carbon alcohol
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comorbidities, fetal alcohol spectrum disorders, genetic risk factors, and
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Title: Sense of Smell
Presenter: Dr. Faiza, Assistant Professor of Physiology
Qualifications:
MBBS (Best Graduate, AIMC Lahore)
FCPS Physiology
ICMT, CHPE, DHPE (STMU)
MPH (GC University, Faisalabad)
MBA (Virtual University of Pakistan)
Learning Objectives:
Describe the primary categories of smells and the concept of odor blindness.
Explain the structure and location of the olfactory membrane and mucosa, including the types and roles of cells involved in olfaction.
Describe the pathway and mechanisms of olfactory signal transmission from the olfactory receptors to the brain.
Illustrate the biochemical cascade triggered by odorant binding to olfactory receptors, including the role of G-proteins and second messengers in generating an action potential.
Identify different types of olfactory disorders such as anosmia, hyposmia, hyperosmia, and dysosmia, including their potential causes.
Key Topics:
Olfactory Genes:
3% of the human genome accounts for olfactory genes.
400 genes for odorant receptors.
Olfactory Membrane:
Located in the superior part of the nasal cavity.
Medially: Folds downward along the superior septum.
Laterally: Folds over the superior turbinate and upper surface of the middle turbinate.
Total surface area: 5-10 square centimeters.
Olfactory Mucosa:
Olfactory Cells: Bipolar nerve cells derived from the CNS (100 million), with 4-25 olfactory cilia per cell.
Sustentacular Cells: Produce mucus and maintain ionic and molecular environment.
Basal Cells: Replace worn-out olfactory cells with an average lifespan of 1-2 months.
Bowman’s Gland: Secretes mucus.
Stimulation of Olfactory Cells:
Odorant dissolves in mucus and attaches to receptors on olfactory cilia.
Involves a cascade effect through G-proteins and second messengers, leading to depolarization and action potential generation in the olfactory nerve.
Quality of a Good Odorant:
Small (3-20 Carbon atoms), volatile, water-soluble, and lipid-soluble.
Facilitated by odorant-binding proteins in mucus.
Membrane Potential and Action Potential:
Resting membrane potential: -55mV.
Action potential frequency in the olfactory nerve increases with odorant strength.
Adaptation Towards the Sense of Smell:
Rapid adaptation within the first second, with further slow adaptation.
Psychological adaptation greater than receptor adaptation, involving feedback inhibition from the central nervous system.
Primary Sensations of Smell:
Camphoraceous, Musky, Floral, Pepperminty, Ethereal, Pungent, Putrid.
Odor Detection Threshold:
Examples: Hydrogen sulfide (0.0005 ppm), Methyl-mercaptan (0.002 ppm).
Some toxic substances are odorless at lethal concentrations.
Characteristics of Smell:
Odor blindness for single substances due to lack of appropriate receptor protein.
Behavioral and emotional influences of smell.
Transmission of Olfactory Signals:
From olfactory cells to glomeruli in the olfactory bulb, involving lateral inhibition.
Primitive, less old, and new olfactory systems with different path
4. Definition of Protein.
General Chemistry of Amino acid.
Composition.
Amphoteric Nature.
Structure of Protein.
Classification of Protein.
Properties of Proteins.
Denaturation of Protein.
Function of Protein.
Biological Importance of Protein.
Objectives:
5. Any of a group of complex organic macromolecules
that contain Carbon, Hydrogen, Oxygen, Nitrogen
and usually sulphur and are composed of amino
acids is called Protein.
Protein include many substances such as enzymes,
hormones, antibodies etc. that are necessary for the
proper functioning of an organism.
They are essential for growth and repair of tissues in
an organism.
Protein:
6. Amino Acids are the building units of proteins.
Proteins are polymers of amino acids linked
together by what is called “ Peptide bond”.
There are about 300 amino acids occur in nature.
Only 20 of them occur in proteins.
7. Each amino acid has 4 different groups attached
to α- carbon ( which is C-atom next to COOH).
These 4 groups are :
amino group,
COOH group,
hydrogen atom.
side chain (R).
10. Essential Amino Acid:
Those amino acid which are not synthesized
in living organism and they have to ingest
them.
e.g.
Isoleucine, Leucine, Methionine, Lysine.
Non-essential Amino Acid:
The amino acid which are continuously
synthesized in our body are called non-
essential amino acid.
e.g.
Alanine, Asparagines, Aspartic Acid, Cysteine.
11. Semi-essential amino acid:
Amino acid which are present in our body
but not in adequate amount are called semi-
essential amino acid.
Acidic Amino Acid:
They have more carboxyl group rather than
amino group i.e. 2 carboxyl group and 1
amino group.
e.g.
Aspartic acid, Asparagine, Glutamic acid,
Glutamine.
12. Basic amino acid:
They have more amino group rather than
carboxyl group i.e. 2 amine group and 1
carboxyl group.
e.g.
Arginine, Lysine, Hydroxylysine, Histidine.
Aromatic Amino acid:
They contain aromatic (benzene) ring in their
molecules.
e.g.
Phenylalanine, Tyrosine, Tryptophan
13. Sulphur Amino acid:
Contain sulphur in their structure.
E.g. Cystine, Cysteine, Metheone.
Side Chain-OH Amino acid:
They contain OH in their group.
14. An α-amino acid in which the functional
group attached to the α-carbon (R in
RCH(NH3+)COO−) has hydrophilic
properties, serine, cysteine,
homocysteine.
15. Non Polar Amino Acids have equal number
of amino and carboxyl groups and are
neutral. These amino acids are hydrophobic
and have no charge on the 'R' group. The
amino acids in this group are alanine,
valine, leucine, isoleucine, phenyl
alanine, glycine, tryptophan, methionine
and proline.
16. Zwitter Ion:
Neutral amino acids (monobasic,
monocarboxylic) exist in aqueous solution
as “ Zwitter ion” i.e. contain both positive
and negative charge. Zwitter ion is
electrically neutral and can’t migrate into
electric field.
17. Amino acids are Amphoteric organic
acids that contain the amine group, -NH2
and the carboxylic acid group -COOH.
Amine groups are basic ( you could say
they are a modified form of the ammonia
molecule) and carboxylic are acidic.
As an example of the Amphoteric nature
of an amino acid, we can look at Glycine,
which is chemically, the simplest of the
amino acids.
18. Two amino acids joined by one
peptide bond.
Example: Aspartame which acts as
sweetening agent being used in
replacement of cane sugar. It is
composed of aspartic acid and phenyl
alkaline.
19.
20. There are four levels of protein structure:
Primary.
Secondary.
Tertiary.
Quaternary.
21. The primary structure of a protein refers
to the linear sequence of amino acids in the
polypeptide chain. The primary
structure is held together by covalent
bonds such as peptide bonds, which are
made during the process of
protein biosynthesis.
22.
23. The folding of the polypeptides chains into
a specific coiled structure held together by
disulfide and hydrogen bonds is called
secondary structure of protein.
It consist of:
a- helix
b- pleated sheet
b- bends
Non repetitive structure.
Super secondary structure.
24.
25. The 3D (Three-dimensional) structure of
an entire amino acid chain is called
tertiary structure. Is determined by a
variety of interactions (bond formation)
among R groups and between R groups
and the polypeptide backbone.
26.
27. Arrangement of two or more polypeptide
chains into multi subunit molecule.
Results from the aggregation
(combination) of two or more polypeptide
subunits held together by non-covalent
interaction like H-bonds, ionic or
hydrophobic interactions.
28.
29.
30.
31. Protein can be classified into three
groups.
1. Simple proteins.
2. Conjugated proteins.
3. Derived proteins.
32. Simple proteins are proteins which on
hydrolysis yields only amino acids and
possess no non-protein part in molecules.
Major subclasses of simple proteins are as
follows:
Protamines
Histones
Albumin
Globulin
33. Glutelins
Prolamines
Sceloproteins (albuminoids).
Keratins
Collagens
Elastins.
Conjugated Proteins:
Conjugated proteins are complexes of
simple protein and with non-proteins; the
protein part is called apoprotein and the
non-protein part is called prostheticc group
and the entire molecules is known as
holoprotein.
34. Conjugated proteins are classified on the
basis of prosthetic group.
Subclasses of conjugated proteins are:
I. Nucleoproteins.
II. Mucoproteins.
III. Glycoprotein.
IV. Chromoproteins.
V. Phosphoproteins.
VI. Lipoprotiens.
VII. Metalloproteins.
35. Derived proteins are produced from
natural proteins by various physical and
chemical factors and divided into two
major groups:
a) Primary protein
b) Secondary protein
36. They are coagulated and denatured
proteins.
Proteans Heat, water, X-Rays, UV Rays,
agitation, or alcohol change soluble
globular proteins like ovalbumin to fibrous
insoluble, coagulated and denatured
proteins.
Metaprotein and coagulated protein are
the subclasses of primary protein
37. Progressive hydrolysis of peptide bonds
breaks the protein into progressively smaller
molecules called proteases, peptones and
peptides. They are generally soluble in
water and not coagulated by heat.
38. Collagen:
Holds the tissues together.
Keratin:
Toughens and waterproofs the skin.
Hormone:
Regulate body function.
Actin and Myosin:
Relaxation and contraction.
39. Hemoglobin:
Transfer Oxygen.
Antibody:
Fights infection.
Enzymes:
Assist other chemical to react with each
other.
Defense protein:
Immunoglobulin are involved in defense
mechanisms.
40. Contractile protein:
Protein of skeletal muscle are involved in
muscle contraction and relaxation.
Respiratory protein:
These involved in the respiration. E.g.
Hemoglobin.
Structure protein:
These are the protein of skin, cartilage
and nail.
41. There are two types of properties
1. Physical Properties.
2. Chemical Properties.
42. 1-Proteins are mainly water soluble which
is explained by its polarity and the
presence of charged groups. They are
soluble thus in polar solvents and not
soluble in non-polar solvents.
2-They have a high melting point reflecting
the high energy needed to break the ionic
forces.
43. 3. Colorless
4. Crystalline
5. May be sweet (glycine, alanine)
6. Tasteless (leucine)
7. Bitter (Arginine)
8. Colloidal Nature: Hydration shell and
electric repulsion make proteins stable
in solution.
45. Denaturation of protein:
Denaturation is a process in which protein
or nucleic acid loose the Quaternary
structure, tertiary and secondary structure
which is present in their native state by
application of some external stress or
compound such as strong acid or base a
concentrated inorganic salt, an organic
solvent e.g. alcohol, radiation of heat.
46.
47. Physical agent:
Heat, UV Lights, Ultrasound, High
Pressure etc.
Chemical agent:
Organic solvent, acid and alkalis, urea
and various detergent.
Denaturation destroys enzyme and
hormonal activity but increase digestibility
of protein.
48. Membrane Formation:
Protein and lipid form the major structural
component of cell membrane.
Enzymes:
Enzyme are Protein in nature and are
biocatalyst which influence the rate of
chemical reaction usually without
undergoing any change in themselves.
49. Homeostasis:
Several hormones are peptides and
proteins. They play an important role in
the regulation of homeostasis.
Blood proteins:
The blood proteins include plasma
proteins and hemoglobin.
a. Plasma proteins:
Albumin
Globulin
Fibrinogen
50. Albumin:
Maintain the colloid osmotic pressure of
plasma and transport material.
Globulin:
Inhibit proteolytic enzymes and promote
immune system of the body..
Fibrinogen:
Help in blood clotting.
b. Hemoglobin:
Carry oxygen in the form of oxyhemoglobin
in blood.
51. Antibodies:
Resist against viable pathogen.
Nucleoproteins:
These are conjugated protein of cell nuclei.
Collagen:
Found in connective tissue.
Contractile Protein:
Actin and myosin help in contraction and
relaxation of muscle.