This document discusses the structure of proteins at four levels: primary, secondary, tertiary, and quaternary. The primary structure refers to the amino acid sequence in the polypeptide chain. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding between amino acids. Tertiary structure describes the overall 3D shape of the protein formed by interactions between amino acid side chains. Quaternary structure applies to proteins composed of multiple polypeptide subunits that combine through non-covalent bonds. The structures are determined through techniques like X-ray crystallography and NMR spectroscopy.
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
starch is an branched homo polysaccharide.
(contains same type of monomers)
It is the most common carbohydrate in human diet.
Starch is the storage form of glucose in plants. the plants utilize the glucose by using enzymes like amylase.
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
starch is an branched homo polysaccharide.
(contains same type of monomers)
It is the most common carbohydrate in human diet.
Starch is the storage form of glucose in plants. the plants utilize the glucose by using enzymes like amylase.
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.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
WHAT IS CARBOHYDRATE? CLASSIFICATION OF CARBOHYDRATE? WHAT IS MONOSACCHARIDE? CLASSIFICATION OF MONOSACCHARIDE. PHYSICAL PROPERTY. CHEMICAL PROPERTY. ATRUCTURAL FORMULA. METABOLISM . IMPORTANCE OF MONOSACCHARIDE. IMPORTANT FACT RELATED TO MONOSACCHARIDE. DISORDER OF MONOSACCHARIDE CONCLUSION. REFRANCES
Biochemistry, Biomolecules and Cell: An IntroductionPrincy Agarwal
This presentation will help you to understand the introduction of Biochemistry, Biomolecules and Cell along with transport mechanisms across cell membrane in an easy and friendly manner along with summarised notes.
Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation.
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.
Gives in detail primary, secondary, tertiary and Quaternary structure of proteins. Gives classification of secondary structure: alpha helix, beta pleated sheet and different types of tight turns and explains most commonly found tight turn in proteins i.e. beta turn. Briefs about the Ramachandran plot of proteins, dihedral or torsion angles and explains why glycine and proline act as alpha helix breakers. Explains tertiary structure of proteins and different covalent and non covalent bonds in the tertiary structure and relative importance of these bonding interactions. Details about the quaternary structure of proteins and explains why hemoglobin is a quaternary protein and insulin is not.
WHAT IS CARBOHYDRATE? CLASSIFICATION OF CARBOHYDRATE? WHAT IS MONOSACCHARIDE? CLASSIFICATION OF MONOSACCHARIDE. PHYSICAL PROPERTY. CHEMICAL PROPERTY. ATRUCTURAL FORMULA. METABOLISM . IMPORTANCE OF MONOSACCHARIDE. IMPORTANT FACT RELATED TO MONOSACCHARIDE. DISORDER OF MONOSACCHARIDE CONCLUSION. REFRANCES
Biochemistry, Biomolecules and Cell: An IntroductionPrincy Agarwal
This presentation will help you to understand the introduction of Biochemistry, Biomolecules and Cell along with transport mechanisms across cell membrane in an easy and friendly manner along with summarised notes.
Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation.
I shikha popali and my colleague harshpal singh wahi presents a presentation "RECENT DEVELOPMENT IN DRUG DESIGN AND DISCOVERY " A detail account on protein structure is given
Amino acisd structure
Peptide bond formation
Analysis of protein Structure- X-ray Crystallography
Different structural levels of proteins with examples.
Importance of protein structure
Creutzfeldt-Jacob-Disease due to changes in normal protein conformation.
Anti ulcer drugs and their Advance pharmacology ||
Anti-ulcer drugs are medications used to prevent and treat ulcers in the stomach and upper part of the small intestine (duodenal ulcers). These ulcers are often caused by an imbalance between stomach acid and the mucosal lining, which protects the stomach lining.
||Scope: Overview of various classes of anti-ulcer drugs, their mechanisms of action, indications, side effects, and clinical considerations.
micro teaching on communication m.sc nursing.pdfAnurag Sharma
Microteaching is a unique model of practice teaching. It is a viable instrument for the. desired change in the teaching behavior or the behavior potential which, in specified types of real. classroom situations, tends to facilitate the achievement of specified types of objectives.
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Hot Selling Organic intermediates
- Video recording of this lecture in English language: https://youtu.be/lK81BzxMqdo
- Video recording of this lecture in Arabic language: https://youtu.be/Ve4P0COk9OI
- Link to download the book free: https://nephrotube.blogspot.com/p/nephrotube-nephrology-books.html
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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.
Prix Galien International 2024 Forum ProgramLevi Shapiro
June 20, 2024, Prix Galien International and Jerusalem Ethics Forum in ROME. Detailed agenda including panels:
- ADVANCES IN CARDIOLOGY: A NEW PARADIGM IS COMING
- WOMEN’S HEALTH: FERTILITY PRESERVATION
- WHAT’S NEW IN THE TREATMENT OF INFECTIOUS,
ONCOLOGICAL AND INFLAMMATORY SKIN DISEASES?
- ARTIFICIAL INTELLIGENCE AND ETHICS
- GENE THERAPY
- BEYOND BORDERS: GLOBAL INITIATIVES FOR DEMOCRATIZING LIFE SCIENCE TECHNOLOGIES AND PROMOTING ACCESS TO HEALTHCARE
- ETHICAL CHALLENGES IN LIFE SCIENCES
- Prix Galien International Awards Ceremony
Ethanol (CH3CH2OH), or beverage alcohol, is a two-carbon alcohol
that is rapidly distributed in the body and brain. Ethanol alters many
neurochemical systems and has rewarding and addictive properties. It
is the oldest recreational drug and likely contributes to more morbidity,
mortality, and public health costs than all illicit drugs combined. The
5th edition of the Diagnostic and Statistical Manual of Mental Disorders
(DSM-5) integrates alcohol abuse and alcohol dependence into a single
disorder called alcohol use disorder (AUD), with mild, moderate,
and severe subclassifications (American Psychiatric Association, 2013).
In the DSM-5, all types of substance abuse and dependence have been
combined into a single substance use disorder (SUD) on a continuum
from mild to severe. A diagnosis of AUD requires that at least two of
the 11 DSM-5 behaviors be present within a 12-month period (mild
AUD: 2–3 criteria; moderate AUD: 4–5 criteria; severe AUD: 6–11 criteria).
The four main behavioral effects of AUD are impaired control over
drinking, negative social consequences, risky use, and altered physiological
effects (tolerance, withdrawal). This chapter presents an overview
of the prevalence and harmful consequences of AUD in the U.S.,
the systemic nature of the disease, neurocircuitry and stages of AUD,
comorbidities, fetal alcohol spectrum disorders, genetic risk factors, and
pharmacotherapies for AUD.
Tom Selleck Health: A Comprehensive Look at the Iconic Actor’s Wellness Journeygreendigital
Tom Selleck, an enduring figure in Hollywood. has captivated audiences for decades with his rugged charm, iconic moustache. and memorable roles in television and film. From his breakout role as Thomas Magnum in Magnum P.I. to his current portrayal of Frank Reagan in Blue Bloods. Selleck's career has spanned over 50 years. But beyond his professional achievements. fans have often been curious about Tom Selleck Health. especially as he has aged in the public eye.
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Introduction
Many have been interested in Tom Selleck health. not only because of his enduring presence on screen but also because of the challenges. and lifestyle choices he has faced and made over the years. This article delves into the various aspects of Tom Selleck health. exploring his fitness regimen, diet, mental health. and the challenges he has encountered as he ages. We'll look at how he maintains his well-being. the health issues he has faced, and his approach to ageing .
Early Life and Career
Childhood and Athletic Beginnings
Tom Selleck was born on January 29, 1945, in Detroit, Michigan, and grew up in Sherman Oaks, California. From an early age, he was involved in sports, particularly basketball. which played a significant role in his physical development. His athletic pursuits continued into college. where he attended the University of Southern California (USC) on a basketball scholarship. This early involvement in sports laid a strong foundation for his physical health and disciplined lifestyle.
Transition to Acting
Selleck's transition from an athlete to an actor came with its physical demands. His first significant role in "Magnum P.I." required him to perform various stunts and maintain a fit appearance. This role, which he played from 1980 to 1988. necessitated a rigorous fitness routine to meet the show's demands. setting the stage for his long-term commitment to health and wellness.
Fitness Regimen
Workout Routine
Tom Selleck health and fitness regimen has evolved. adapting to his changing roles and age. During his "Magnum, P.I." days. Selleck's workouts were intense and focused on building and maintaining muscle mass. His routine included weightlifting, cardiovascular exercises. and specific training for the stunts he performed on the show.
Selleck adjusted his fitness routine as he aged to suit his body's needs. Today, his workouts focus on maintaining flexibility, strength, and cardiovascular health. He incorporates low-impact exercises such as swimming, walking, and light weightlifting. This balanced approach helps him stay fit without putting undue strain on his joints and muscles.
Importance of Flexibility and Mobility
In recent years, Selleck has emphasized the importance of flexibility and mobility in his fitness regimen. Understanding the natural decline in muscle mass and joint flexibility with age. he includes stretching and yoga in his routine. These practices help prevent injuries, improve posture, and maintain mobilit
These lecture slides, by Dr Sidra Arshad, offer a quick overview of physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar leads (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
3. • Proteins are an important class of
biological macromolecules
which are the polymers of amino
acids.
• Biochemists have distinguished
several levels of structural
organization of proteins. They
are:
– Primary structure
– Secondary structure
– Tertiary structure
– Quaternary structure
INTRODUCTION
4. PRIMARY STRUCTURE
• The primary structure of protein refers to the sequence of amino
acids present in the polypeptide chain.
• Amino acids are covalently linked by peptide bonds.
• Each component amino acid in a polypeptide is called a “residue” or
“moiety”
• By convention, the 10 structure of a protein starts from the amino-
terminal (N) end and ends in the carboxyl-terminal (C) end.
5. IMPORTANCE OF PRIMARY STRUCTURE
• To predict 20 and 30 structures from sequence homologies with
related proteins. (Structure prediction)
• Many genetic diseases result from abnormal amino acid sequences.
• To understand the molecular mechanism of action of proteins.
• To trace evolutionary paths.
• End group analysis – Edman degradation.
• Gene sequencing method.
METHODS OF AMINO ACID SEQUENCE DETERMINATION
6. SECONDARY STRUCTURE
• Localized arrangement of adjacent amino acids formed as the polypeptide
chain folds.
• It consists of
• Linus Pauling proposed some essential features of peptide units and
polypeptide backbone. They are:
– The amide group is rigid and planar as a result of resonance. So rotation
about C-N bond is not feasible.
– Rotation can take place only about N- Cα and Cα – C bonds.
– Trans configuration is more stable than cis for R grps at Cα
• From these conclusions Pauling postulated 2 ordered structures α helix and
β sheet
α-helix
β-pleated sheet
β-bends
Non repetitive structures
Super secondary structures
7. POLYPEPTIDE
CHAIN CONFORMATIONS
• The only reasonably free movements
are rotations around the C α-N bond
(measured as ϕ ) and the C α-C bond
(measured as Ѱ).
• The conformation of the backbone
can therefore be described by the
torsion angles (also called dihedral
angles or rotation angles)
8. • Spiral structure
• Tightly packed, coiled polypeptide
backbone core.
• Side chain extend outwards
• Stabilized by H bonding b/w
carbonyl oxygen and amide
hydrogen.
• Amino acids per turn – 3.6
• Pitch is 5.4 A
• Alpha helical segments are found in
many globular proteins like
myoglobins, troponin- C etc.
ALPHA HELIX
H bonding
9. • Formed when 2 or more polypeptides
line up side by side.
• Individual polypeptide - β strand
• Each β strand is fully extended.
• They are stabilized by H bond b/w N-H
and carbonyl grps of adjacent chains.
BETA PLEATED SHEET
2 types
Parallel Anti -Parallel
N C N
N NC
C
C
12. BETA BENDS
• Permits the change of direction of the
peptide chain to get a folded structure.
• It gives a protein globularity rather than
linearity.
• H bond stabilizes the beta bend
structure.
• Proline and Glycine are frequently
found in beta turns.
• Beta turns often promote the formation
of antiparallel beta sheets.
• Occur at protein surfaces.
• Involve four successive aminoacid
residues
13. NON REPETITIVE STRUCTURES
• A significant portion of globular
protein’s structure may be irregular
or unique.
• They include coils and loops.
• Segments of polypeptide chains
whose successive residues do not
have similar ϕ and Ѱ values are
called coils.
• Almost all proteins with more than
60 residues contain one or more
loops of 6 to 16 residues, called Ω
loops.
Space-filling model of an Ω loop
14. TERTIARY STRUCTURE
• Tertiary structure is the three-
dimensional conformation of a
polypeptide.
• The common features of protein
tertiary structure reveal much about
the biological functions of the proteins
and their evolutionary origins.
• The function of a protein depends on
its tertiary structure. If this is disrupted,
it loses its activity.
15. DOMAINS
• Polypeptide chains containing more than ,200 residues usually
fold into two or more globular clusters known as domains.
• Fundamental functional and 3 dimensional structure of
proteins.
• Domains often have a specific function such as the binding of
a small molecule.
• Many domains are structurally independent units that have the
characteristics of small globular proteins.
The two-domain protein glyceraldehyde-
3-phosphate dehydrogenase.
NAD+
16. INTERACTIONS STABILIZING 30
STRUCTURE
• This final shape is
determined by a variety of
bonding interactions
between the "side chains"
on the amino acids.
• Hydrogen bonds
• Ionic Bonds
• Disulphide Bridges
• Hydrophobic Interactions:
18. DETERMINATION OF TERTIARY
STRUCTURE
• The known protein structures have come to light through:
• X-ray crystallographic studies
• Nuclear Magnetic Resonance studies
• The atomic coordinates of most of these structures are
deposited in a database known as the Protein Data Bank
(PDB).
• It allows the tertiary structures of a variety of proteins to be
analyzed and compared.
19. • The biological function of some
molecules is determined by multiple
polypeptide chains –
multimeric proteins.
• Arrangement of polypeptide sub unit
is called quaternary structure.
• Sub units are held together by non
covalent interactions.
• Eg: Hemoglobin has the subunit
composition a2b2
QUATERNARY STRUCTURE
Quaternary structure of hemoglobin.
20. RECENT DEVELOPMENTS
• A team of scientists at The Scripps Research Institute and the
National Institutes of Health (NIH) has discovered the
structure of a protein – dynamin, that pinches off tiny pouches
from cell’s outer membranes.
• Scientists at the Institute of Structural and Molecular Biology
have revealed the structure of a complex protein called FimD
that acts as an assembly platform for the pili of cystitis
bacteria.
• Researchers from the Walter and Eliza Hall Institute have
found a structural surprise in a type of protein, Bcl-w ,that
encourages cell survival, raising interesting questions about
how the proteins function to influence programmed cell death.
21. CONCLUSION
• Proteins are extraordinarily complex molecules. Of all the
molecules encountered in living organisms, proteins have the
most diverse functions.
• So a basic understanding of the structure of proteins is
necessary to comprehend its role in organisms.
• Further researches will provide more insight into the structure
of several other proteins in the coming year.
22. REFERENCE
• Voet, Donald; Voet Judith. Biochemistry, 3rd edition, John
Wiley and sons.
• Champe, Pamela.C, Harvey, Richard A, Ferrier Denise R
(2005). Lippincott’s Illustrated Reviews: Biochemistry, 3rd
edition. Lippincott William and Wilkins.
• McKee Trudy, McKee James R (2003), Biochemistry: The
molecular basis of life, 3rd edition, McGraw Hill.
• http://esciencenews.com/articles/2011/06/01/new.antibiotics.a.
step.closer.with.discovery.bacterial.protein.structure
• http://www.eurekalert.org/pub_releases/2010-04/sri-
srs042610.php
• http://www.physorg.com/news/2011-10-cell-survival-protein-
reveals.html