1) Proteins exhibit four levels of structural organization: primary, secondary, tertiary, and quaternary.
2) The primary structure is the linear sequence of amino acids in the polypeptide chain. Secondary structure involves folding of the chain into structures like alpha helices and beta sheets.
3) Tertiary structure involves further folding that determines the final three-dimensional shape of the protein. For oligomeric proteins, quaternary structure describes the arrangement of multiple polypeptide subunits.
A simplified presentation of the complex and crucial process of protein folding which takes place after an amino acid chain is translated by ribosomes from mRNA.
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.
A simplified presentation of the complex and crucial process of protein folding which takes place after an amino acid chain is translated by ribosomes from mRNA.
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.
the topic introduction of protein cover their target their primary structure , secondary structure and tertiary structure and their bonding interaction
the topic introduction of protein cover their target their primary structure , secondary structure and tertiary structure and their bonding interaction
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.
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.
New Directions in Targeted Therapeutic Approaches for Older Adults With Mantl...i3 Health
i3 Health is pleased to make the speaker slides from this activity available for use as a non-accredited self-study or teaching resource.
This slide deck presented by Dr. Kami Maddocks, Professor-Clinical in the Division of Hematology and
Associate Division Director for Ambulatory Operations
The Ohio State University Comprehensive Cancer Center, will provide insight into new directions in targeted therapeutic approaches for older adults with mantle cell lymphoma.
STATEMENT OF NEED
Mantle cell lymphoma (MCL) is a rare, aggressive B-cell non-Hodgkin lymphoma (NHL) accounting for 5% to 7% of all lymphomas. Its prognosis ranges from indolent disease that does not require treatment for years to very aggressive disease, which is associated with poor survival (Silkenstedt et al, 2021). Typically, MCL is diagnosed at advanced stage and in older patients who cannot tolerate intensive therapy (NCCN, 2022). Although recent advances have slightly increased remission rates, recurrence and relapse remain very common, leading to a median overall survival between 3 and 6 years (LLS, 2021). Though there are several effective options, progress is still needed towards establishing an accepted frontline approach for MCL (Castellino et al, 2022). Treatment selection and management of MCL are complicated by the heterogeneity of prognosis, advanced age and comorbidities of patients, and lack of an established standard approach for treatment, making it vital that clinicians be familiar with the latest research and advances in this area. In this activity chaired by Michael Wang, MD, Professor in the Department of Lymphoma & Myeloma at MD Anderson Cancer Center, expert faculty will discuss prognostic factors informing treatment, the promising results of recent trials in new therapeutic approaches, and the implications of treatment resistance in therapeutic selection for MCL.
Target Audience
Hematology/oncology fellows, attending faculty, and other health care professionals involved in the treatment of patients with mantle cell lymphoma (MCL).
Learning Objectives
1.) Identify clinical and biological prognostic factors that can guide treatment decision making for older adults with MCL
2.) Evaluate emerging data on targeted therapeutic approaches for treatment-naive and relapsed/refractory MCL and their applicability to older adults
3.) Assess mechanisms of resistance to targeted therapies for MCL and their implications for treatment selection
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.
Flu Vaccine Alert in Bangalore Karnatakaaddon Scans
As flu season approaches, health officials in Bangalore, Karnataka, are urging residents to get their flu vaccinations. The seasonal flu, while common, can lead to severe health complications, particularly for vulnerable populations such as young children, the elderly, and those with underlying health conditions.
Dr. Vidisha Kumari, a leading epidemiologist in Bangalore, emphasizes the importance of getting vaccinated. "The flu vaccine is our best defense against the influenza virus. It not only protects individuals but also helps prevent the spread of the virus in our communities," he says.
This year, the flu season is expected to coincide with a potential increase in other respiratory illnesses. The Karnataka Health Department has launched an awareness campaign highlighting the significance of flu vaccinations. They have set up multiple vaccination centers across Bangalore, making it convenient for residents to receive their shots.
To encourage widespread vaccination, the government is also collaborating with local schools, workplaces, and community centers to facilitate vaccination drives. Special attention is being given to ensuring that the vaccine is accessible to all, including marginalized communities who may have limited access to healthcare.
Residents are reminded that the flu vaccine is safe and effective. Common side effects are mild and may include soreness at the injection site, mild fever, or muscle aches. These side effects are generally short-lived and far less severe than the flu itself.
Healthcare providers are also stressing the importance of continuing COVID-19 precautions. Wearing masks, practicing good hand hygiene, and maintaining social distancing are still crucial, especially in crowded places.
Protect yourself and your loved ones by getting vaccinated. Together, we can help keep Bangalore healthy and safe this flu season. For more information on vaccination centers and schedules, residents can visit the Karnataka Health Department’s official website or follow their social media pages.
Stay informed, stay safe, and get your flu shot today!
Recomendações da OMS sobre cuidados maternos e neonatais para uma experiência pós-natal positiva.
Em consonância com os ODS – Objetivos do Desenvolvimento Sustentável e a Estratégia Global para a Saúde das Mulheres, Crianças e Adolescentes, e aplicando uma abordagem baseada nos direitos humanos, os esforços de cuidados pós-natais devem expandir-se para além da cobertura e da simples sobrevivência, de modo a incluir cuidados de qualidade.
Estas diretrizes visam melhorar a qualidade dos cuidados pós-natais essenciais e de rotina prestados às mulheres e aos recém-nascidos, com o objetivo final de melhorar a saúde e o bem-estar materno e neonatal.
Uma “experiência pós-natal positiva” é um resultado importante para todas as mulheres que dão à luz e para os seus recém-nascidos, estabelecendo as bases para a melhoria da saúde e do bem-estar a curto e longo prazo. Uma experiência pós-natal positiva é definida como aquela em que as mulheres, pessoas que gestam, os recém-nascidos, os casais, os pais, os cuidadores e as famílias recebem informação consistente, garantia e apoio de profissionais de saúde motivados; e onde um sistema de saúde flexível e com recursos reconheça as necessidades das mulheres e dos bebês e respeite o seu contexto cultural.
Estas diretrizes consolidadas apresentam algumas recomendações novas e já bem fundamentadas sobre cuidados pós-natais de rotina para mulheres e neonatos que recebem cuidados no pós-parto em unidades de saúde ou na comunidade, independentemente dos recursos disponíveis.
É fornecido um conjunto abrangente de recomendações para cuidados durante o período puerperal, com ênfase nos cuidados essenciais que todas as mulheres e recém-nascidos devem receber, e com a devida atenção à qualidade dos cuidados; isto é, a entrega e a experiência do cuidado recebido. Estas diretrizes atualizam e ampliam as recomendações da OMS de 2014 sobre cuidados pós-natais da mãe e do recém-nascido e complementam as atuais diretrizes da OMS sobre a gestão de complicações pós-natais.
O estabelecimento da amamentação e o manejo das principais intercorrências é contemplada.
Recomendamos muito.
Vamos discutir essas recomendações no nosso curso de pós-graduação em Aleitamento no Instituto Ciclos.
Esta publicação só está disponível em inglês até o momento.
Prof. Marcus Renato de Carvalho
www.agostodourado.com
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
Explore natural remedies for syphilis treatment in Singapore. Discover alternative therapies, herbal remedies, and lifestyle changes that may complement conventional treatments. Learn about holistic approaches to managing syphilis symptoms and supporting overall health.
Knee anatomy and clinical tests 2024.pdfvimalpl1234
This includes all relevant anatomy and clinical tests compiled from standard textbooks, Campbell,netter etc..It is comprehensive and best suited for orthopaedicians and orthopaedic residents.
Report Back from SGO 2024: What’s the Latest in Cervical Cancer?bkling
Are you curious about what’s new in cervical cancer research or unsure what the findings mean? Join Dr. Emily Ko, a gynecologic oncologist at Penn Medicine, to learn about the latest updates from the Society of Gynecologic Oncology (SGO) 2024 Annual Meeting on Women’s Cancer. Dr. Ko will discuss what the research presented at the conference means for you and answer your questions about the new developments.
Couples presenting to the infertility clinic- Do they really have infertility...Sujoy Dasgupta
Dr Sujoy Dasgupta presented the study on "Couples presenting to the infertility clinic- Do they really have infertility? – The unexplored stories of non-consummation" in the 13th Congress of the Asia Pacific Initiative on Reproduction (ASPIRE 2024) at Manila on 24 May, 2024.
Title: Sense of Taste
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 structure and function of taste buds.
Describe the relationship between the taste threshold and taste index of common substances.
Explain the chemical basis and signal transduction of taste perception for each type of primary taste sensation.
Recognize different abnormalities of taste perception and their causes.
Key Topics:
Significance of Taste Sensation:
Differentiation between pleasant and harmful food
Influence on behavior
Selection of food based on metabolic needs
Receptors of Taste:
Taste buds on the tongue
Influence of sense of smell, texture of food, and pain stimulation (e.g., by pepper)
Primary and Secondary Taste Sensations:
Primary taste sensations: Sweet, Sour, Salty, Bitter, Umami
Chemical basis and signal transduction mechanisms for each taste
Taste Threshold and Index:
Taste threshold values for Sweet (sucrose), Salty (NaCl), Sour (HCl), and Bitter (Quinine)
Taste index relationship: Inversely proportional to taste threshold
Taste Blindness:
Inability to taste certain substances, particularly thiourea compounds
Example: Phenylthiocarbamide
Structure and Function of Taste Buds:
Composition: Epithelial cells, Sustentacular/Supporting cells, Taste cells, Basal cells
Features: Taste pores, Taste hairs/microvilli, and Taste nerve fibers
Location of Taste Buds:
Found in papillae of the tongue (Fungiform, Circumvallate, Foliate)
Also present on the palate, tonsillar pillars, epiglottis, and proximal esophagus
Mechanism of Taste Stimulation:
Interaction of taste substances with receptors on microvilli
Signal transduction pathways for Umami, Sweet, Bitter, Sour, and Salty tastes
Taste Sensitivity and Adaptation:
Decrease in sensitivity with age
Rapid adaptation of taste sensation
Role of Saliva in Taste:
Dissolution of tastants to reach receptors
Washing away the stimulus
Taste Preferences and Aversions:
Mechanisms behind taste preference and aversion
Influence of receptors and neural pathways
Impact of Sensory Nerve Damage:
Degeneration of taste buds if the sensory nerve fiber is cut
Abnormalities of Taste Detection:
Conditions: Ageusia, Hypogeusia, Dysgeusia (parageusia)
Causes: Nerve damage, neurological disorders, infections, poor oral hygiene, adverse drug effects, deficiencies, aging, tobacco use, altered neurotransmitter levels
Neurotransmitters and Taste Threshold:
Effects of serotonin (5-HT) and norepinephrine (NE) on taste sensitivity
Supertasters:
25% of the population with heightened sensitivity to taste, especially bitterness
Increased number of fungiform papillae
5. Know the Qs
Key Points to Remember
Structure of proteins
• Proteins are made up of one or more
polypeptide / protein chains.
• Proteins with a single polypeptide chain are
called monomeric proteins, while the
proteins with more than one monomeric unit
are called oligomeric proteins. Monomeric
proteins are predominant in nature.
• Each polypeptide chain in an oligomeric
protein is called subunit or monomer.
• Examples for oligomeric proteins are
hemoglobin (which has 4 polypeptide
chains),lactate dehydrogenase (which has 4
polypeptide chains).
• Proteins with a single polypeptide
chains are called monomeric and with
multiple units are called oligomeric
proteins.
6. Know the Qs
Key Points to Remember
• Each protein has a unique 3-D
structure, which is referred to as its
native conformation.
• In native form, proteins do not exist in a
linear or single dimension form. Instead
they exist as coiled or folded structure or
three-dimensional (3-D) conformation.
Only such 3-D conformations are
biologically active.
• Formation of active 3-D conformation
from linear form of proteins is considered
under structural organization of proteins.
• Protein do not exist in a linear form.
• They exist in folded form.
• When the proteins are formed on
ribosomes, they are synthesized in
linear form. Then they fold and attain
native conformation.
7. Know the Qs
Key Points to Remember
Structural organisation of proteins:
Proteins exhibit four different levels of
structural organization.
1) Primary structure
2) Secondary structure
3) Tertiary structure
4) Quaternary structure
8. Know the Qs
Key Points to Remember
Ans1) Primary structure of protein:
Definition :
• Primary structure of proteins indicates the
number and sequence of amino acid
residues from N -terminal to the C- terminal.
Features:
1) Peptide bonds maintain the primary
structure. Peptide bonds form the
backbone of primary structures.
2) Side chains protrude from the sides and in
opposite direction. In primary structure,
amino acids are arranged in linear chain.
• Peptide bonds form the backbone of
primary structure of protein.
• Amino acids are arranged in linear
form.
Q1) Discuss the primary structure of
protein.
9. Know the Qs
Key Points to Remember
3) The primary structure of each protein
has a unique amino acid sequence and
numbers, decided by their genes
contained in DNA.
4) Primary structure is not affected during
denaturation (as they are made up of
strong covalent peptide bonds).
• Primary structure is not affected by
denaturation.
10. Know the Qs
Key Points to Remember
Ans2) Secondary structure of protein
• Twisting & folding of polypeptide chains
results in secondary structures.
• Secondary structures refer to the folding of
the polypeptide chain, formed by the
interaction between amino acids, which are
relatively close in the primary structure of
amino acids.
• Different secondary structures are, a helix,~
sheet, Bends, Loops & Disordered
regions.
• Secondary structure is formed by the
folding of polypeptide chain.
• They are formed by the interaction of
amino acids.
Q2) Give an account of secondary
structure of protein in detail.
Ans 2) alpha helix and beta plated sheets
11. Know the Qs
Key Points to Remember
Alpha Helix:
• alpha helix is the most common secondary
structure found in proteins.
Salient Features :
1) alpha helix is a right-handed coiled
structure (as proteins are made up of L-
amino acids).
2) alpha helix structure is stabilized by
extensive hydrogen bonding. Hydrogen
bonds are formed between peptide bonds
that are 3 amino acid residues down the
polypeptide chain. (i.e. Hydrogen bond is
formed between CO- & -HN of the 4th
residue down the chain).
12. Know the Qs
Key Points to Remember
3)The hydrogen bonds are parallel to the a
helix.
4) Hydrogen bonds are individually weak, but
collectively large number of hydrogen bonds
maintains the helical structure in stable
form.
5) Each turn of helix contains 3.6 amino acid
residues and each amino acid is separated
by a distance of 1.5 Aº. So the pitch of the
helix is 5.4 Aº (3.6 X 1.5 = 5.4 Aº). • Individually hydrogen bonds are weak
but collection of large number of
hydrogen bonds maintains its stability.
13. Know the Qs
Key Points to Remember
6) Proline, hydroxy proline, glycine are
considered as helix destabilizing amino
acids(Helix breakers), as they disrupts the
formation of a helix, producing a bend.
7) Amino acids alanine and cysteine promote
helix formation.
Examples:
• alpha helix is seen in proteins such as
hemoglobin, myoglobin, alpha Keratin,
Collagen etc.
• alpha Keratin has exclusive a-helix
structure.
• Alanine and cysteine promotes helix
formation.
• Proline, glycine and hydroxy proline are
the destabilizing amino acids.
• Alpha keratin, myoglobin are the
examples of alpha helix.
14. Know the Qs
Key Points to Remember
Beta-pleated sheet :
1) sheet is an extended structure, where
bonding polypeptide chains are arranged in
the form sheets (in a pleated or zigzag
pattern, unlike the compact backbone of a
helix).
2) sheet is stabilized by hydrogen bonds,
formed between the CO & NH of peptide
bonds of adjacent segment of same
polypeptide chain.
• Bonding chains lie side by side.
• The hydrogen bonds are perpendicular to
the polypeptide chains.
• Polypeptide chains are arranged in the
sheet form
• Sheet is stabilized by hydrogen bonds.
15. Know the Qs
Key Points to Remember
3) Parallel / antiparallel sheets: sheet
structures can be parallel or antiparallel,
depending on the direction of the bonding
chains.
a) Parallel: If the bonding chains run in the
same direction
b) Antiparallel: If the bonding chains run in
opposite direction
• (E.g: Fibroin of silk).
• Beta pleated sheets are present in
parallel or antiparallel form.
• Parallel – when bonding in same
direction
• Antiparallel – when bonding in different
direction.
16. Know the Qs
Key Points to Remember
Ans3) Tertiary structure:
• Tertiary structure of protein refers to the
further folding of secondary structure of
polypeptide chain giving the compact three-
dimensional conformation.
• In monomeric proteins, tertiary structure
results in the formation of final three-
dimensional conformation of the polypeptide
chain and formation of the functionally
active protein. • Further folding of secondary structure
of polypeptide chain forms the tertiary
structure of protein.
Q3) Describe the tertiary structure of
protein.
Ans 3)
17. Know the Qs
Key Points to Remember
• Tertiary structure explains the spatial
relationship of amino acids which are far
apart from each other in the linear primary
structure, but brought closer as a result of
folding.
• Tertiary structure results in the orientation of
hydrophobic side chains towards the water
free interior and the hydrophilic polar groups
towards the surface of the protein.
• In tertiary structure, the hydrophobic
side chain are present towards the
water free interior and hydrophilic
towards the surface of protein.
18. Know the Qs
Key Points to Remember
• Tertiary structure results in the formation of
domains.
• Domains are structurally connected but
functionally independent units of a protein
that perform a particular function, such as
binding with substrate (or other ligands) in
enzymes etc.
19. Know the Qs
Key Points to Remember
Ans4) Quaternary structure:
• Proteins having more than one polypeptide
chain (oligomeric proteins) show one more
level of higher structure called the
quaternary structure.
• Quaternary structure refers to the spatial
arrangement of the subunits of an
oligomeric protein.
• For instance; Hemoglobin has four globin
chains. So it shows quaternary structure.
Other examples are Immunoglobulins,
lactate dehydrogenase etc. • Spatial arrangement of subunits of
oligomeric protein.
• Oligomeric protein show one more
level of higher structure.
• E.g : hemoglobin
Q4) Write a short note on quaternary
structure of protein.
Ans 4) Main heading
20. Know the Qs
Key Points to Remember
Ans5) Bonds stabilizing tertiary
structure :
• Tertiary structure is stabilized by weak non
covalent bonds like hydrogen bond, vander
Waals forces, ionic bonds and hydrophobic
bonds. Even though these bonds are weak,
large number of these bonds gives stability
to the structure.
• Some proteins contain strong covalent
disulfide (S-S) bonds, which are formed
between two cysteine residues of the same
protein chain. Intrachain disulfide bonds
further enhance the stability of the tertiary
structure of proteins.
Tertiary structure is stabilized by :
• Vander waal forces
• Weak non covalent bonds
• Hydrophobic bonds.
Q5) Which are the different kinds of
bonds that help in stabilizing of tertiary
protein?
Ans 5) Main heading
21. Know the Qs
Key Points to Remember
Bonds stabilizing quaternary structure :
• Quaternary structure is stabilized by weak
noncovalent bonds like hydrogen bonds,van
der Waals forces, ionic bonds, hydrophobic
bonds and also few covalent disulphide
bonds.
• Quaternary structures are interchain
interaction between polypeptide chains.
(unlike secondary & tertiary structures,
which are intrachain interactions within the
same chain). Quaternary structure is stabilized by
weak noncovalent bonds like hydrogen
bonds,van der Waals forces, ionic
bonds, hydrophobic bonds and also
few covalent disulphide bonds.
22. Know the Qs
Key Points to Remember
• Monomeric proteins exhibit only 3 levels of
structures-primary, secondary and tertiary,
• whereas oligomeric proteins exhibit all 4
levels of protein structures including
quaternary structure.
• In oligomeric proteins, each monomeric unit
has its own primary, secondary, tertiary
structure & then these monomeric units
interact with each other (quaternary
structure) to form a fully functional
oligomeric protein.
• Oligomeric proteins lose their biological
activity if the subunits are dissociated.
• Monomeric proteins consists of only
three types of structure – primary ,
secondary and tertiary.
• Oligomeric proteins consists of all four
types of proteins.
23. Know the Qs
Key Points to Remember
Ans6) Importance of higher structures of
proteins:
• Proteins are biologically active only in their
three dimensional conformations.
• So the biological activities of proteins are
attributed to their higher structures. If a
protein loses its three dimensional form (as
in denaturation), it loses its biological
activity.
Q6) Write a short note on the importance
of structures of proteins.
Ans 6)