This document provides an overview of protein chemistry, structure, and function. It begins by listing learning objectives related to describing protein structures like the peptide bond and classifying proteins. It then covers the primary, secondary, tertiary, and quaternary structures of proteins. Examples of globular proteins like hemoglobin and myoglobin and fibrous proteins like collagen and elastin are described. The document also discusses protein folding, misfolding diseases, and classification of proteins by function.
Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure is the three-dimensional folding determined by interactions between secondary structures. Quaternary structure involves interactions between multiple polypeptide chains. Proteins can also be classified based on shape, function, and composition. Denaturation disrupts non-covalent bonds leading to loss of native structure and biological function.
1. Proteins are complex organic macromolecules composed of amino acids arranged in a linear chain. They fold into complex three-dimensional shapes determined by their amino acid sequence.
2. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure involves folding into a compact 3D shape.
3. Misfolding of proteins can cause neurodegenerative diseases like Alzheimer's and prion diseases. Chaperone proteins assist the normal folding process to prevent misfolding.
Proteins are macromolecules made of amino acids linked by peptide bonds. They serve critical structural, functional, and regulatory roles in the body. Proteins have primary, secondary, tertiary and sometimes quarternary structures determined by their amino acid sequence. They perform diverse roles such as catalyzing biochemical reactions, transporting molecules, providing structure, and participating in immune defenses. Proteins are essential to the structure and function of all living organisms.
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
This document provides information on the structure and properties of proteins. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets. Tertiary structure involves the folding of the polypeptide chain. Quaternary structure involves the assembly of multiple polypeptide subunits. Proteins are classified by function, structure, composition, and nutritional value. Proteins play many important roles in the human body and are used in various applications.
This document discusses the classification and structure of proteins. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The secondary structure involves local folding patterns stabilized by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of a protein determined by interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple protein subunits. The document also categorizes proteins based on their biological functions and physical properties.
Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonds. Tertiary structure is the three-dimensional folding determined by interactions between secondary structures. Quaternary structure involves interactions between multiple polypeptide chains. Proteins can also be classified based on shape, function, and composition. Denaturation disrupts non-covalent bonds leading to loss of native structure and biological function.
1. Proteins are complex organic macromolecules composed of amino acids arranged in a linear chain. They fold into complex three-dimensional shapes determined by their amino acid sequence.
2. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure involves folding into a compact 3D shape.
3. Misfolding of proteins can cause neurodegenerative diseases like Alzheimer's and prion diseases. Chaperone proteins assist the normal folding process to prevent misfolding.
Proteins are macromolecules made of amino acids linked by peptide bonds. They serve critical structural, functional, and regulatory roles in the body. Proteins have primary, secondary, tertiary and sometimes quarternary structures determined by their amino acid sequence. They perform diverse roles such as catalyzing biochemical reactions, transporting molecules, providing structure, and participating in immune defenses. Proteins are essential to the structure and function of all living organisms.
Quaternary structure refers to the arrangement of multiple protein subunits into a single protein complex. Hemoglobin is a common example that is made of two alpha and two beta subunits. The subunits interact through hydrophobic interactions, hydrogen bonding, and other bonds. Globular proteins tend to have quaternary structure that clusters the subunits into a spherical shape, while fibrous proteins form long coils or sheets through interactions between subunits. Quaternary structure allows proteins to take on specialized functions beyond what individual subunits could achieve alone.
This document provides information on the structure and properties of proteins. It discusses the four levels of protein structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets. Tertiary structure involves the folding of the polypeptide chain. Quaternary structure involves the assembly of multiple polypeptide subunits. Proteins are classified by function, structure, composition, and nutritional value. Proteins play many important roles in the human body and are used in various applications.
This document discusses the classification and structure of proteins. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. The secondary structure involves local folding patterns stabilized by hydrogen bonds. The tertiary structure is the overall three-dimensional shape of a protein determined by interactions between amino acid side chains. Quaternary structure refers to the arrangement of multiple protein subunits. The document also categorizes proteins based on their biological functions and physical properties.
levels of protein structure , Domains ,motifs & Folds in protein structureAaqib Naseer
Protein structure is hierarchical, with four levels: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding between amino acids in the sequence. Tertiary structure involves folding of the entire chain into a compact 3D structure. Quaternary structure involves the assembly of protein subunits. Other structural features include domains, which are independently folded and functional regions, motifs like loops and barrels formed by secondary structure elements, and folds defined by the arrangement of alpha helices and beta sheets. Understanding protein structure is important for studying protein function and for developing drugs.
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
The document provides information about proteins including their introduction, chemical nature, physical properties, structure, classification, and functions. Some key points:
- Proteins are macromolecules composed of amino acid chains that serve important structural and functional roles in the body.
- They have complex hierarchical structures ranging from primary sequences to quaternary arrangements and take on globular or fibrous shapes.
- Proteins can be classified based on their shape, composition, solubility, and biological function. This includes categories like enzymes, structural proteins, and transport proteins.
- In addition to providing structure, proteins regulate body chemistry through roles as hormones, antibodies, and contractile proteins involved in muscle movement.
The document discusses tertiary and quaternary protein structures. It defines tertiary structure as the specific 3D shape of a protein based on interactions between amino acid side chains. Tertiary structure results from disulfide bonds, hydrophobic interactions, hydrogen bonds, ionic interactions, and Van der Waals forces. Quaternary structure refers to the assembly of multiple polypeptide subunits into a single functional protein. Protein folding and molecular chaperones facilitate proper tertiary and quaternary structure formation.
Unit 2: Proteins, abnormalities and methods of proteins investigation DrElhamSharif
This document outlines the objectives and content of a lecture series on proteins, abnormalities, and methods of protein investigation. The objectives include identifying various proteins, distinguishing acute phase reactants, identifying causes of abnormal protein levels, and differentiating types of proteinuria. The document then covers topics such as protein structure and function, classification of proteins, plasma proteins including albumin and globulins, medical relevance of amino acids and total protein, and details on specific proteins like prealbumin and albumin. Laboratory methods for analyzing proteins are also discussed.
This document discusses proteins and their structure and functions. It notes that proteins are composed of chains of amino acids and perform a variety of important functions in organisms, including catalyzing reactions and transporting molecules. It describes the primary, secondary, tertiary, and quaternary structure of proteins. Proteins are assembled through the translation of genetic codes and can be synthesized chemically in laboratories. The document outlines several key cellular functions of proteins and notes they are responsible for carrying out the instructions specified in genes.
This document discusses protein structure and folding. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves folding into alpha helices or beta sheets. Tertiary structure is the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to interactions between multiple polypeptide chains in a protein. The document also discusses protein folding, denaturation, and misfolding, noting that many neurodegenerative diseases are associated with misfolded protein aggregates.
Proteins are composed of chains of amino acids linked together by peptide bonds. There are 20 common amino acids that make up proteins. The sequence of amino acids is determined by the DNA sequence. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Proteins serve many important functions in the body such as catalysis, muscle contraction, cytoskeleton structure, transport, cell signaling, and immunity.
Proteins-Classification ,Structure of protein, properties and biological impo...SoniaBajaj10
This document provides an overview of proteins, including their definition, classification, structure, and properties. It discusses how proteins are composed of amino acids and classified based on their chemical nature, structure, shape and solubility. The four levels of protein structure - primary, secondary, tertiary, and quaternary structure - are also summarized. Key properties of proteins like solubility, denaturation and functions in the body are highlighted. The document serves as an introduction to proteins and provides a high-level classification and structural overview.
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
PROTEINS & LEVELS OF STRUCTURAL CONFORMATION pptx.pptxVIVIEN63
This document discusses various aspects of protein structure and function. It begins by defining proteins and describing their essential roles in the body. It then covers the four levels of protein structural organization: primary, secondary, tertiary, and quaternary structure. Specific examples are provided to illustrate alpha helices, beta sheets, and triple helical structures. The document also discusses protein classification, functions, and conjugated proteins. Overall, it provides a comprehensive overview of the key concepts regarding protein structure and the important roles of proteins in biological systems.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
This document provides an overview of proteins, including their classification, structure, and functions. It discusses how proteins are formed through peptide bonds between amino acids. It describes the primary, secondary, tertiary, and quaternary structure of proteins and how hydrogen bonds, disulfide bonds, and other interactions stabilize protein structures. The document also covers different types of proteins classified by composition, shape, and solubility, including globular, fibrous, albumins, globulins, and others. Key protein functions like catalysis and structure are summarized.
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Protein is composed of amino acids and is necessary for proper growth and function of the human body. It has many important biological functions including structural, enzymatic, transport, motile, regulatory, and storage functions. There are different types and levels of protein structure. Changes in protein shape can cause diseases like prion diseases and Creutzfeldt-Jakob disease which affect the nervous system. These diseases are difficult to diagnose and are generally fatal.
Proteins are composed of amino acids linked together in chains and serve important functions in the body. They exist in complex 3D structures including primary, secondary, tertiary and quaternary forms which determine their function. Proteins can be classified based on their composition, function, shape or nature. They play key roles such as structure, movement, signaling, catalysis and immunity. Their importance includes being enzymes, hormones, structural components and in processes like DNA expression, oxygen transport, homeostasis and immunity.
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UPRAHUL
This Dissertation explores the particular circumstances of Mirzapur, a region located in the
core of India. Mirzapur, with its varied terrains and abundant biodiversity, offers an optimal
environment for investigating the changes in vegetation cover dynamics. Our study utilizes
advanced technologies such as GIS (Geographic Information Systems) and Remote sensing to
analyze the transformations that have taken place over the course of a decade.
The complex relationship between human activities and the environment has been the focus
of extensive research and worry. As the global community grapples with swift urbanization,
population expansion, and economic progress, the effects on natural ecosystems are becoming
more evident. A crucial element of this impact is the alteration of vegetation cover, which plays a
significant role in maintaining the ecological equilibrium of our planet.Land serves as the foundation for all human activities and provides the necessary materials for
these activities. As the most crucial natural resource, its utilization by humans results in different
'Land uses,' which are determined by both human activities and the physical characteristics of the
land.
The utilization of land is impacted by human needs and environmental factors. In countries
like India, rapid population growth and the emphasis on extensive resource exploitation can lead
to significant land degradation, adversely affecting the region's land cover.
Therefore, human intervention has significantly influenced land use patterns over many
centuries, evolving its structure over time and space. In the present era, these changes have
accelerated due to factors such as agriculture and urbanization. Information regarding land use and
cover is essential for various planning and management tasks related to the Earth's surface,
providing crucial environmental data for scientific, resource management, policy purposes, and
diverse human activities.
Accurate understanding of land use and cover is imperative for the development planning
of any area. Consequently, a wide range of professionals, including earth system scientists, land
and water managers, and urban planners, are interested in obtaining data on land use and cover
changes, conversion trends, and other related patterns. The spatial dimensions of land use and
cover support policymakers and scientists in making well-informed decisions, as alterations in
these patterns indicate shifts in economic and social conditions. Monitoring such changes with the
help of Advanced technologies like Remote Sensing and Geographic Information Systems is
crucial for coordinated efforts across different administrative levels. Advanced technologies like
Remote Sensing and Geographic Information Systems
9
Changes in vegetation cover refer to variations in the distribution, composition, and overall
structure of plant communities across different temporal and spatial scales. These changes can
occur natural.
levels of protein structure , Domains ,motifs & Folds in protein structureAaqib Naseer
Protein structure is hierarchical, with four levels: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structures include alpha helices and beta sheets formed by hydrogen bonding between amino acids in the sequence. Tertiary structure involves folding of the entire chain into a compact 3D structure. Quaternary structure involves the assembly of protein subunits. Other structural features include domains, which are independently folded and functional regions, motifs like loops and barrels formed by secondary structure elements, and folds defined by the arrangement of alpha helices and beta sheets. Understanding protein structure is important for studying protein function and for developing drugs.
Proteins are essential macromolecules that make up 20% of the human body. They are composed of amino acids and perform many critical functions including structure, regulation, catalysis, movement and more. Protein synthesis occurs in ribosomes within cells. Proteins are not stored but are broken down if excess amino acids are consumed. They have primary, secondary, tertiary and quaternary levels of structure determined by amino acid sequence and interactions. There are 20 standard amino acids that are linked by peptide bonds to form proteins.
The document provides information about proteins including their introduction, chemical nature, physical properties, structure, classification, and functions. Some key points:
- Proteins are macromolecules composed of amino acid chains that serve important structural and functional roles in the body.
- They have complex hierarchical structures ranging from primary sequences to quaternary arrangements and take on globular or fibrous shapes.
- Proteins can be classified based on their shape, composition, solubility, and biological function. This includes categories like enzymes, structural proteins, and transport proteins.
- In addition to providing structure, proteins regulate body chemistry through roles as hormones, antibodies, and contractile proteins involved in muscle movement.
The document discusses tertiary and quaternary protein structures. It defines tertiary structure as the specific 3D shape of a protein based on interactions between amino acid side chains. Tertiary structure results from disulfide bonds, hydrophobic interactions, hydrogen bonds, ionic interactions, and Van der Waals forces. Quaternary structure refers to the assembly of multiple polypeptide subunits into a single functional protein. Protein folding and molecular chaperones facilitate proper tertiary and quaternary structure formation.
Unit 2: Proteins, abnormalities and methods of proteins investigation DrElhamSharif
This document outlines the objectives and content of a lecture series on proteins, abnormalities, and methods of protein investigation. The objectives include identifying various proteins, distinguishing acute phase reactants, identifying causes of abnormal protein levels, and differentiating types of proteinuria. The document then covers topics such as protein structure and function, classification of proteins, plasma proteins including albumin and globulins, medical relevance of amino acids and total protein, and details on specific proteins like prealbumin and albumin. Laboratory methods for analyzing proteins are also discussed.
This document discusses proteins and their structure and functions. It notes that proteins are composed of chains of amino acids and perform a variety of important functions in organisms, including catalyzing reactions and transporting molecules. It describes the primary, secondary, tertiary, and quaternary structure of proteins. Proteins are assembled through the translation of genetic codes and can be synthesized chemically in laboratories. The document outlines several key cellular functions of proteins and notes they are responsible for carrying out the instructions specified in genes.
This document discusses protein structure and folding. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves folding into alpha helices or beta sheets. Tertiary structure is the overall 3D shape formed by interactions between amino acid side chains. Quaternary structure refers to interactions between multiple polypeptide chains in a protein. The document also discusses protein folding, denaturation, and misfolding, noting that many neurodegenerative diseases are associated with misfolded protein aggregates.
Proteins are composed of chains of amino acids linked together by peptide bonds. There are 20 common amino acids that make up proteins. The sequence of amino acids is determined by the DNA sequence. Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Proteins serve many important functions in the body such as catalysis, muscle contraction, cytoskeleton structure, transport, cell signaling, and immunity.
Proteins-Classification ,Structure of protein, properties and biological impo...SoniaBajaj10
This document provides an overview of proteins, including their definition, classification, structure, and properties. It discusses how proteins are composed of amino acids and classified based on their chemical nature, structure, shape and solubility. The four levels of protein structure - primary, secondary, tertiary, and quaternary structure - are also summarized. Key properties of proteins like solubility, denaturation and functions in the body are highlighted. The document serves as an introduction to proteins and provides a high-level classification and structural overview.
- The document discusses protein metabolism and nitrogen fixation. It covers the classification of proteins based on their structure, composition, and functions. There are four levels of protein structure - primary, secondary, tertiary, and quaternary.
- The primary structure is the linear sequence of amino acids. The secondary structure involves folding into alpha helices or beta sheets via hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid R groups. Quaternary structure applies to proteins with multiple polypeptide chains that combine to form complexes.
- Proteins are classified as globular, fibrous, or intermediate based on their shape. They can also be simple or conjugated based on composition
PROTEINS & LEVELS OF STRUCTURAL CONFORMATION pptx.pptxVIVIEN63
This document discusses various aspects of protein structure and function. It begins by defining proteins and describing their essential roles in the body. It then covers the four levels of protein structural organization: primary, secondary, tertiary, and quaternary structure. Specific examples are provided to illustrate alpha helices, beta sheets, and triple helical structures. The document also discusses protein classification, functions, and conjugated proteins. Overall, it provides a comprehensive overview of the key concepts regarding protein structure and the important roles of proteins in biological systems.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
This document provides an overview of proteins, including their classification, structure, and functions. It discusses how proteins are formed through peptide bonds between amino acids. It describes the primary, secondary, tertiary, and quaternary structure of proteins and how hydrogen bonds, disulfide bonds, and other interactions stabilize protein structures. The document also covers different types of proteins classified by composition, shape, and solubility, including globular, fibrous, albumins, globulins, and others. Key protein functions like catalysis and structure are summarized.
Proteins play key roles in living systems through catalysis, transport, and information transfer. They have a hierarchical structure including primary, secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence, and higher levels of organization are determined by the primary structure. Protein folding and interactions between residues determine the final 3D tertiary and quaternary structures, which are critical for protein function. Misfolded proteins can cause diseases.
Protein is composed of amino acids and is necessary for proper growth and function of the human body. It has many important biological functions including structural, enzymatic, transport, motile, regulatory, and storage functions. There are different types and levels of protein structure. Changes in protein shape can cause diseases like prion diseases and Creutzfeldt-Jakob disease which affect the nervous system. These diseases are difficult to diagnose and are generally fatal.
Proteins are composed of amino acids linked together in chains and serve important functions in the body. They exist in complex 3D structures including primary, secondary, tertiary and quaternary forms which determine their function. Proteins can be classified based on their composition, function, shape or nature. They play key roles such as structure, movement, signaling, catalysis and immunity. Their importance includes being enzymes, hormones, structural components and in processes like DNA expression, oxygen transport, homeostasis and immunity.
LAND USE LAND COVER AND NDVI OF MIRZAPUR DISTRICT, UPRAHUL
This Dissertation explores the particular circumstances of Mirzapur, a region located in the
core of India. Mirzapur, with its varied terrains and abundant biodiversity, offers an optimal
environment for investigating the changes in vegetation cover dynamics. Our study utilizes
advanced technologies such as GIS (Geographic Information Systems) and Remote sensing to
analyze the transformations that have taken place over the course of a decade.
The complex relationship between human activities and the environment has been the focus
of extensive research and worry. As the global community grapples with swift urbanization,
population expansion, and economic progress, the effects on natural ecosystems are becoming
more evident. A crucial element of this impact is the alteration of vegetation cover, which plays a
significant role in maintaining the ecological equilibrium of our planet.Land serves as the foundation for all human activities and provides the necessary materials for
these activities. As the most crucial natural resource, its utilization by humans results in different
'Land uses,' which are determined by both human activities and the physical characteristics of the
land.
The utilization of land is impacted by human needs and environmental factors. In countries
like India, rapid population growth and the emphasis on extensive resource exploitation can lead
to significant land degradation, adversely affecting the region's land cover.
Therefore, human intervention has significantly influenced land use patterns over many
centuries, evolving its structure over time and space. In the present era, these changes have
accelerated due to factors such as agriculture and urbanization. Information regarding land use and
cover is essential for various planning and management tasks related to the Earth's surface,
providing crucial environmental data for scientific, resource management, policy purposes, and
diverse human activities.
Accurate understanding of land use and cover is imperative for the development planning
of any area. Consequently, a wide range of professionals, including earth system scientists, land
and water managers, and urban planners, are interested in obtaining data on land use and cover
changes, conversion trends, and other related patterns. The spatial dimensions of land use and
cover support policymakers and scientists in making well-informed decisions, as alterations in
these patterns indicate shifts in economic and social conditions. Monitoring such changes with the
help of Advanced technologies like Remote Sensing and Geographic Information Systems is
crucial for coordinated efforts across different administrative levels. Advanced technologies like
Remote Sensing and Geographic Information Systems
9
Changes in vegetation cover refer to variations in the distribution, composition, and overall
structure of plant communities across different temporal and spatial scales. These changes can
occur natural.
This slide is special for master students (MIBS & MIFB) in UUM. Also useful for readers who are interested in the topic of contemporary Islamic banking.
How to Add Chatter in the odoo 17 ERP ModuleCeline George
In Odoo, the chatter is like a chat tool that helps you work together on records. You can leave notes and track things, making it easier to talk with your team and partners. Inside chatter, all communication history, activity, and changes will be displayed.
Exploiting Artificial Intelligence for Empowering Researchers and Faculty, In...Dr. Vinod Kumar Kanvaria
Exploiting Artificial Intelligence for Empowering Researchers and Faculty,
International FDP on Fundamentals of Research in Social Sciences
at Integral University, Lucknow, 06.06.2024
By Dr. Vinod Kumar Kanvaria
ISO/IEC 27001, ISO/IEC 42001, and GDPR: Best Practices for Implementation and...PECB
Denis is a dynamic and results-driven Chief Information Officer (CIO) with a distinguished career spanning information systems analysis and technical project management. With a proven track record of spearheading the design and delivery of cutting-edge Information Management solutions, he has consistently elevated business operations, streamlined reporting functions, and maximized process efficiency.
Certified as an ISO/IEC 27001: Information Security Management Systems (ISMS) Lead Implementer, Data Protection Officer, and Cyber Risks Analyst, Denis brings a heightened focus on data security, privacy, and cyber resilience to every endeavor.
His expertise extends across a diverse spectrum of reporting, database, and web development applications, underpinned by an exceptional grasp of data storage and virtualization technologies. His proficiency in application testing, database administration, and data cleansing ensures seamless execution of complex projects.
What sets Denis apart is his comprehensive understanding of Business and Systems Analysis technologies, honed through involvement in all phases of the Software Development Lifecycle (SDLC). From meticulous requirements gathering to precise analysis, innovative design, rigorous development, thorough testing, and successful implementation, he has consistently delivered exceptional results.
Throughout his career, he has taken on multifaceted roles, from leading technical project management teams to owning solutions that drive operational excellence. His conscientious and proactive approach is unwavering, whether he is working independently or collaboratively within a team. His ability to connect with colleagues on a personal level underscores his commitment to fostering a harmonious and productive workplace environment.
Date: May 29, 2024
Tags: Information Security, ISO/IEC 27001, ISO/IEC 42001, Artificial Intelligence, GDPR
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How to Build a Module in Odoo 17 Using the Scaffold MethodCeline George
Odoo provides an option for creating a module by using a single line command. By using this command the user can make a whole structure of a module. It is very easy for a beginner to make a module. There is no need to make each file manually. This slide will show how to create a module using the scaffold method.
This presentation was provided by Steph Pollock of The American Psychological Association’s Journals Program, and Damita Snow, of The American Society of Civil Engineers (ASCE), for the initial session of NISO's 2024 Training Series "DEIA in the Scholarly Landscape." Session One: 'Setting Expectations: a DEIA Primer,' was held June 6, 2024.
A review of the growth of the Israel Genealogy Research Association Database Collection for the last 12 months. Our collection is now passed the 3 million mark and still growing. See which archives have contributed the most. See the different types of records we have, and which years have had records added. You can also see what we have for the future.
1. CHEMISTRY OF
PROTEINS
Learning Objectives
As a result of this class, students shall be able to: Describe the
peptide bond
Describe the Biuret qualitative and quantitative tests for
proteins
Classify proteins as simple or conjugated
Classify proteins based on their functions
Classify proteins based on their shapes
Describe the primary, secondary, tertiary and quaternary
structures of proteins
Describe protein denaturation
Discuss protein misfolding; Prion diseases, Alzheimer disease
2. Learning Objectives,
continued
Describe myoglobin and hemoglobin as examples of
globular proteins
Describe collagen and elastin as examples of fibrous
proteins
Describe the following hemoglobinopathies in simple
terms—sickle cell disease, HbC, HbSC, Thalassemias
Compare collagen with elastin in terms of structure
and functions. Describe the collagen and elastin
diseases
Differentiate between plasma and serum.
Identify the serum proteins and their functions
4. 20 amino acids are
used to synthesize
proteins; they are
joined together by
peptide bonds.
Linear sequence of
the amino acid
residues contains the
information
necessary to
generate a protein
molecule with a
unique three-
dimensional shape.
Complexity of
protein structure
is best analyzed
by considering
the molecule in
terms of 4
organizational
levels: primary,
secondary,
tertiary, and
quaternary
levels.
5. Primary Structure of
Proteins
The primary structure of a protein is
defined as the linear sequence of its
amino acids.
Understanding the primary structure of
proteins is important because many
genetic diseases result in proteins with
abnormal amino acid sequences, which
can cause improper folding and loss or
impairment of normal function.
6.
7. Peptide bonds join
the individual amino
acids, attaching the
α-amino group of one
amino acid to the α-
carboxyl group of
another.
The peptide bonds
can be hydrolyzed
non-enzymatically by
prolonged exposure
to a strong acid or
base at elevated
temperatures.
Peptide bonds have a
partial double-bond
character (shorter
than single bonds;
rigid and planar).
They are generally in
the trans
configuration.
They are polar, and
can hydrogen bond
to each other or to
other polar
compounds.
8. Amino-terminal (N-
terminal) end:
written to the left.
Carboxyl-terminal
(C-terminal) end:
written to the
right.
Each component
amino acid in a
polypeptide is
called a “residue”
or “moiety”.
--Amino acid sequences are
read from the N- to the C-
terminal end of the peptide.
9. SECONDARY STRUCTURE
OF PROTEINS
The secondary structure of a protein is
generally defined as regular arrangements
of amino acids that are located near to each
other in the linear sequence.
Examples of such elements are the α-helix,
β-sheet, and β-bends (reverse turns).
Some secondary structure is not regular,
but rather is considered non-repetitive
(loop or coil).
10. A and B are antiparallel: the two strands are in
opposite orientations.
B and C are parallel: the two strands are in the same
orientation
11. Diagrams 2 and 3 show two different views of the same
beta - pleated sheets rich protein. In yellow, the parts of
the protein involved in the beta - pleated sheets; in
pink, some alpha - helices. Loops are in grey / white.
12. Secondary structural elements are stabilized by
extensive hydrogen bonding.
Supersecondary structures (motifs) are produced by
packing side chains from adjacent secondary
structural elements close to each other.
13. TERTIARY STRUCTURE OF
GLOBULAR PROTEINS
--The primary structure of a
polypeptide determines its
tertiary structure.
--Domains are the fundamental
functional and three-
dimensional structural units
of a polypeptide.
--They are formed from
combinations of motifs.
--Tertiary structure refers to
the folding of the domains
and their final arrangement
in the polypeptide.
Tertiary structure is stabilized by
disulfide bonds, hydrophobic
interactions, hydrogen bonds,
and ionic bonds.
A specialized group of proteins,
named chaperones, is required
for the proper folding of many
species of proteins.
14. QUATERNARY STRUCTURE
OF PROTEINS
Proteins consisting of
more than one
polypeptide chain have
quaternary structure.
2 subunits—dimeric (the
protein is a dimer);
3 subunits—trimeric;
4 subunits—tetrameric;
Several subunits—
multimeric.
--Subunits are held
together by noncovalent
interactions (e.g.,
hydrogen bonds, ionic
bonds, and hydrophobic
interactions).
15. In some proteins, the subunits function
independently of each other.
In other proteins, e.g., hemoglobin, the subunits
work cooperatively: the binding of oxygen to one
subunit of hemoglobin increases the affinity of the
other subunits for oxygen.
16. DENATURATION OF
PROTEINS
Proteins can be denatured: unfolded and
disorganized; denaturation makes them
nonfunctional.
--denaturation results in the unfolding and
disorganization of the protein’s secondary and
tertiary structures;
--not accompanied by hydrolysis of peptide bonds
(primary structure not affected).
Denaturation agents include heat, organic solvents,
mechanical mixing, strong acids or bases, detergents,
and ions of heavy metals such as lead and mercury.
17. PROTEIN MISFOLDING
Protein misfolding may occur
spontaneously, or
caused by genetic mutation.
Some apparently normal proteins can,
after abnormal proteolytic cleavage,
take on a unique conformational state
that leads to the formation of long,
fibrillar protein assemblies consisting of
β-pleated sheets.
The spontaneously aggregating proteins
are called amyloids.
18. Alzheimer’s disease
Protein misfolding is implicated
in Alzheimer's disease (AD) --a
neurodegenerative disorder.
AD is characterized by
accumulation of amyloid plaque
(Aβ) and neurofibrillary tangles
(abnormal form of tau protein).
19. Prion diseases
Definition of Prion: A microscopic protein particle
similar to a virus but lacking nucleic acid---- the
infectious agent responsible for scrapie and certain
other degenerative diseases of the nervous system.
Prions — short for proteinaceous infectious particle
— are infectious protein structures that replicate
through conversion of normal host proteins of the
same type.
20. Though the exact mechanisms of
their actions and reproduction are
unknown, it is commonly accepted
that prions are responsible for a
number of previously known but
little-understood diseases generally
classified under transmissible
spongiform encephalopathy diseases
(TSEs), including scrapie (a disease
of sheep), kuru (found in members of
the cannibalistic Foré tribe in Papua
New Guinea), Creutzfeldt-Jakob
disease (CJD), Chronic Wasting
Disease, Fatal Familial Insomnia
(FFI), Gerstmann-Sträussler-
Scheinker syndrome (GSS), and
bovine spongiform encephalopathy
(BSE or mad cow disease).
These diseases
affect the
structure of
brain tissue and
all are fatal and
untreatable.
So far all prions
discovered are
believed to
infect and
replicate by
propagation of
an amyloid
fold.
21. FUNCTIONAL CLASSIFICATION
OF PROTEINS
Proteins can be classified
according to their
biological functions as
follows:
1. Enzymes: They are
proteins that catalyze
almost all the chemical
reactions in the cells.
E.g., catalase,
glucokinase, hexokinase.
2. Contractile and motile
proteins: They give the
cells and organisms the
ability to contract, to
change shape, or to move
about. Examples are the
muscle proteins myosin,
actin, troponin,
tropomyosin .
3. Structural proteins: They
serve as supporting filaments,
cables, or sheets, to give
strength and protection to
biological structures.
Examples are collagen,
keratin, and elastin.
4. Transport proteins:
Transport proteins of the
blood bind and carry specific
molecules or ions from one
organ to another. E.g.,
hemoglobin and plasma
proteins.
Transport proteins of cell
membranes transport
nutrients/ions across the
membrane into and out of
cells. E.g., Na+/K+-ATPase.
22. 5. Defence proteins:
These include the
antibodies which
recognize and destroy
invading bacteria, viruses,
or foreign proteins;
the blood-clotting proteins
(e.g., fibrinogen and
thrombin) which prevent
loss of blood when the
vascular system is injured,
the snake venoms,
bacterial toxins, and toxic
plant proteins (e.g., ricin)
which function in
defence.
6. Nutrient and storage
proteins: These include
the proteins in the seeds
of many plants, e.g.,
gliadins and glutelins of
cereals, and legumin of
legumes.
The major protein of egg
is ovalbumin and casein is
the major protein of milk.
Ferritin of animal tissues
stores iron.
23. 7. Regulatory proteins: These proteins regulate
cellular or physiological activities.
They include protein hormones such as insulin and
glucagon, and the gene-regulating proteins, such as
histones and non-histone proteins.
24. Globular and Fibrous
proteins
Proteins can also be
classified as either
globular or fibrous,
based on their overall
shape.
25. Fibrous proteins
Fibrous proteins are elongated
molecules in which the secondary
structure (either α-helices or β-pleated
sheets) forms the dominant structure.
Fibrous proteins are insoluble, and play
a structural or supportive role in the
body, and are also involved in
movement (as in muscle and ciliary
proteins).
One feature of fibrous tissues is that
they often have regular repeating
structures.
26. Keratin, for example, which is found in hair, horns,
wool, nails, and feathers, is a helix of helices (2 pairs
of α-helices wound around one another).
Collagen is the major protein component of
connective tissue. In collagen, every third amino acid
is glycine and many of the others are proline.
27. Globular proteins
Globular proteins are a highly diverse group of
proteins that are soluble and form compact
spheroidal molecules in water.
All have tertiary structure and some have
quaternary structure in addition to secondary
structure.
Globular proteins typically consist of relatively
straight runs of secondary structure joined by
stretches of polypeptides that abruptly change
direction.
Enzymes are globular proteins as are transport
proteins and receptor proteins.
Myoglobin and hemoglobin are globular proteins.
28. Aside from the difference in shape (elongated vs.
spheroidal) and solubility (insoluble vs. soluble),
fibrous proteins generally have only primary and
secondary structure whereas globular proteins have
tertiary and sometimes quaternary structure in
addition to primary and secondary structure.
29. COLLAGEN
Collagen: the most
abundant protein in the
human body.
A typical collagen
molecule is a long, stiff,
extracellular structure in
which three polypeptides
(referred to as “α-
chains”, each 1000 amino
acids in length) are wound
around one another in a
rope-like triple-helix.
The chains are held
together by hydrogen
bonds.
30. Collagen Diseases
Collagen diseases
include Ehlers-Danlos
syndrome,
Osteogenesis
imperfecta, Alport
syndrome and
Epidermolysis bullosa.
33. ELASTIN
Elastin consists of fibers, whose main
property is their elasticity. Elastin
fibers are composed of protein
molecules with the following properties
that differ from collagen in many
respects.
Elastin contains:
--Abundant glycine, about 33% (as in
collagen)
--Little hydroxyproline
--No hydroxylysine
34. Abundant hydrophobic amino acids
--Helical segments that are responsible for its
elasticity
--Desmosine in non-helical segments, which is
responsible for cross-linkage of the molecules to form
a network that can alter its configuration when
stretched.
35. The diagrams illustrate the cross-linking of elastin to
form a network
(a) in the relaxed state;
(b) when stretched.
36. ELASTIN DISEASES
Elastin diseases include cutis laxa, Marfan’s syndrome
(mutation in fibrillin gene) and α1-antiproteinase (α1-
antitrypsin) deficiency----causing emphysema.
38. HEMOGLOBIN AND MYOGLOBIN (EXAMPLES OF
GLOBULAR PROTEINS)
Myoglobin (Mb) is a
hemeprotein present in
heart and skeletal
muscle.
It functions both as a
reservoir for oxygen,
and as an oxygen carrier
that increases the rate
of transport of oxygen
within the muscle cell.
---consists of a single
polypeptide chain that is
structurally similar to
the individual subunit
polypeptide chains of
the hemoglobin
molecule.
39. Myoglobin has 153
aminoacyl residues
and molecular
weight of 17,000.
The surface is polar
and the interior
nonpolar—this is
characteristic of
globular proteins.
Apart from two
histidine residues
that function in
oxygen binding, the
interior of myoglobin
contains only
nonpolar residues
(e.g., Leu, Val, Phe,
Met).