Introduction to protein and classification by sohail
•Download as PPTX, PDF•
14 likes•3,480 views
This document provides an introduction and overview of protein structure and classification. It discusses the basic building blocks of proteins, the four levels of protein structure (primary, secondary, tertiary, and quaternary), and two main methods of protein classification - by shape (globular vs. fibrous proteins) and by function (enzymes, hormones, structural proteins, etc.). The document aims to cover key concepts about protein structure and organization in a comprehensive yet concise manner.
Report
Share
Report
Share
Recommended
4.3 proteins
Proteins are made up of elements like carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus. They are formed through condensation reactions between amino acids and can be broken down through hydrolysis. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids, secondary structure involves alpha helices and beta sheets, tertiary is the overall 3D shape, and quaternary involves combinations of tertiary structures. There are essential and non-essential amino acids, with essential ones not synthesized by the body.
Proteins and its classification in details by @sushant juneja
This document is a chemistry project report submitted by Sushant Juneja, a 12th grade student, to his teacher Mrs. Inderpreet Sujlana. The project is about proteins and includes an introduction, sections on amino acids, protein structure, classification of proteins, isoelectric pH, and protein denaturation. It provides details on the various levels of protein structure from primary to quaternary structure. It also classifies proteins based on function and shape.
Classification and properties of protein
This document discusses the classification and properties of proteins. It describes four levels of protein structure: primary, secondary, tertiary, and quaternary. Proteins can also be classified by their biological function, which includes enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, defense proteins, regulatory proteins, and other functional proteins. Classification by shape and solubility includes fibrous, globular, and membrane proteins. Classification by composition distinguishes between simple and conjugated proteins. Nutritionally, proteins are either complete or incomplete. The document concludes by discussing properties like denaturation and its causes like heat, alcohol, acids, bases, and heavy metal salts.
proteins and its classification
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.
Protein structural organisation
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.
Proteins
Proteins are macromolecules composed of amino acids linked by peptide bonds. They perform many important functions in the body and are obtained from both animal and plant sources. The document discusses the structure of proteins including their composition of amino acids, classification based on shape and complexity, properties, and sources. It provides a detailed overview of the key aspects of protein structure and function.
Proteins
This document discusses proteins and their structure. It begins by introducing proteins and their composition of amino acids linked into peptide chains. It then describes the 20 main amino acids and how they are classified. The four levels of protein structural organization - primary, secondary, tertiary, and quaternary structure - are outlined. Common secondary structures like the alpha helix and beta sheet are also defined. Specific proteins like hemoglobin and myoglobin are then examined in more detail, including their subunit composition and role in oxygen transport.
Protein sturucture
This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
Recommended
4.3 proteins
Proteins are made up of elements like carbon, hydrogen, oxygen, nitrogen, sulfur, and phosphorus. They are formed through condensation reactions between amino acids and can be broken down through hydrolysis. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids, secondary structure involves alpha helices and beta sheets, tertiary is the overall 3D shape, and quaternary involves combinations of tertiary structures. There are essential and non-essential amino acids, with essential ones not synthesized by the body.
Proteins and its classification in details by @sushant juneja
This document is a chemistry project report submitted by Sushant Juneja, a 12th grade student, to his teacher Mrs. Inderpreet Sujlana. The project is about proteins and includes an introduction, sections on amino acids, protein structure, classification of proteins, isoelectric pH, and protein denaturation. It provides details on the various levels of protein structure from primary to quaternary structure. It also classifies proteins based on function and shape.
Classification and properties of protein
This document discusses the classification and properties of proteins. It describes four levels of protein structure: primary, secondary, tertiary, and quaternary. Proteins can also be classified by their biological function, which includes enzymes, transport proteins, storage proteins, contractile/motile proteins, structural proteins, defense proteins, regulatory proteins, and other functional proteins. Classification by shape and solubility includes fibrous, globular, and membrane proteins. Classification by composition distinguishes between simple and conjugated proteins. Nutritionally, proteins are either complete or incomplete. The document concludes by discussing properties like denaturation and its causes like heat, alcohol, acids, bases, and heavy metal salts.
proteins and its classification
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.
Protein structural organisation
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.
Proteins
Proteins are macromolecules composed of amino acids linked by peptide bonds. They perform many important functions in the body and are obtained from both animal and plant sources. The document discusses the structure of proteins including their composition of amino acids, classification based on shape and complexity, properties, and sources. It provides a detailed overview of the key aspects of protein structure and function.
Proteins
This document discusses proteins and their structure. It begins by introducing proteins and their composition of amino acids linked into peptide chains. It then describes the 20 main amino acids and how they are classified. The four levels of protein structural organization - primary, secondary, tertiary, and quaternary structure - are outlined. Common secondary structures like the alpha helix and beta sheet are also defined. Specific proteins like hemoglobin and myoglobin are then examined in more detail, including their subunit composition and role in oxygen transport.
Protein sturucture
This document discusses protein structure and function. It begins by defining proteins and their essential roles in the human body. It then describes the general characteristics of proteins, such as their chemical composition and functions. The document classifies proteins based on their composition, axial ratio, and biological functions. It explains the different levels of protein structure from primary to quaternary, focusing on secondary structure elements like alpha helices and beta sheets. The roles of hydrogen bonding, disulfide bridges, and ionic bonds in tertiary and quaternary structure are also described.
Protein: structure, classification,function and assay methods
definition , alpha helix beta pleated sheets tertiary and quarternary structure , peptide bond protein classification , assay methods, rhuemanns purple
Protein Structure & Function
The document discusses the levels of protein structure from primary to quaternary structure. It defines the primary structure as the amino acid sequence. Secondary structure forms from hydrogen bonding between amino acids and includes alpha helices and beta pleated sheets. Tertiary structure results from folding influenced by interactions between amino acid side chains. Quaternary structure occurs when multiple polypeptide chains interact to form a protein complex. Examples including hemoglobin and glyceraldehyde-3-phosphate dehydrogenase are provided to illustrate the different levels of structure.
Classif. amino acids proteins
Amino Acids are the building units of proteins. Proteins are polymers of amino acids linked together by what is called
“ Peptide bond”.
Protein classification
Proteins are complex biomolecules composed of amino acids. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves folding into shapes like alpha helices and beta sheets. Tertiary structure is the overall 3D shape of a single protein chain. Quaternary structure refers to the shape of proteins with multiple chains. Proteins are classified based on shape (globular or fibrous) and function (enzymes, hormones, etc.). They have various properties including solubility, hydrolysis, and denaturation.
Biochemistry lecture notes proteins
Proteins have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonding between amino acid residues. Tertiary structure involves folding of the chain into a three-dimensional shape determined by interactions between R groups. Quaternary structure refers to complexes of multiple polypeptide subunits held together by various bonds and interactions. Hemoglobin is an example of a protein with quaternary structure, consisting of four subunits - two alpha chains and two beta chains.
Protein
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.
PROTEINS
Proteins have a variety of important functions in living organisms. They are made up of chains of amino acids that join together to form complex structures ranging from simple primary to advanced quaternary structures which determine their specific roles. Globular proteins have spherical shapes defined by their amino acid sequences which allow metabolic functions like enzymatic reactions, while changes in structure through denaturation disrupt protein functioning.
Protein structure
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 bonding of the polypeptide chain. Tertiary structure refers to the overall three-dimensional shape that results from interactions between amino acid side chains. Quaternary structure involves interactions between multiple protein subunits.
Proteins: Biochemistry
Proteins are naturally occurring polymers made up of amino acids and linked together by peptide bonds.
Proteins are the most abundant organic molecules in the living system.
The term "protein" is derived from the Greek word proteios, meaning holding the first place.
These are nitrogenous organic compounds that have large molecules weight of one or more long chains of amino acids.
Proteins are made from 20 ɑ-amino acids. (chains of amino acids)
A single unit of amino acid is known as a monomer. When many monomers combine together, they form polymers.
THE THREE DIMENSIONAL STRUCTURE OF PROTEINS.pdf
The document discusses the hierarchical structure of proteins from primary to quaternary levels. It describes the basic classifications of proteins and the secondary structures of alpha helices and beta sheets. Tertiary structure is formed by folding and interactions between amino acid side chains. Quaternary structure arises from the association of multiple polypeptide chains. Examples discussed include collagen, myoglobin and hemoglobin which have distinct tertiary and quaternary configurations that enable their functions.
Proteins
This document discusses the structure and properties of amino acids and proteins. It begins by defining amino acids as organic compounds containing amino and carboxyl groups. There are 20 standard amino acids that combine to form proteins through peptide bonds. The document then covers protein structure, describing primary, secondary, tertiary, and quaternary levels. Common structural elements like alpha helices, beta sheets, and turns are explained. The document concludes by classifying proteins based on solubility, shape and nutritional importance.
Proteins
Biochemistry of Proteins. and an overview of the protein structure and classification. also explains the biological significance of proteins in Body.
Proteins
Proteins have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
Protein structure and function
proteins their structure ,types of structures ,there roles in our life there major function at minor and major level .there building blocks .
Structure of protiens and the applied aspects
The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
Chemistry of amino acids
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, PRIMARY, SECONDARY, TERTIARY AND QUATERNARY STRUCTURE, FIBROUS AND GLOBULAR STRUCTURE, SOURCES, TYPES OF PROTEINS, FUNCTIONS,DEFICIENCIES
Structural organisation of protiens
Proteins are polymers of amino acids joined by peptide bonds. They have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures include alpha helices and beta sheets. Tertiary structure refers to the overall 3D shape of a protein formed by interactions between residues. Quaternary structure involves interactions between multiple polypeptide subunits. Examples like myoglobin, hemoglobin, and collagen illustrate these different structural levels.
STRUCTURAL ORGANIZATION OF PROTEINS
Primary structure of protein
Secondary structure of protein
Tertiary structure of protein
Quaternary structure of protein
Methods to determine protein structure
Conclusion
References
METHODS TO DETERMINE PROTEIN STRUCTURE
Each protein has a unique sequence of amino acids.
The amino acids are held together in a protein by
covalent peptide bonds or linkages.
A peptide bond are formed when amino group of an
amino acid combines with the carboxyl group of another.
The conformation of polypeptide chain by twisting or folding is referred to as secondary structure.
Two types of secondary structures α-helix and β-sheet are mainly identified.
α-Helical structure was proposed by Pauling and Corey in 1951.
It occurs when the sequence of amino acids are linked by hydrogen bonds.
Each turn of α-helix contains 3.6 amino acids.
β-pleated sheets are composed of two or more segments of fully extended peptide chains.
β-Sheets may be arranged either in parallel or anti-parallel direction.
Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs.
The three dimensional arrangement of protein structure is referred to as tertiary structure.
It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface.
This type of arrangement provide stability of the molecule.
Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
Protein metabolism and nitrogen fixation and metabolism
- 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
Protein classification
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
More Related Content
What's hot
Protein: structure, classification,function and assay methods
definition , alpha helix beta pleated sheets tertiary and quarternary structure , peptide bond protein classification , assay methods, rhuemanns purple
Protein Structure & Function
The document discusses the levels of protein structure from primary to quaternary structure. It defines the primary structure as the amino acid sequence. Secondary structure forms from hydrogen bonding between amino acids and includes alpha helices and beta pleated sheets. Tertiary structure results from folding influenced by interactions between amino acid side chains. Quaternary structure occurs when multiple polypeptide chains interact to form a protein complex. Examples including hemoglobin and glyceraldehyde-3-phosphate dehydrogenase are provided to illustrate the different levels of structure.
Classif. amino acids proteins
Amino Acids are the building units of proteins. Proteins are polymers of amino acids linked together by what is called
“ Peptide bond”.
Protein classification
Proteins are complex biomolecules composed of amino acids. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structure involves folding into shapes like alpha helices and beta sheets. Tertiary structure is the overall 3D shape of a single protein chain. Quaternary structure refers to the shape of proteins with multiple chains. Proteins are classified based on shape (globular or fibrous) and function (enzymes, hormones, etc.). They have various properties including solubility, hydrolysis, and denaturation.
Biochemistry lecture notes proteins
Proteins have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonding between amino acid residues. Tertiary structure involves folding of the chain into a three-dimensional shape determined by interactions between R groups. Quaternary structure refers to complexes of multiple polypeptide subunits held together by various bonds and interactions. Hemoglobin is an example of a protein with quaternary structure, consisting of four subunits - two alpha chains and two beta chains.
Protein
Proteins are composed of amino acids and play many essential roles in the body. They have four levels of structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence, secondary involves hydrogen bonding into shapes like alpha helices and beta sheets, tertiary is the 3D folding of these structures, and quaternary involves the assembly of multiple protein subunits. Proteins serve as enzymes, hormones, antibodies, and structures. They undergo synthesis from amino acids and breakdown through catabolism. Disorders can occur if amino acid metabolism is disrupted.
PROTEINS
Proteins have a variety of important functions in living organisms. They are made up of chains of amino acids that join together to form complex structures ranging from simple primary to advanced quaternary structures which determine their specific roles. Globular proteins have spherical shapes defined by their amino acid sequences which allow metabolic functions like enzymatic reactions, while changes in structure through denaturation disrupt protein functioning.
Protein structure
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 bonding of the polypeptide chain. Tertiary structure refers to the overall three-dimensional shape that results from interactions between amino acid side chains. Quaternary structure involves interactions between multiple protein subunits.
Proteins: Biochemistry
Proteins are naturally occurring polymers made up of amino acids and linked together by peptide bonds.
Proteins are the most abundant organic molecules in the living system.
The term "protein" is derived from the Greek word proteios, meaning holding the first place.
These are nitrogenous organic compounds that have large molecules weight of one or more long chains of amino acids.
Proteins are made from 20 ɑ-amino acids. (chains of amino acids)
A single unit of amino acid is known as a monomer. When many monomers combine together, they form polymers.
THE THREE DIMENSIONAL STRUCTURE OF PROTEINS.pdf
The document discusses the hierarchical structure of proteins from primary to quaternary levels. It describes the basic classifications of proteins and the secondary structures of alpha helices and beta sheets. Tertiary structure is formed by folding and interactions between amino acid side chains. Quaternary structure arises from the association of multiple polypeptide chains. Examples discussed include collagen, myoglobin and hemoglobin which have distinct tertiary and quaternary configurations that enable their functions.
Proteins
This document discusses the structure and properties of amino acids and proteins. It begins by defining amino acids as organic compounds containing amino and carboxyl groups. There are 20 standard amino acids that combine to form proteins through peptide bonds. The document then covers protein structure, describing primary, secondary, tertiary, and quaternary levels. Common structural elements like alpha helices, beta sheets, and turns are explained. The document concludes by classifying proteins based on solubility, shape and nutritional importance.
Proteins
Biochemistry of Proteins. and an overview of the protein structure and classification. also explains the biological significance of proteins in Body.
Proteins
Proteins have many important functions in the body including structure, catalysis, movement, transport, hormones, protection, storage, and regulation. They are composed of amino acids that are linked together through peptide bonds to form polypeptide chains or folded structures. The structure of proteins includes primary, secondary, tertiary, and sometimes quaternary levels that determine the protein's shape and function. Denaturation can disrupt a protein's structure through physical or chemical means.
Protein structure and function
proteins their structure ,types of structures ,there roles in our life there major function at minor and major level .there building blocks .
Structure of protiens and the applied aspects
The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
Chemistry of amino acids
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
Structure of protein
This document summarizes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It provides details on each level: primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure involves hydrogen bonding between amino acids to form regular structures like alpha helices and beta pleated sheets. Tertiary structure describes the overall 3D shape of the protein arising from secondary structures. Quaternary structure involves interactions between two or more polypeptide chains, as seen in hemoglobin which is made of four polypeptide subunits.
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, PRIMARY, SECONDARY, TERTIARY AND QUATERNARY STRUCTURE, FIBROUS AND GLOBULAR STRUCTURE, SOURCES, TYPES OF PROTEINS, FUNCTIONS,DEFICIENCIES
Structural organisation of protiens
Proteins are polymers of amino acids joined by peptide bonds. They have four levels of structural organization: primary, secondary, tertiary, and quaternary. The primary structure is the linear sequence of amino acids. Secondary structures include alpha helices and beta sheets. Tertiary structure refers to the overall 3D shape of a protein formed by interactions between residues. Quaternary structure involves interactions between multiple polypeptide subunits. Examples like myoglobin, hemoglobin, and collagen illustrate these different structural levels.
STRUCTURAL ORGANIZATION OF PROTEINS
Primary structure of protein
Secondary structure of protein
Tertiary structure of protein
Quaternary structure of protein
Methods to determine protein structure
Conclusion
References
METHODS TO DETERMINE PROTEIN STRUCTURE
Each protein has a unique sequence of amino acids.
The amino acids are held together in a protein by
covalent peptide bonds or linkages.
A peptide bond are formed when amino group of an
amino acid combines with the carboxyl group of another.
The conformation of polypeptide chain by twisting or folding is referred to as secondary structure.
Two types of secondary structures α-helix and β-sheet are mainly identified.
α-Helical structure was proposed by Pauling and Corey in 1951.
It occurs when the sequence of amino acids are linked by hydrogen bonds.
Each turn of α-helix contains 3.6 amino acids.
β-pleated sheets are composed of two or more segments of fully extended peptide chains.
β-Sheets may be arranged either in parallel or anti-parallel direction.
Many globular proteins contain combinations of α-helix and β-pleated sheet secondary structure, these patterns are called supersecondary structures also called motifs.
The three dimensional arrangement of protein structure is referred to as tertiary structure.
It is a compact structure with hydrophobic side chains held interior while the hydrophilic groups are on the surface.
This type of arrangement provide stability of the molecule.
Besides the H-bongs, disulfide bonds, ionic interactions, hydrophobic interactions also contribute to the tertiary structure.
What's hot (20)
Protein: structure, classification,function and assay methods
Protein: structure, classification,function and assay methods
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...
Similar to Introduction to protein and classification by sohail
Protein metabolism and nitrogen fixation and metabolism
- 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
Protein classification
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
Classification of protein
Proteins are complex organic molecules composed of amino acids linked by peptide bonds. They serve important structural and functional roles in the body. As the document outlines, proteins are classified based on their shape (globular or fibrous) or function, such as enzymes, hormones, structural proteins, transport proteins, and immune proteins. The four levels of protein structure - primary, secondary, tertiary, and quaternary - determine a protein's 3D structure. Proteins perform vital roles like muscle contraction, oxygen transport, preventing blood loss, and participating in metabolic reactions as enzymes. They are essential biomolecules that make up tissues and carry out important functions in the body.
Proteins by anjali kotwal
Proteins are polymers of amino acids bonded by peptide linkages. They can be classified based on their chemical composition into simple proteins and conjugated proteins, or based on their molecular shape into fibrous proteins and globular proteins. Proteins have a complex structure that can be studied at four levels - primary, secondary, tertiary, and quaternary structure. Proteins are important biomolecules that serve essential functions in the body such as catalyzing biochemical reactions as enzymes and regulating metabolic processes as hormones.
PROTEIN.pptx
Proteins are composed of amino acids and play many essential roles in biology. They exist in primary, secondary, tertiary, and quaternary structures. The primary structure is the amino acid sequence, and secondary structures include alpha helices and beta sheets formed by hydrogen bonding. Tertiary structure involves further folding stabilized by various bonds. Quaternary structure refers to the arrangement of subunits in some proteins. Proteins are classified by their composition, function, shape, and nature. They function as enzymes, hormones, antibodies, and structural components, and are essential for all living processes.
Biological roles of proteins
Proteins play very significant role in cell functioning. they are known as workhorse of cell. they are made up of amino acids.
Proteins
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.
Protein bph
Proteins are organic macromolecules made of amino acids linked by peptide bonds. They range widely in size and function. The fundamental units are 20 different amino acids that make up the primary structure in different sequences. Secondary structures like alpha helices and beta sheets form due to hydrogen bonding of amino acid R groups. Tertiary and quaternary structures arise from further folding and interactions between polypeptide subunits. Proteins have important roles like enzymatic catalysis, transport, structure, regulation and defense. They are classified based on solubility and presence of non-protein groups.
Protein and its classification
This document discusses protein classification and structure. It begins by defining proteins and noting that there are 22 standard amino acids that make up all proteins. Proteins are then classified based on their shape into globular, fibrous, and intermediate proteins. Globular proteins are more compact and spherical while fibrous proteins are long strands used for structure. The document also discusses protein structure at the primary, secondary, tertiary, and quaternary levels. Primary structure is the amino acid sequence, secondary involves coiling into alpha helices or beta sheets, tertiary is the protein's 3D shape from folding, and quaternary involves interactions of multiple protein subunits. Common structural proteins like collagen and keratin are also mentioned.
Quaternary structure of protein
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.
Proteins & amino acids (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as being formed from amino acids, which are the monomers or building blocks of proteins. The document then covers the structure of amino acids, including their general formula and configurations. It also discusses the properties of amino acids in aqueous solutions and their classification as essential or non-essential. The document goes on to explain how amino acids can bond together to form peptides and polypeptides, and the levels of protein structure from primary to quaternary. It concludes with sections on the metabolism of proteins and amino acids in the body.
Proteins final
Proteins are composed of amino acids linked together by peptide bonds. They are essential to biological structure and function. Proteins can be classified as simple, conjugated, or derived based on their structure and components. The primary structure of a protein refers to the sequence of its amino acids, while secondary structure describes amino acid conformation into alpha helices or beta sheets. Tertiary structure describes the three-dimensional folding of polypeptide chains, and quaternary structure involves the aggregation of multiple polypeptide chains.
Protein & amino acid (ulivina pratini)
This document discusses amino acids and proteins. It begins by defining proteins as polymers of amino acids and describing the basic structure of amino acids. It then covers the different configurations of amino acids, their properties in aqueous solutions, and classifications. The document also discusses the structures of peptides and proteins at the primary, secondary, tertiary, and quaternary levels. It describes the digestion and metabolism of amino acids as well as the urea cycle. Finally, it provides an overview of protein biosynthesis, including the roles of DNA, mRNA, tRNA, and ribosomes.
Protein biochemistry
The document discusses the structure and classification of proteins. It notes that proteins are composed of chains of amino acids and can be classified based on chain length. There are four levels of protein structure: primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Secondary structure involves twisting of the chain into alpha helices or beta sheets. Tertiary structure describes the three-dimensional folding, and quaternary structure refers to the arrangement of multiple folded chains. Proteins play diverse roles in organisms, including enzymatic catalysis, oxygen transport, structure, and defense.
Protiens and polypeptides.pptx
The document discusses proteins and polypeptides. It defines proteins as polymers of amino acids that perform important structural and functional roles in the body. Proteins are classified based on shape, constitution and nature. Polypeptides are continuous chains of amino acids joined by peptide bonds. They are precursors to proteins and are synthesized through a process involving transcription and translation. Common methods for synthesizing polypeptides include Fischer's method which uses protecting groups to join amino acids, and modifications of this method.
Proteins
Proteins are made up of chains of amino acids that fold into complex 3D shapes defined by their sequence. There are 20 types of amino acids that can be combined to form the primary structure of a protein. The sequence determines the unique secondary, tertiary, and sometimes quaternary structures which define a protein's specific function. Proteins perform most of the work in cells and have roles in structure, function, regulation and catalysis. The seven main types of proteins include enzymes, structural proteins, transport proteins and more, each with distinct functions in the body.
Proteins.pdf
Proteins are polypeptide structures made up of one or more extended chains of residues from the amino acid. They provide a wide range of organism tasks, including as DNA replication, molecule transport, metabolic process catalysis, and cell structural support.
The albumins seen in vast quantities in egg whites typically have a distinct 3D structure as a result of bonds that form between the protein’s various amino acids. These bonds are broken by heating, exposing the hydrophobic (water-hating) amino acids that are typically maintained on the inside of the protein 1, 1 comma, 2 end superscript, 2, start superscript. In an effort to escape the water that surrounds them in the egg white, the hydrophobic amino acids will bind to one another, creating a protein network that gives the egg white structure and makes it white and opaque. Ta-da! Protein denaturation, thank you for another wonderful breakfast
AS Biology - Proteins
Proteins are made up of amino acid monomers that join together via condensation reactions to form polypeptide chains. A protein's primary structure is the sequence of its amino acids, which determines its higher order structures including secondary, tertiary, and possibly quaternary structures. These structures ultimately define a protein's specific 3D shape and functional role in the body, such as structural support, movement, or cellular communication.
Similar to Introduction to protein and classification by sohail (20)
Protein metabolism and nitrogen fixation and metabolism
Protein metabolism and nitrogen fixation and metabolism
Proteins_Energy_____________Metabolism___importance.pdf
Proteins_Energy_____________Metabolism___importance.pdf
Proteins_Energy_____________Metabolism___importance.pdf
Proteins_Energy_____________Metabolism___importance.pdf
More from Quaid-e-Azam University, Islamabad
Blood, Blood Plasma and Blood group systems
Introduction
Blood group systems
ABO Blood Group System
Blood Plasma
Blood cells and cell like bodies
Blood transfusions in ABO blood group system
Mycorrhiza and it's types.Ecto-Mycorrhiza
Mycorrhiza
Types of Mycorrhiza
Ecto-Mycorrhiza
Endo-Mycorrhiza
EctendoMycorrhiza
Arbuscular mycorrhizas (AM)
Ericoid mycorrhizas
Arbutoid mycorrhizas
Monotropoid mycorrhizas
Orchidaceous mycorrhizas
Human genome project by M.Sohail Riaz Hashmi
Human Genome Project (HGP)
Main objectives Human Genome Project (HGP)
Goals for the HGP
Medical Implications
Applications of HGP
Timeline of HGP
Technical aspects in HGP
Mapping strategies
Sequencing strategies
. Shotgun sequencing method
Sanger sequencing method
Outcomes of HGP
Active and passive transport by M.Sohail Riaz Hashmi
This document provides an overview of active and passive transport mechanisms in cells. It defines active transport as movement against a concentration gradient requiring energy, and defines types of active transport including primary and secondary. It then discusses endocytosis and exocytosis, the processes by which cells take in and release substances. It also defines different types of passive transport including diffusion, osmosis, and facilitated diffusion, and provides examples of each.
Envoirnment by M.Sohail Riaz
Environment
Natural Environment
Why we need Environment?
Types of Environment
Components of Environment
Types of Components of Environment
Factors responsible for change in Environment
Effect of insecticides on environment
Effect of fungicides on environment
Effect of herbicides on environment
The Earth Is Getting Warmer
Sea Levels Are Rising
The Ocean Is Acidifying
What is Environmental Management?
Characteristics of Environmental Management
Significance of Environmental Management
General Scheme for Environmental Management
Approaches of environmental management
Elements of EMS
Workflow of EMS
ISO 140001
Components of ISO 140001
Application of bio informatics by sohail
The document discusses various applications of bioinformatics including developing insect and drought resistant crop varieties, improving crop nutrition, studying microbes that use carbon dioxide and generate energy from light, identifying genes for crop improvement, veterinary and evolutionary studies, waste cleanup, gene therapy, forensic analysis, antibiotic resistance, drug development, preventative medicine, and biotechnology applications. Genome sequencing is enabling researchers to better understand disease mechanisms and identify new drug targets.
Water cycle and Carbon cycle by sohail
Water cycle stages:
Evaporation
Transpiration
Condensation
Precipitation
Runoff
Infiltration
Accumulation
Carbon cycle stages:
Photosynthesis
Decomposition, Animal & Plant respiration, Soil micro-organisms respiration
Partly decomposed plant remains (Coal)
Marine Plankton remains
Effect and applications of different mineral nutrients on plants by Sohail
Effect and applications of different mineral nutrients on plants by SohailQuaid-e-Azam University, Islamabad
Mineral Nutrition
Mineral Nutrition importance
Classification Of Minerals
Essential Elements
Classification of minerals
Role, Properties and Deficiency symptoms of MineralsBarriers in evolution by Sohail
Evolution
Types of evolution
Biological Species Concept
Other Species Definitions
Barriers in Evolution
Reproductive Isolation
Reproductive Isolation’s types
Prezygotic Reproductive Isolating Barriers
Ecological isolation
Ecological isolation’s types
Postzygotic Reproductive Isolating Barriers
Speciation
Types of Speciation
How Does Speciation Occur?
Evolutionary tendencies in Monera by sohail
The document summarizes key evolutionary tendencies in the kingdom Monera. It describes Monera as the oldest and simplest living organisms, including bacteria and cyanobacteria. Bacteria first evolved approximately 3.2-3.5 billion years ago, as evidenced by gene sequencing and ancient microfossils. Cyanobacteria were among the first organisms to evolve oxygenic photosynthesis approximately 2.45 billion years ago, introducing oxygen into the atmosphere. Actinomycetes are a group of bacteria that share characteristics with fungi and play an important role in decomposing organic materials in soil.
Phloem plant physiology by sohail
The document discusses the transport of organic nutrients through the phloem tissue in plants. It describes how photosynthesis produces sugars in source tissues like leaves, which are then actively loaded into the sieve tube elements and companion cells of the phloem. This loading creates pressure that pushes the phloem sap from sources to sinks, where the sugars are unloaded to support growth and storage. Key components of the phloem discussed include sieve plates, sieve-tube members, companion cells and the pressure-flow hypothesis to explain long-distance translocation of nutrients from sources to sinks throughout the plant.
Pit presentation by sohail
pits
pit pair
pit structure
types of pits
Simple pits
Bordered pits
Half bordered pits
Blind pits
Compound pits
Vestured pits
Difference between simple and bordered pits
Combinations in bordered pits
Similarities Between Pits and Plasmodesmata
Bio statistics-Sampling techniques, Probability Sampling, Non-Probability Sam...
Bio statistics-Sampling techniques, Probability Sampling, Non-Probability Sam...Quaid-e-Azam University, Islamabad
Basic Terminologies
Population
Sample and Sampling
Advantages & Disadvantages of Sampling
Probability Sampling
Types of Probability sampling
Non-Probability Sampling
Types of Non-probability sampling
Industrial and biotechnological application of fungi by sohail riaz
Industrial and biotechnological application of fungi by sohail riazQuaid-e-Azam University, Islamabad
This document discusses various ways that fungi are used commercially. It describes how certain fungi can produce useful steroids, antibiotics, enzymes, vitamins, and organic acids. It also lists the top mushrooms produced worldwide by tonnage and discusses fungi that can break down substances like cellulose, kerosene, and starch. Finally, it mentions several fungal biopesticides and the pests they target.Ustilago tritici by sohail mycology
Ustilago tritici, or loose smut of wheat, is a seed-borne fungal disease that causes heavy damage to wheat. The fungus infects wheat seeds and replaces the inflorescence with powdery black spores. It has a monokaryotic and dikaryotic stage in its life cycle. Control methods include rogueing infected plants, hot water treatment of seeds, growing resistant varieties, and using fungicide seed treatments.
Zygomycota by sohail
Introduction
Class Zygomycetes
General characters of Zygomycetes
Order Mucorales
Order Entomophthorales
Order Zoopagales
Life cycle of zygomycetes in Rhizopus stolonifer
Basidiomycota by sohail
Introduction
Salient features
Characteristics
Classification
Somatic structures
Basidium
Asexual reproduction in basidiomycetes
Basidiocarp
Bio molecules by sohail
This document summarizes the four major classes of biomolecules: carbohydrates, proteins, lipids, and nucleic acids. Carbohydrates include sugars and perform structural and energy storage roles. Proteins function as enzymes, provide structure, and transport materials. Lipids store energy and form cell membranes. Nucleic acids like DNA and RNA contain the genetic code and are made of nucleotides linked in chains. Overall, biomolecules are essential organic compounds that perform critical functions in living organisms.
Introduction to protein and classification by sohail
Introduction to protein and classification
Introduction
Protein structure
Classification based on shape
Classification based on functions
More from Quaid-e-Azam University, Islamabad (20)
Active and passive transport by M.Sohail Riaz Hashmi
Active and passive transport by M.Sohail Riaz Hashmi
Effect and applications of different mineral nutrients on plants by Sohail
Effect and applications of different mineral nutrients on plants by Sohail
Bio statistics-Sampling techniques, Probability Sampling, Non-Probability Sam...
Bio statistics-Sampling techniques, Probability Sampling, Non-Probability Sam...
Industrial and biotechnological application of fungi by sohail riaz
Industrial and biotechnological application of fungi by sohail riaz
Introduction to protein and classification by sohail
Introduction to protein and classification by sohail
Recently uploaded
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Current descriptions of immersive learning cases are often difficult or impossible to compare. This is due to a myriad of different options on what details to include, which aspects are relevant, and on the descriptive approaches employed. Also, these aspects often combine very specific details with more general guidelines or indicate intents and rationales without clarifying their implementation. In this paper we provide a method to describe immersive learning cases that is structured to enable comparisons, yet flexible enough to allow researchers and practitioners to decide which aspects to include. This method leverages a taxonomy that classifies educational aspects at three levels (uses, practices, and strategies) and then utilizes two frameworks, the Immersive Learning Brain and the Immersion Cube, to enable a structured description and interpretation of immersive learning cases. The method is then demonstrated on a published immersive learning case on training for wind turbine maintenance using virtual reality. Applying the method results in a structured artifact, the Immersive Learning Case Sheet, that tags the case with its proximal uses, practices, and strategies, and refines the free text case description to ensure that matching details are included. This contribution is thus a case description method in support of future comparative research of immersive learning cases. We then discuss how the resulting description and interpretation can be leveraged to change immersion learning cases, by enriching them (considering low-effort changes or additions) or innovating (exploring more challenging avenues of transformation). The method holds significant promise to support better-grounded research in immersive learning.
Authoring a personal GPT for your research and practice: How we created the Q...
Thematic analysis in qualitative research is a time-consuming and systematic task, typically done using teams. Team members must ground their activities on common understandings of the major concepts underlying the thematic analysis, and define criteria for its development. However, conceptual misunderstandings, equivocations, and lack of adherence to criteria are challenges to the quality and speed of this process. Given the distributed and uncertain nature of this process, we wondered if the tasks in thematic analysis could be supported by readily available artificial intelligence chatbots. Our early efforts point to potential benefits: not just saving time in the coding process but better adherence to criteria and grounding, by increasing triangulation between humans and artificial intelligence. This tutorial will provide a description and demonstration of the process we followed, as two academic researchers, to develop a custom ChatGPT to assist with qualitative coding in the thematic data analysis process of immersive learning accounts in a survey of the academic literature: QUAL-E Immersive Learning Thematic Analysis Helper. In the hands-on time, participants will try out QUAL-E and develop their ideas for their own qualitative coding ChatGPT. Participants that have the paid ChatGPT Plus subscription can create a draft of their assistants. The organizers will provide course materials and slide deck that participants will be able to utilize to continue development of their custom GPT. The paid subscription to ChatGPT Plus is not required to participate in this workshop, just for trying out personal GPTs during it.
Compexometric titration/Chelatorphy titration/chelating titration
Classification
Metal ion ion indicators
Masking and demasking reagents
Estimation of Magnisium sulphate
Calcium gluconate
Complexometric Titration/ chelatometry titration/chelating titration, introduction, Types-
1.Direct Titration
2.Back Titration
3.Replacement Titration
4.Indirect Titration
Masking agent, Demasking agents
formation of complex
comparition between masking and demasking agents,
Indicators/Metal ion indicators/ Metallochromic indicators/pM indicators,
Visual Technique,PM indicators (metallochromic), Indicators of pH, Redox Indicators
Instrumental Techniques-Photometry
Potentiometry
Miscellaneous methods.
Complex titration with EDTA.
8.Isolation of pure cultures and preservation of cultures.pdf
Isolation of pure culture, its various method.
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...Abdul Wali Khan University Mardan,kP,Pakistan
hematic appreciation test is a psychological assessment tool used to measure an individual's appreciation and understanding of specific themes or topics. This test helps to evaluate an individual's ability to connect different ideas and concepts within a given theme, as well as their overall comprehension and interpretation skills. The results of the test can provide valuable insights into an individual's cognitive abilities, creativity, and critical thinking skillsShallowest Oil Discovery of Turkiye.pptx
The Petroleum System of the Çukurova Field - the Shallowest Oil Discovery of Türkiye, Adana
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
The pygmy halfbeak Dermogenys colletei, is known for its viviparous nature, this presents an intriguing case of relatively low fecundity, raising questions about potential compensatory reproductive strategies employed by this species. Our study delves into the examination of fecundity and the Gonadosomatic Index (GSI) in the Pygmy Halfbeak, D. colletei (Meisner, 2001), an intriguing viviparous fish indigenous to Sarawak, Borneo. We hypothesize that the Pygmy halfbeak, D. colletei, may exhibit unique reproductive adaptations to offset its low fecundity, thus enhancing its survival and fitness. To address this, we conducted a comprehensive study utilizing 28 mature female specimens of D. colletei, carefully measuring fecundity and GSI to shed light on the reproductive adaptations of this species. Our findings reveal that D. colletei indeed exhibits low fecundity, with a mean of 16.76 ± 2.01, and a mean GSI of 12.83 ± 1.27, providing crucial insights into the reproductive mechanisms at play in this species. These results underscore the existence of unique reproductive strategies in D. colletei, enabling its adaptation and persistence in Borneo's diverse aquatic ecosystems, and call for further ecological research to elucidate these mechanisms. This study lends to a better understanding of viviparous fish in Borneo and contributes to the broader field of aquatic ecology, enhancing our knowledge of species adaptations to unique ecological challenges.
The debris of the ‘last major merger’ is dynamically young
The Milky Way’s (MW) inner stellar halo contains an [Fe/H]-rich component with highly eccentric orbits, often referred to as the
‘last major merger.’ Hypotheses for the origin of this component include Gaia-Sausage/Enceladus (GSE), where the progenitor
collided with the MW proto-disc 8–11 Gyr ago, and the Virgo Radial Merger (VRM), where the progenitor collided with the
MW disc within the last 3 Gyr. These two scenarios make different predictions about observable structure in local phase space,
because the morphology of debris depends on how long it has had to phase mix. The recently identified phase-space folds in Gaia
DR3 have positive caustic velocities, making them fundamentally different than the phase-mixed chevrons found in simulations
at late times. Roughly 20 per cent of the stars in the prograde local stellar halo are associated with the observed caustics. Based
on a simple phase-mixing model, the observed number of caustics are consistent with a merger that occurred 1–2 Gyr ago.
We also compare the observed phase-space distribution to FIRE-2 Latte simulations of GSE-like mergers, using a quantitative
measurement of phase mixing (2D causticality). The observed local phase-space distribution best matches the simulated data
1–2 Gyr after collision, and certainly not later than 3 Gyr. This is further evidence that the progenitor of the ‘last major merger’
did not collide with the MW proto-disc at early times, as is thought for the GSE, but instead collided with the MW disc within
the last few Gyr, consistent with the body of work surrounding the VRM.
Equivariant neural networks and representation theory
Or: Beyond linear.
Abstract: Equivariant neural networks are neural networks that incorporate symmetries. The nonlinear activation functions in these networks result in interesting nonlinear equivariant maps between simple representations, and motivate the key player of this talk: piecewise linear representation theory.
Disclaimer: No one is perfect, so please mind that there might be mistakes and typos.
dtubbenhauer@gmail.com
Corrected slides: dtubbenhauer.com/talks.html
Bob Reedy - Nitrate in Texas Groundwater.pdf
Presented at June 6-7 Texas Alliance of Groundwater Districts Business Meeting
Immersive Learning That Works: Research Grounding and Paths Forward
We will metaverse into the essence of immersive learning, into its three dimensions and conceptual models. This approach encompasses elements from teaching methodologies to social involvement, through organizational concerns and technologies. Challenging the perception of learning as knowledge transfer, we introduce a 'Uses, Practices & Strategies' model operationalized by the 'Immersive Learning Brain' and ‘Immersion Cube’ frameworks. This approach offers a comprehensive guide through the intricacies of immersive educational experiences and spotlighting research frontiers, along the immersion dimensions of system, narrative, and agency. Our discourse extends to stakeholders beyond the academic sphere, addressing the interests of technologists, instructional designers, and policymakers. We span various contexts, from formal education to organizational transformation to the new horizon of an AI-pervasive society. This keynote aims to unite the iLRN community in a collaborative journey towards a future where immersive learning research and practice coalesce, paving the way for innovative educational research and practice landscapes.
waterlessdyeingtechnolgyusing carbon dioxide chemicalspdf
The technology uses reclaimed CO₂ as the dyeing medium in a closed loop process. When pressurized, CO₂ becomes supercritical (SC-CO₂). In this state CO₂ has a very high solvent power, allowing the dye to dissolve easily.
SAR of Medicinal Chemistry 1st by dk.pdf
In this presentation include the prototype drug SAR on thus or with their examples .
Syllabus of Second Year B. Pharmacy
2019 PATTERN.
The binding of cosmological structures by massless topological defects
Assuming spherical symmetry and weak field, it is shown that if one solves the Poisson equation or the Einstein field
equations sourced by a topological defect, i.e. a singularity of a very specific form, the result is a localized gravitational
field capable of driving flat rotation (i.e. Keplerian circular orbits at a constant speed for all radii) of test masses on a thin
spherical shell without any underlying mass. Moreover, a large-scale structure which exploits this solution by assembling
concentrically a number of such topological defects can establish a flat stellar or galactic rotation curve, and can also deflect
light in the same manner as an equipotential (isothermal) sphere. Thus, the need for dark matter or modified gravity theory is
mitigated, at least in part.
Recently uploaded (20)
aziz sancar nobel prize winner: from mardin to nobel
aziz sancar nobel prize winner: from mardin to nobel
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Describing and Interpreting an Immersive Learning Case with the Immersion Cub...
Authoring a personal GPT for your research and practice: How we created the Q...
Authoring a personal GPT for your research and practice: How we created the Q...
Compexometric titration/Chelatorphy titration/chelating titration
Compexometric titration/Chelatorphy titration/chelating titration
8.Isolation of pure cultures and preservation of cultures.pdf
8.Isolation of pure cultures and preservation of cultures.pdf
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
THEMATIC APPERCEPTION TEST(TAT) cognitive abilities, creativity, and critic...
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...
The debris of the ‘last major merger’ is dynamically young
The debris of the ‘last major merger’ is dynamically young
Equivariant neural networks and representation theory
Equivariant neural networks and representation theory
Basics of crystallography, crystal systems, classes and different forms
Basics of crystallography, crystal systems, classes and different forms
Immersive Learning That Works: Research Grounding and Paths Forward
Immersive Learning That Works: Research Grounding and Paths Forward
waterlessdyeingtechnolgyusing carbon dioxide chemicalspdf
waterlessdyeingtechnolgyusing carbon dioxide chemicalspdf
The binding of cosmological structures by massless topological defects
The binding of cosmological structures by massless topological defects
Introduction to protein and classification by sohail
- 2. Presented by: M.Sohail Riaz Presented to: Ma’am Anum
- 3. Table of contents Introduction Protein structure Classification based on shape Classification based on functions
- 4. Introduction Protein name is derived form a Greek word PROTOS which means “the first or the supreme. Protein are extremely complicated and nitrogenous molecule made up of variable number of amino acid residue joined to each other by a specific covalent bond called peptide bond. 20 amino acid which have been found to occur in all proteins, known as standard amino acid
- 5. Continue… Amino acids are the building blocks of protein Amino acids are linked by peptide bonds A polypeptide is a polymer of amino acid Polypeptide range in length from a few to more than a thousand monomers
- 6. Protein structure There are 4 structure of protein: 1. Primary structure 2. Secondary structure 3. Tertiary structure 4. Quaternary structure
- 7. Primary structure The sequence of amino acids in a protein, is like the order of letters in a long word Linear, ordered and 1 dimensional Written from amino end to carboxyl end that is N to C
- 8. Secondary structure The folding of polypeptide chain into specific coiled structure held together by H-bond Alpha-helix Beta-pleated sheets
- 9. Tertiary structure The tertiary structure mean the overall conformation of a polypeptide. Myoglobin chain is when fully extended its length is 20 time than is width. X-rays diffraction show that its structure is just like a foot ball i.e. globular. The globular structure is due to folding and refolding
- 10. Quaternary structure Structure form when two or more polypeptides chains form one macro-molecule For example Collagen
- 11. Classification based on shape The protein are classify into two type of protein: 1. Globular protein 2. Fibrous protein
- 12. Globular protein Spheroid or ovoid in shape. Enzyme are mostly globular in shape. Subdivided into two type of protein: 1. Albumins: Water soluble. 2. Globulin: Soluble in dilute salt solution
- 13. Fibrous Protein Long thread like molecule. Their helical strands mainly form fibers. These protein are insoluble in water. Form structure of the tissue Present where support is required. Example: Collagen, Elastin, Keratin
- 14. Classification based upon Function Catalytic Protein: These are enzyme which may be simple or conjugated. 1. Alkaline phosphatase 2. Alanine transaminase Hormonal protein: Many protein and peptide acts as Hormone. 1. Insulin 2. Growth Hormone
- 15. Continue…. Structural Protein: Contribute to the structure of the tissue. 1. Collagen 2. Elastin Transport Protein: Serve to carry substances. 1. Transferrin carry Iron 2. Hemoglobin carry Oxygen
- 16. Continue… Immune Protein: Serve in defense mechanism 1. Immunoglobulin Contractile Protein: Takes part in the muscle contraction. 1. Actin 2. Myosin
- 17. Continue… Genetic Protein: Protein present in combination with nucleic acid. 1. Histone Protein Storage Protein: To store protein for nutritional purposes. 1. Casein in Milk 2. Gliadin in Wheat
- 18. Thank you