This document discusses the classification and properties of amino acids. It describes 20 standard amino acids that are classified based on their side chains into groups containing aliphatic, hydroxyl, sulfur, acidic, basic, aromatic, and imino side chains. Amino acids are also classified based on their hydrophobicity/hydrophilicity, nutritional requirements, and fate of their carbon skeletons. Key properties of amino acids include forming zwitterions and peptide bonds between amino acids in protein primary structure. The document outlines secondary structure elements like alpha helices and beta sheets that are stabilized by hydrogen bonds and other interactions.
This presentation the chemical structure of natural amino acids. It also classifies amino acids according to several criteria e.g., structure (aliphatic, aromatic, and heterocyclic amino acids), reaction (Neutral, acidic and basic amino acids), polarity (polar and nonpolar amino acids), and metabolic fate ( glucogenic, ketogenic and glucoketogenic amino acids)
Proteins are made up of amino acids and have a variety of important functions in the body. There are two main types of proteins: globular proteins and fibrous proteins. Globular proteins are spherical and consist of multiple lobes, while fibrous proteins have a linear structure and form strong fibers. Common globular proteins include enzymes, hormones, and transport proteins, whereas collagen and keratin are examples of fibrous proteins that provide structure and support. The structure of a protein determines its specific roles and functions.
1. Nucleic acids and proteins are macromolecules that are essential to life. Nucleic acids store and transmit genetic information, while proteins are composed of amino acids and perform important functions.
2. There are 20 common amino acids that are the building blocks of proteins. Amino acids contain an amino group and a carboxyl group, and can be classified based on the properties of their side chains as nonpolar, polar but uncharged, positively charged, or negatively charged.
3. Important chemical reactions of amino acids include salt formation, ester formation, and decarboxylation of their carboxyl group as well as reactions of their amino group like the ninhydrin reaction.
The document discusses protein structure and function. It describes the basic building blocks of proteins, amino acids, and how they combine to form the primary structure. It then explains how the primary structure can take on regular patterns called secondary structures, including alpha helices and beta sheets. Alpha helices form coiled structures stabilized by hydrogen bonds between amino acids, while beta sheets involve hydrogen bonding between peptide chains to form extended structures. The precise sequence and folding of a protein's amino acids determines its final three-dimensional shape and function.
proteins: structure ,types and purification techniques CHIRANTANMONDAL2
This document provides information on proteins including their structure, types, and purification techniques. It begins with definitions of proteins and amino acids. It then describes the primary, secondary, tertiary, and quaternary levels of protein structure. The document outlines different classifications of amino acids and discusses essential aspects. Finally, it details several common protein purification techniques such as ammonium sulfate precipitation, dialysis, gel filtration chromatography, ion exchange chromatography, and affinity chromatography.
Lecture 1 - General Properties of Amino Acids(2) (1).pdfKundaBwalya1
General Properties of Amino Acids- Biochemistry
Proteins
Proteins serve as basic structural molecules of all cells and tissues of living
organisms. Proteins make up nearly 17% of the total body weight. There are
90-140 million molecules of proteins per one yeast cell; or up to 1010
proteins per one mammalian cell.
To understand role and function of a protein, it is important to know its basic
structure and composition.
Amino acids
Amino acids are fundamental building blocks of proteins. Long linear chains
of amino acids, called polypeptides, make up proteins and determine their
structure, properties and functions. Amino acids are built of the following
elements: carbon, hydrogen, oxygen, nitrogen, and sometimes, sulfur.
Amino acids
The general structure of amino acids consists of a carbon centre
termed an -carbon atom and four substituents linked to this atom,
which are: one amino group (NH2 → NH3
+
), one carboxyl group
(COOH → COO−
), a hydrogen atom (H), and a fourth group, referred
to as the R-group or side radical, that determines the structural
identity and chemical properties of individual amino acids.
The first three groups are common to all amino acids. The basic
amino acid structure is R-CH(NH2
)-COOH or NH3
+
-RCH-COO−
(both
variants are correct)
Properties of amino acids
5
➢ All amino acids share several common chemical properties
because all of possessing the following functional groups:
• One alpha-amino group;
• One alpha-carboxyl group;
➢ Several common properties can be explained by the presence of
both these radicals, alpha-amino group and alpha-carboxyl group,
attached to the same carbon atom.
➢ Side radicals of amino acids bear other functional groups (aliphatic
chains, aromatic rings, hydroxyl groups and additional amino and
carboxyl groups), which are specific for every amino acid.
Side radicals determine the individual properties of amino acids.
You have to be able to tell difference between common and individual
properties of amino acids and be able to explain these properties by the
presence of functional groups responsible for these properties.
Properties of amino acids
7
Properties of amino acids due to carboxyl group
◼ Decarboxylation. Amino acids may undergo alpha
decarboxylation to form the corresponding amines. This is a
natural pathway of biosynthesis of many important amines
produced from amino acids in living organisms:
➢ Histidine → Histamine + CO2
(local immune response);
➢ Tyrosine → Tyramine + CO2
(role in blood-brain barrier);
➢ Tryptophan → Tryptamine + CO2
(neurotransmitter);
➢ Glutamic acid → g-amino butyric acid (GABA) + CO2
(neurotransmitter);
➢ Lysine → Cadaverine + CO2
(toxin – is created spontaneously in
dead bodies. In contrast to other reactions shown above,
cadaverine formation is not controlled by any enzymes, whereas all
other reactions shown above are catalyzed by specific enzymes)
Properties of amino acids
12
Properties due to amino group + carboxyl group
◼ Zwitterions. The name zwitter
All proteins are composed of the same set of 20 amino acids that are linked together via peptide bonds. There are two main categories of amino acids - nonpolar amino acids that cluster in the interior of proteins, and polar amino acids that are charged or contain functional groups that allow hydrogen bonding. Key properties of amino acids include their ionization states, which depend on pH, and their ability to participate in covalent bonds like disulfide bridges that help determine protein structure. Amino acid sequences ultimately define the diverse functions that proteins perform in biological processes.
This presentation the chemical structure of natural amino acids. It also classifies amino acids according to several criteria e.g., structure (aliphatic, aromatic, and heterocyclic amino acids), reaction (Neutral, acidic and basic amino acids), polarity (polar and nonpolar amino acids), and metabolic fate ( glucogenic, ketogenic and glucoketogenic amino acids)
Proteins are made up of amino acids and have a variety of important functions in the body. There are two main types of proteins: globular proteins and fibrous proteins. Globular proteins are spherical and consist of multiple lobes, while fibrous proteins have a linear structure and form strong fibers. Common globular proteins include enzymes, hormones, and transport proteins, whereas collagen and keratin are examples of fibrous proteins that provide structure and support. The structure of a protein determines its specific roles and functions.
1. Nucleic acids and proteins are macromolecules that are essential to life. Nucleic acids store and transmit genetic information, while proteins are composed of amino acids and perform important functions.
2. There are 20 common amino acids that are the building blocks of proteins. Amino acids contain an amino group and a carboxyl group, and can be classified based on the properties of their side chains as nonpolar, polar but uncharged, positively charged, or negatively charged.
3. Important chemical reactions of amino acids include salt formation, ester formation, and decarboxylation of their carboxyl group as well as reactions of their amino group like the ninhydrin reaction.
The document discusses protein structure and function. It describes the basic building blocks of proteins, amino acids, and how they combine to form the primary structure. It then explains how the primary structure can take on regular patterns called secondary structures, including alpha helices and beta sheets. Alpha helices form coiled structures stabilized by hydrogen bonds between amino acids, while beta sheets involve hydrogen bonding between peptide chains to form extended structures. The precise sequence and folding of a protein's amino acids determines its final three-dimensional shape and function.
proteins: structure ,types and purification techniques CHIRANTANMONDAL2
This document provides information on proteins including their structure, types, and purification techniques. It begins with definitions of proteins and amino acids. It then describes the primary, secondary, tertiary, and quaternary levels of protein structure. The document outlines different classifications of amino acids and discusses essential aspects. Finally, it details several common protein purification techniques such as ammonium sulfate precipitation, dialysis, gel filtration chromatography, ion exchange chromatography, and affinity chromatography.
Lecture 1 - General Properties of Amino Acids(2) (1).pdfKundaBwalya1
General Properties of Amino Acids- Biochemistry
Proteins
Proteins serve as basic structural molecules of all cells and tissues of living
organisms. Proteins make up nearly 17% of the total body weight. There are
90-140 million molecules of proteins per one yeast cell; or up to 1010
proteins per one mammalian cell.
To understand role and function of a protein, it is important to know its basic
structure and composition.
Amino acids
Amino acids are fundamental building blocks of proteins. Long linear chains
of amino acids, called polypeptides, make up proteins and determine their
structure, properties and functions. Amino acids are built of the following
elements: carbon, hydrogen, oxygen, nitrogen, and sometimes, sulfur.
Amino acids
The general structure of amino acids consists of a carbon centre
termed an -carbon atom and four substituents linked to this atom,
which are: one amino group (NH2 → NH3
+
), one carboxyl group
(COOH → COO−
), a hydrogen atom (H), and a fourth group, referred
to as the R-group or side radical, that determines the structural
identity and chemical properties of individual amino acids.
The first three groups are common to all amino acids. The basic
amino acid structure is R-CH(NH2
)-COOH or NH3
+
-RCH-COO−
(both
variants are correct)
Properties of amino acids
5
➢ All amino acids share several common chemical properties
because all of possessing the following functional groups:
• One alpha-amino group;
• One alpha-carboxyl group;
➢ Several common properties can be explained by the presence of
both these radicals, alpha-amino group and alpha-carboxyl group,
attached to the same carbon atom.
➢ Side radicals of amino acids bear other functional groups (aliphatic
chains, aromatic rings, hydroxyl groups and additional amino and
carboxyl groups), which are specific for every amino acid.
Side radicals determine the individual properties of amino acids.
You have to be able to tell difference between common and individual
properties of amino acids and be able to explain these properties by the
presence of functional groups responsible for these properties.
Properties of amino acids
7
Properties of amino acids due to carboxyl group
◼ Decarboxylation. Amino acids may undergo alpha
decarboxylation to form the corresponding amines. This is a
natural pathway of biosynthesis of many important amines
produced from amino acids in living organisms:
➢ Histidine → Histamine + CO2
(local immune response);
➢ Tyrosine → Tyramine + CO2
(role in blood-brain barrier);
➢ Tryptophan → Tryptamine + CO2
(neurotransmitter);
➢ Glutamic acid → g-amino butyric acid (GABA) + CO2
(neurotransmitter);
➢ Lysine → Cadaverine + CO2
(toxin – is created spontaneously in
dead bodies. In contrast to other reactions shown above,
cadaverine formation is not controlled by any enzymes, whereas all
other reactions shown above are catalyzed by specific enzymes)
Properties of amino acids
12
Properties due to amino group + carboxyl group
◼ Zwitterions. The name zwitter
All proteins are composed of the same set of 20 amino acids that are linked together via peptide bonds. There are two main categories of amino acids - nonpolar amino acids that cluster in the interior of proteins, and polar amino acids that are charged or contain functional groups that allow hydrogen bonding. Key properties of amino acids include their ionization states, which depend on pH, and their ability to participate in covalent bonds like disulfide bridges that help determine protein structure. Amino acid sequences ultimately define the diverse functions that proteins perform in biological processes.
This document provides information on amino acids and proteins. It discusses the basic properties and characteristics of amino acids, including their structures, classifications, stereochemistry, and reactions. It also covers how amino acids join together through peptide bonds to form polypeptides and proteins. The document discusses various protein structures like primary, secondary, tertiary and quaternary structure. It provides examples of specific proteins like myoglobin, hemoglobin and collagen. Various techniques for analyzing and separating proteins are also summarized, including chromatography and electrophoresis.
This was a report regarding amino acids and peptides that was prepared by our group and this report made in order to make a score. Hope this slide makes more it to be on help.
Food proteins can be obtained from both animal and plant sources. The document discusses the physicochemical properties of proteins including their amino acid composition, classification, ionization behavior, and structure. It also covers the various levels of protein structure from primary to quaternary. The main sources of protein discussed include soybean products, cottonseed flour, mycoprotein, leaf protein concentrate, and microbial biomass protein.
- Amino acids exist in two forms, L and D, depending on their stereoisomer configuration. Only L-amino acids are used in protein synthesis.
- Amino acids are amphoteric, meaning they can act as acids or bases depending on the pH. At low pH they are protonated and at high pH they are deprotonated.
- In solution, amino acids exist as zwitterions - molecules with both positive and negative charges that cancel out to have no overall charge. The isoelectric point is the pH at which the zwitterion form dominates.
Amino acids are the building blocks of proteins and peptides. They contain non-polar, polar, and charged R groups. Peptides are formed through condensation reactions between amino acids, linking them through peptide bonds. There are four levels of protein structure - primary, secondary, tertiary, and quaternary. The secondary structure involves folding into alpha helices or beta sheets. The alpha helix is stabilized by hydrogen bonds between residues four places apart in the sequence. Tertiary structure describes the three-dimensional folding of the polypeptide chain. Quaternary structure involves the interaction of multiple polypeptide chains in a protein.
This document provides an overview of protein structure. It discusses the primary structure as the linear sequence of amino acids joined by peptide bonds. It describes secondary structure as the regular folding of polypeptide chains into alpha helices or beta pleated sheets. Alpha helices form when the carbonyl oxygen of each amino acid hydrogen bonds to the amino hydrogen of the amino acid four positions away in the sequence. Beta pleated sheets consist of beta strands connected laterally by hydrogen bonds between backbone groups. Tertiary structure involves the folding of secondary structure elements into a compact 3D structure. Quaternary structure refers to the assembly of multiple polypeptide chains into a single functional unit.
The document discusses various methods for synthesizing amino acids, including the Strecker synthesis and Gabriel phthalimide synthesis. It then covers topics related to the properties of amino acids such as their dipolar nature, reactions that support this nature, and electrophoresis. The document concludes by discussing peptide bond formation and the four levels of protein structure: primary, secondary, tertiary, and quaternary.
The document discusses the key biomolecules found in living things including proteins, carbohydrates, lipids, and nucleic acids. It describes the basic monomers like amino acids and nucleotides that make up these biomolecules, and how they are linked together through peptide bonds in proteins or phosphodiester bonds in nucleic acids. It also provides examples of specific biomolecules like collagen, hemoglobin, and fatty acids to illustrate their structures and functions.
Proteins are composed of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Common secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Globular proteins fold such that hydrophobic residues are buried inside and hydrophilic residues face outward, while fibrous proteins form insoluble fibers.
General structure of amino acid
Specific learning objective (SLO): Amino acid as Ampholytes (acid and base), Zwitter ions.
Classification of amino acid on the basis of side chain, chemical composition, Nutritional Requirement and metabolic fate.
Derived amino acids.
Optical properties of amino acids.
Acid-Base properties and Buffer characteristic.
Biological Important Peptides
Proteins based on nutritional value
The document summarizes key aspects of amino acids and protein structure in 3 paragraphs or less:
Amino acids are the building blocks of proteins. They contain common structural features and exist in L- and D-forms. In proteins, amino acids are exclusively in the L-conformation. Amino acids are classified based on the properties of their side chains into nonpolar, aromatic, polar, positively charged, and negatively charged categories.
Protein structure is hierarchical, progressing from primary to secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence. Secondary structures include alpha helices, beta sheets, and turns formed by hydrogen bonding. Tertiary structure refers to the overall 3
biochemistry-secondary structure of proteinsroyabasser
The document discusses the secondary structure of proteins, focusing on alpha helices. It defines secondary structure as the local dimensional segments of a protein's primary structure that are folded due to chemical interactions. The main type of secondary structure discussed is the alpha helix, which is a right-handed coil stabilized by hydrogen bonds between amino acids that are 3-4 residues apart. Factors that stabilize or destabilize the alpha helix include amino acid side chains, hydrophobic/hydrophilic interactions, and hydrogen bonding. Proline is highlighted as an alpha helix breaker due to its rigid cyclic side chain.
Amino acids are organic compounds that contain amino and carboxyl groups. They are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids can be classified based on their structure, including whether they are nonpolar, polar, or have other functional groups. The classification determines each amino acid's properties and role in protein structure and function. Some amino acids are essential to obtain through diet, while others can be synthesized in the body. Amino acids have optical activity, acid-base properties, and can absorb ultraviolet light depending on their structure. They generally exist as zwitterions at physiological pH.
Amino acids are the building blocks of proteins. They join together through peptide bonds to form polypeptide chains. There are over 300 amino acids but only 20 are commonly found in mammalian proteins. Amino acids have various roles like forming enzymes, hormones, antibodies and being precursors for other important molecules. They are amphoteric due to possessing both amino and carboxyl groups. Amino acids differ in their physical and chemical properties like color, solubility, isomerism and reactions.
Amino acids are the building blocks of proteins. They join together through peptide bonds to form polypeptide chains. There are over 300 amino acids described in nature but only 20 are commonly found in mammalian proteins. Amino acids have various roles including forming enzymes, hormones, antibodies and being precursors for other important molecules. They are also important for buffering pH changes and participating in metabolic reactions through side chain functional groups.
This document discusses amino acids and their properties. It begins by explaining that amino acids are organic compounds that contain amine and carboxyl groups and have different R groups. Proteins are composed of chains of amino acids linked by peptide bonds. There are 20 standard amino acids that are the building blocks of proteins. The document then classifies amino acids based on their R groups and discusses their structures, chemical properties, and roles in the body.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They have physical properties like solubility and melting points. Amino acids play important roles in many biological functions and reactions due to their amino, carboxyl, and side chain groups. They are essential for protein synthesis, cellular functions, and as precursors for other biomolecules.
This document provides information on amino acids and proteins. It discusses the basic properties and characteristics of amino acids, including their structures, classifications, stereochemistry, and reactions. It also covers how amino acids join together through peptide bonds to form polypeptides and proteins. The document discusses various protein structures like primary, secondary, tertiary and quaternary structure. It provides examples of specific proteins like myoglobin, hemoglobin and collagen. Various techniques for analyzing and separating proteins are also summarized, including chromatography and electrophoresis.
This was a report regarding amino acids and peptides that was prepared by our group and this report made in order to make a score. Hope this slide makes more it to be on help.
Food proteins can be obtained from both animal and plant sources. The document discusses the physicochemical properties of proteins including their amino acid composition, classification, ionization behavior, and structure. It also covers the various levels of protein structure from primary to quaternary. The main sources of protein discussed include soybean products, cottonseed flour, mycoprotein, leaf protein concentrate, and microbial biomass protein.
- Amino acids exist in two forms, L and D, depending on their stereoisomer configuration. Only L-amino acids are used in protein synthesis.
- Amino acids are amphoteric, meaning they can act as acids or bases depending on the pH. At low pH they are protonated and at high pH they are deprotonated.
- In solution, amino acids exist as zwitterions - molecules with both positive and negative charges that cancel out to have no overall charge. The isoelectric point is the pH at which the zwitterion form dominates.
Amino acids are the building blocks of proteins and peptides. They contain non-polar, polar, and charged R groups. Peptides are formed through condensation reactions between amino acids, linking them through peptide bonds. There are four levels of protein structure - primary, secondary, tertiary, and quaternary. The secondary structure involves folding into alpha helices or beta sheets. The alpha helix is stabilized by hydrogen bonds between residues four places apart in the sequence. Tertiary structure describes the three-dimensional folding of the polypeptide chain. Quaternary structure involves the interaction of multiple polypeptide chains in a protein.
This document provides an overview of protein structure. It discusses the primary structure as the linear sequence of amino acids joined by peptide bonds. It describes secondary structure as the regular folding of polypeptide chains into alpha helices or beta pleated sheets. Alpha helices form when the carbonyl oxygen of each amino acid hydrogen bonds to the amino hydrogen of the amino acid four positions away in the sequence. Beta pleated sheets consist of beta strands connected laterally by hydrogen bonds between backbone groups. Tertiary structure involves the folding of secondary structure elements into a compact 3D structure. Quaternary structure refers to the assembly of multiple polypeptide chains into a single functional unit.
The document discusses various methods for synthesizing amino acids, including the Strecker synthesis and Gabriel phthalimide synthesis. It then covers topics related to the properties of amino acids such as their dipolar nature, reactions that support this nature, and electrophoresis. The document concludes by discussing peptide bond formation and the four levels of protein structure: primary, secondary, tertiary, and quaternary.
The document discusses the key biomolecules found in living things including proteins, carbohydrates, lipids, and nucleic acids. It describes the basic monomers like amino acids and nucleotides that make up these biomolecules, and how they are linked together through peptide bonds in proteins or phosphodiester bonds in nucleic acids. It also provides examples of specific biomolecules like collagen, hemoglobin, and fatty acids to illustrate their structures and functions.
Proteins are composed of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. The primary structure is the amino acid sequence. Common secondary structures include alpha helices and beta pleated sheets formed by hydrogen bonding. Tertiary structure describes the overall 3D shape formed by interactions between amino acid side chains. Globular proteins fold such that hydrophobic residues are buried inside and hydrophilic residues face outward, while fibrous proteins form insoluble fibers.
General structure of amino acid
Specific learning objective (SLO): Amino acid as Ampholytes (acid and base), Zwitter ions.
Classification of amino acid on the basis of side chain, chemical composition, Nutritional Requirement and metabolic fate.
Derived amino acids.
Optical properties of amino acids.
Acid-Base properties and Buffer characteristic.
Biological Important Peptides
Proteins based on nutritional value
The document summarizes key aspects of amino acids and protein structure in 3 paragraphs or less:
Amino acids are the building blocks of proteins. They contain common structural features and exist in L- and D-forms. In proteins, amino acids are exclusively in the L-conformation. Amino acids are classified based on the properties of their side chains into nonpolar, aromatic, polar, positively charged, and negatively charged categories.
Protein structure is hierarchical, progressing from primary to secondary, tertiary, and quaternary levels. The primary structure is the amino acid sequence. Secondary structures include alpha helices, beta sheets, and turns formed by hydrogen bonding. Tertiary structure refers to the overall 3
biochemistry-secondary structure of proteinsroyabasser
The document discusses the secondary structure of proteins, focusing on alpha helices. It defines secondary structure as the local dimensional segments of a protein's primary structure that are folded due to chemical interactions. The main type of secondary structure discussed is the alpha helix, which is a right-handed coil stabilized by hydrogen bonds between amino acids that are 3-4 residues apart. Factors that stabilize or destabilize the alpha helix include amino acid side chains, hydrophobic/hydrophilic interactions, and hydrogen bonding. Proline is highlighted as an alpha helix breaker due to its rigid cyclic side chain.
Amino acids are organic compounds that contain amino and carboxyl groups. They are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids can be classified based on their structure, including whether they are nonpolar, polar, or have other functional groups. The classification determines each amino acid's properties and role in protein structure and function. Some amino acids are essential to obtain through diet, while others can be synthesized in the body. Amino acids have optical activity, acid-base properties, and can absorb ultraviolet light depending on their structure. They generally exist as zwitterions at physiological pH.
Amino acids are the building blocks of proteins. They join together through peptide bonds to form polypeptide chains. There are over 300 amino acids but only 20 are commonly found in mammalian proteins. Amino acids have various roles like forming enzymes, hormones, antibodies and being precursors for other important molecules. They are amphoteric due to possessing both amino and carboxyl groups. Amino acids differ in their physical and chemical properties like color, solubility, isomerism and reactions.
Amino acids are the building blocks of proteins. They join together through peptide bonds to form polypeptide chains. There are over 300 amino acids described in nature but only 20 are commonly found in mammalian proteins. Amino acids have various roles including forming enzymes, hormones, antibodies and being precursors for other important molecules. They are also important for buffering pH changes and participating in metabolic reactions through side chain functional groups.
This document discusses amino acids and their properties. It begins by explaining that amino acids are organic compounds that contain amine and carboxyl groups and have different R groups. Proteins are composed of chains of amino acids linked by peptide bonds. There are 20 standard amino acids that are the building blocks of proteins. The document then classifies amino acids based on their R groups and discusses their structures, chemical properties, and roles in the body.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They perform important functions including serving as monomers for protein synthesis, participating in cellular processes, and acting as precursors for other compounds.
Amino acids are organic compounds that contain an amino group, a carboxyl group, a central carbon atom, and a side chain. There are 20 standard amino acids that are the building blocks of proteins. Amino acids can be classified based on their structure, polarity, nutritional requirements, and metabolic fate. They have physical properties like solubility and melting points. Amino acids play important roles in many biological functions and reactions due to their amino, carboxyl, and side chain groups. They are essential for protein synthesis, cellular functions, and as precursors for other biomolecules.
These lecture slides, by Dr Sidra Arshad, offer a simplified look into the mechanisms involved in the regulation of respiration:
Learning objectives:
1. Describe the organisation of respiratory center
2. Describe the nervous control of inspiration and respiratory rhythm
3. Describe the functions of the dorsal and respiratory groups of neurons
4. Describe the influences of the Pneumotaxic and Apneustic centers
5. Explain the role of Hering-Breur inflation reflex in regulation of inspiration
6. Explain the role of central chemoreceptors in regulation of respiration
7. Explain the role of peripheral chemoreceptors in regulation of respiration
8. Explain the regulation of respiration during exercise
9. Integrate the respiratory regulatory mechanisms
10. Describe the Cheyne-Stokes breathing
Study Resources:
1. Chapter 42, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 36, Ganong’s Review of Medical Physiology, 26th edition
3. Chapter 13, Human Physiology by Lauralee Sherwood, 9th edition
Histololgy of Female Reproductive System.pptxAyeshaZaid1
Dive into an in-depth exploration of the histological structure of female reproductive system with this comprehensive lecture. Presented by Dr. Ayesha Irfan, Assistant Professor of Anatomy, this presentation covers the Gross anatomy and functional histology of the female reproductive organs. Ideal for students, educators, and anyone interested in medical science, this lecture provides clear explanations, detailed diagrams, and valuable insights into female reproductive system. Enhance your knowledge and understanding of this essential aspect of human biology.
Hiranandani Hospital in Powai, Mumbai, is a premier healthcare institution that has been serving the community with exceptional medical care since its establishment. As a part of the renowned Hiranandani Group, the hospital is committed to delivering world-class healthcare services across a wide range of specialties, including kidney transplantation. With its state-of-the-art facilities, advanced medical technology, and a team of highly skilled healthcare professionals, Hiranandani Hospital has earned a reputation as a trusted name in the healthcare industry. The hospital's patient-centric approach, coupled with its focus on innovation and excellence, ensures that patients receive the highest standard of care in a compassionate and supportive environment.
Rasamanikya is a excellent preparation in the field of Rasashastra, it is used in various Kushtha Roga, Shwasa, Vicharchika, Bhagandara, Vatarakta, and Phiranga Roga. In this article Preparation& Comparative analytical profile for both Formulationon i.e Rasamanikya prepared by Kushmanda swarasa & Churnodhaka Shodita Haratala. The study aims to provide insights into the comparative efficacy and analytical aspects of these formulations for enhanced therapeutic outcomes.
Osteoporosis - Definition , Evaluation and Management .pdfJim Jacob Roy
Osteoporosis is an increasing cause of morbidity among the elderly.
In this document , a brief outline of osteoporosis is given , including the risk factors of osteoporosis fractures , the indications for testing bone mineral density and the management of osteoporosis
Local Advanced Lung Cancer: Artificial Intelligence, Synergetics, Complex Sys...Oleg Kshivets
Overall life span (LS) was 1671.7±1721.6 days and cumulative 5YS reached 62.4%, 10 years – 50.4%, 20 years – 44.6%. 94 LCP lived more than 5 years without cancer (LS=2958.6±1723.6 days), 22 – more than 10 years (LS=5571±1841.8 days). 67 LCP died because of LC (LS=471.9±344 days). AT significantly improved 5YS (68% vs. 53.7%) (P=0.028 by log-rank test). Cox modeling displayed that 5YS of LCP significantly depended on: N0-N12, T3-4, blood cell circuit, cell ratio factors (ratio between cancer cells-CC and blood cells subpopulations), LC cell dynamics, recalcification time, heparin tolerance, prothrombin index, protein, AT, procedure type (P=0.000-0.031). Neural networks, genetic algorithm selection and bootstrap simulation revealed relationships between 5YS and N0-12 (rank=1), thrombocytes/CC (rank=2), segmented neutrophils/CC (3), eosinophils/CC (4), erythrocytes/CC (5), healthy cells/CC (6), lymphocytes/CC (7), stick neutrophils/CC (8), leucocytes/CC (9), monocytes/CC (10). Correct prediction of 5YS was 100% by neural networks computing (error=0.000; area under ROC curve=1.0).
Our backs are like superheroes, holding us up and helping us move around. But sometimes, even superheroes can get hurt. That’s where slip discs come in.
13. CLASSIFICATION OF AMINO ACIDS BASED ON
THEIR FATE OF CARBON SKELETONS
GLYCOGENIC AND KETOGENIC :
1. PHENYLALANINE
2.TYROSINE
3.TRYPTOPHAN
4. LYSINE
5. ISOLEUCINE
15. PROPERTIES OF AMINO ACIDS
GLYCINE--- SMALLEST
GETS ACCOMODATED IN
OTHERWISE INACCESSIBLE REGIONS OF
PROTEIN STRUCTURE
HYDROPHOBIC AMINO ACIDS GET
ACCOMODATED IN INTERIOR OF CYTOSOLIC
PROTEINS.
CHARGED ‘R’ GROUPS OF POLAR AMINO
ACIDS - FORM SALT BONDS OF PROTEIN
STRUCTURE.
16. PROPERTIES CONTD.
-OH OF SERINE AND -SH OF CYSTEINE
HELP IN ENZYME CATALYSIS.
AMINO ACIDS HELP IN ACID BASE
BALANCE DUE TO THEIR IONIZABLE
WEAK ACIDIC AND BASIC GROUPS.
17. ZWITTERIONS
AMINO ACIDS ARE AMPHOTERIC
MOLECULES --- CONTAIN BOTH POSITIVE &
NEGATIVE CHARGES WHICH ARE AFFECTED
BY THE Ph of THE SURROUNDING MEDIUM.
THEY HAVE AT LEAST 2 IONIZABLE WEAK
ACID GROUPS (PROTON DONORS ) ---COOH
AND ---NH3+ AND THEIR CONJUGATE
BASES ( PROTON ACCEPTORS) -- --COO-
AND NH2.
18. AT PHYSIOLOGICAL Ph BLOOD PLASMA
7.4 CARBOXYL GROUPS MAINLY EXIST
AS CARBOXYLATE IONS R—COO-.
AMINO GROUPS AS R-NH3+.
MOLECULAR SPECIES LIKE THESE WITH
EQUAL NUMBER OF POSITIVEAND
NEGATIVE CHARGESARE CALLED
ZWITTERIONS.
THE Ph at which the molecule exists as
Zwitterion is - Isoelectric pH.
19. PEPTIDE BOND
CONDENSATION REACTION
INVOLVES REMOVAL OF ONE MOL. OF
WATER BETWEEN THE ALPHA AMINO
GROUP OF ONE AMINO ACIDAND ALPHA
CARBOXYL GROUP OF THE SECOND
AMINO ACID.
AMIDE LINKAGE
REQUIRES ENERGY IN THE FORM OF ATP.
20. PEPTIDE BOND
H
NH3+---C—COOH
I H
CH3 + NH2---C---COO-
I
H2O R
H H
NH3+----C---C----NH----C---COO-
I II I
CH3 O R
21. PEPTIDE BOND IS PRESENT IN TRANS
CONFIGURATION
H H
I I
NH3----- C N
1.32 COO-
R C C
R
O H
22. CHARACTERISTICS OF PEPTIDE BOND
ALMOST ALL PEPTIDE BONDS ARE TRANS
IN CONFIGURATION.
THE 2 ALPHA CARBON ATOMS ARE ON
THE OPPOSITE SIDES OF PEPTIDE BOND.
IT IS PLANAR WITH NO FREEDOM OF
ROTATION ABOUT THE BOND THAT
CONNECTS THE C AND N ATOMS.
23. CHARACTERISTICS OF PEPTIDE BOND
THIS SEMIRIGIDITY HAS IMPORTANT
CONSEQUENCES FOR ORDERS OF PROTEIN
STRUCTURE ABOVE THE PRIMARY LEVEL.
PEPTIDE BOND HAS A PARTIAL DOUBLE
BOND CHARACTER.
C—N DISTANCE -- 1-32A
SINGLE BOND --- 1.49A
DOUBLE BOND --- 1.27 A
24. .
PEPTIDE BOND IS UNCHARGED WHICH
ALLOWS POLYMERS OF AMINO ACIDS TO
FORM TIGHTLY PACKED GLOBULAR
STRUCTURES.
25. .
TRIPEPTIDE
CYSTEINE ALANINE GLYCINE
SH
I
CH2 H CH3 H H
I I I I I
NH3---C-----C-----N----C---C----N----C—COO-
I II I II I
H O H O H
31. STRUCTURE OF GLUTATHIONE
SH
I
O CH2 H
II I I
C C N
CH2 N C CH2
I I II I
CH2 H O COO-
I
H-- C—NH3 GAMMA GLUTAMYL CYSTEINYL
I GLYCINE
COO-
32. PRIMARY STRUCTURE OF PROTEIN
Primary Structure of the Polypeptide chain
is the order in which Amino Acids are joined
together and it includes the location of any
Disulfide bonds.
It shows the number, structure and order of
all the amino acid residues in a polypeptide
chain.
33. SECONDARY STRUCTURE
IT IS THE REGULAR , RECURRING
ARRANGEMENTS IN SPACE OF ADJACENT
AMINO ACID RESIDUES IN A
POLYPEPTIDE CHAIN.
34. FORCES/BONDS THAT STABILIZE THE SECONDARY
STRUCTURE OF PROTEIN
1. HYDROGEN BONDS:
- POLAR ‘R’ GROUPS PRESENT ON THE
SURFACE OF PROTEINS FORM HYDROGEN
BONDS WITH WATER MOLECULES.
- AMINOACYL RESIDUES OF THE
BACKBONE FORM HYDROGEN BONDS
WITH ONE ANOTHER.
35. HYDROPHOBIC INTERACTIONS
HYDROPHOBIC INTERACTIONS INVOLVE
NONPOLAR ‘R’ GROUPS OF AMINOACYL
RESIDUES.
IN POLAR SOLUTION LIKE WATER
HYDRPHOBIC ARE CONCENTRATED IN THE
INTERIOR OF THE PROTEIN.
IN NONPOLAR ENVIRONMENT , NONPOLAR
‘R’ GROUPS PARTICIPATE IN HYDROPHOBIC
INTERACTIONS WITH ALKYL SIDE CHAINS OF
FATTY ACYL ESTERS OF MEMBRANE
BILAYERS.
36. ELECTROSTATIC INTERACTIONS
ELECTROSTATIC INTERACTIONS OR SALT
BONDS ARE FORMED BETWEEN OPPOSITELY
CHARGED GROUPS LIKE AMINO TERMINAL
OR CARBOXYL TERMINAL GROUPS OF
PEPTIDES AND THE CHARGED ‘R’ GROUPS
OF POLAR AMINOACYL RESIDUES.
37. VAN DER WAALS INTERACTIONS
Van derWaals forces are weak and act
over extremely short distances and include
both an attractive & repulsive component.
The distance at which the attractive force
is maximal and repulsive force is minimal
is - VAN DERWAALS CONTACT
DISTANCE
38. ALPHA HELIX
BACK BONE OF THE POLYPEPTIDE CHAIN
IS TWISTED ABOUT EACH ALPHA
CARBON ATOM BY EQUAL AMOUNTS TO
FORM A COIL OR HELIX.
THEY ARE EITHER RIGHT OR LEFT
HANDED. RIGHT HANDED MORE
COMMON.
39. .
NUMBER OF RESIDUES PER TURN= 3.6.
AMINOACYL RESIDUES ARE DIRECTED
OUTWARD FROM THE HELIX MINIMIZING
MUTUAL STERIC HINDERANCE.
H- BONDS STABILIZE ALPHA HELIX.
PEPTIDE NITROGENS DONORS OF H.
CARBONYL OXYGEN OF THE 4TH RESIDUE
IN LINE BEHIND HYDROGEN
ACCEPTOR
40. .
TIGHTLY PACKED ATOMS AT THE CORE
OF AN ALPHA HELIX ARE VAN DER
WAALS CONTACT WITH ONE ANOTHER.
ALPHA HELICES SEEN IN:
1. HEMOGLOBIN
2. PLASMA LIPOPROTEINS
3. POLYPEPTIDE HORMONES
43. BETA PLEATED SHEETS
SECOND REGULAR STRUCTURE
DESCRIBED.
ALPHA CARBONS AND THEIR
ASSOCIATED ‘R’ GROUPS ALTERNATE
BETWEEN SLIGHTLY ABOVE AND BELOW
THE MAIN CHAIN OF THE POLYPEPTIDE.
STABILIZED BY MAXIMUM NUMBER OF
HYDROGEN BONDS.
44. .
POLYPEPTIDES ALIGNED ALONGSIDE ONE
ANOTHER ARE STABILIZED BY HYDROGEN
BONDS FORMED BETWEEN PEPTIDE
NITROGEN HYDROGENS AND CARBONYL
OXYGENS OF ADJACENT STRANDS.
UNLIKE THE COMPACT STRUCTURE OF
ALPHA HELIX , PEPTIDE BACKBONES OF
BETA SHEETS ARE FULLY EXTENDED.
THEY ARE PARALLEL OR ANTIPARALLEL.
48. BETA PLEATED SHEETS
FOUND IN BOTH FIBROUS AND
GLOBULAR PROTEINS.
TWISTED BETA PLEATED SHEET FIBRILS
( AMYLOID PROTEIN) ARE DEPOSITED IN
BRAINS OF ALZHEIMER PATIENTS.
49. LOOP REGIONS
LOOP OR COIL CONFORMATIONS ARE
IRREGULARLY ORDERED.
FORM MAJOR SURFACE FEATURES OF
PROTEINS.
EXPOSED TO SOLVENT , RICH IN
CHARGED AND POLAR RESIDUES.
THEY CONNECT ADJACENT
ANTIPARALLEL BETA SHEETS.
50. LOOP REGIONS
THEY FORM SITE FOR LIGAND
INTERACTIONS.
LOOP REGIONS FORM ANTIGEN BINDING
SITES OF ANTIBODIES.
51. BETA TURN OR BETA BEND
THEY CONNECT TWO ADJACENT STRANDS
OF ANTIPARALLEL BETA SHEETS.
CONSIST OF 4 AMINO ACIDS AND MAKE A
180 DEGREE TURN.
FIRST AMINO ACID IS HYDROGEN BONDED
TO FOURTH.
CONTAIN GLYCINE AND PROLINE.
OCCUR PRIMARILY AT PROTEIN SURFACES
52.
53. SUPER SECONDARY MOTIFS
SEEN MOSTLY IN GLOBULAR PROTEINS.
SMALL SUBUNITS OF SECONDARY
STRUCTURAL ELEMENTS.
Eg.
1. BETA –ALPHA –BETA 2 STRANDS OF
BETA SHEET CONNECTED BY AN ALPHA
HELIX.
2. GREEK KEY MOTIF.
56. TERTIARY STRUCTURE
TERTIARY STRUCTURE REFERSTO
SPATIAL RELATIONSHIPS BETWEEN
SECONDARY STRUCTURAL ELEMENTS.
SECONDARY & SUPERSECONDARY
STRUCTURES OF LARGE PROTEINS GET
ORGANIZED AS DOMAINS ( COMPACT
UNITS) CONNECTED BY THE
POLYPEPTIDE BACKBONE.
57. TERTIARY STRUCTURE
PROTEIN FOLDING IN FORMATION OF
TERTIARY STRUCTURE BRINGS
TOGETHER AMINO ACIDS WHICH ARE
FAR APART INTHE PRIMARY STRUCTURE.
DOMAINS PERFORM DISCRETE
FUNCTIONS:
Eg: BINDING SPECIFIC LIGANDS
60. QUARTERNARY
STRUCTURE
PROTEINS WITH 2 OR MORE
POLYPEPTIDE CHAINS ASSOCIATED
BY NON COVALENT FORCES EXHIBIT
QUARTERNARY STRUCTURE.
THESE ARE MULTIMERIC PROTEINS
AND THE INDIVIDUAL POLYPEPTIDE
CHAINS ARE TERMED PROTOMERS
OR SUBUNITS.
ADJACENT SUBUNITS ARE LINKED
BY HYDROGEN BONDS AND
ELECTROSTATIC BONDS.
61. QUARTERNARY
STRUCTURE
2 SUBUNITS DIMERIC
4 SUBUNITS TETRAMERIC etc.
HOMO-OLIGMERIC PROTEINS: IDENTICAL
SUBUNITS
HETERO-OLIGOMERIC PROTEINS:
DISSIMILAR SUBUNITS , EACH
PERFORMING A DIFFERENT FUNCTION.
Eg: ONE SUBUNIT CATALYTIC ROLE
ANOTHER SUBUNIT LIGAND
RECOGNITION OR A REGULATORY
ROLE.
64. DETERMINATION OF PRIMARY STRUCTURE OF PROTEIN
PURIFICATION OF THE PROTEIN
( MANY MOLECULES OF THE SAME PROTEIN ARE TAKEN )
DETERMINE THE NUMBER OF AMINO ACIDS
MULTIMERIC PROTEIN SMALL SINGLE
PEPTIDE ( < 100 AMINO -
( ACIDS)
BREAK INTO ITS SUBUNITS
PUT IN
SEQUENATOR
LARGE PEPTIDES SMALL PEPTIDES WITH EDMAN’S
REAGENT
( > 100 PEPTIDES ) ( < 100 PEPTIDES) TO DETERMINE
SEQUENCE
DIGEST WITH SPECIFIC ENZ. SEQUENCE
TO FORM OVERLAPPING
PEPTIDES
SEQUENCE
65. PURIFICATION OF
PEPTIDES
PRIOR TO DETERMINATION OF
PROTEIN STRUCTURE, PROTEINS
ARE PURIFIED BY :
1. ULTRACENTRIFUGATION
2. POLYACRYLAMIDE GEL
ELECTROPHORESIS.
66. DETERMINATION OF THE NUMBER
OF AMINO ACIDS
1. PEPTIDE BONDS ARE BROKEN
BY
ACID HYDROLYSIS WITH 6N HCL
AT 110DEGREES CENTIGRADE.
2. AMINO ACIDS SEPARATED BY:
3. HPLC OR
4. ION EXCHANGE
CHROMATOGRAPHY.
67. SINGLE SMALL PEPTIDE OF
LESS THAN 100 AMINO ACIDS.
1. PUT IN SEQUENATOR TO DETERMINE
SEQUENCE.
2. SANGER’S REAGENT ( 1-FLOURO 2,4
DINITROBENZENE) OR
3. EDMAN’S REAGENT ( PHENYL
ISOTHIOCYANATE ) CAN BE USED.
BOTH REAGENTS CLEAVE AMINO
ACIDS ONE BY ONE FROM AMINO
TERMINAL END.
68. .
SEPARATED AMINO ACIDS ARE
IDENTIFIED BY
CHROMATOGRAPHY AND BY USING
NINHYDRIN REAGENT.
69. MULTIMERIC PROTEIN
BREAK INTO PEPTIDE CHAINS USING
:
1. UREA HYDROLYSES ‘H’
BONDS
2. GUANIDINE HCL & NONCOVALENT
BONDS
1. REDUCING AGENTS ( BREAK
DISULPHIDE BONDS).
71. BREAKING DOWN OF LARGE PEPTIDES INTO
SMALLER FRAGMENTS SO THAT THEY CAN BE
SEQUENCED.
REAGENTS USED FOR ABOVE
PURPOSE:
1. CYANOGEN BROMIDE: CLEAVES ON
–COOH SIDE OF METHIONINE.
2. TRYPSIN: CLEAVES ON THE –COOH
SIDE OF LYSINE & ARGININE
3. O-IODOSOBENZNENE
4. HYDROXYLAMINE
5. MILD ACID HYDROLYSIS
74. CLASSIFICATION OF
PROTEINS
1. CLASSIFICATION BASED ON
FUNCTION:
A. CATALYTIC PROTEINS,
B. STRUCTURAL PROTEINS - COLLAGEN
C. CONTRACTILE PROTEINS
D. TRANSPORT PROTEINS
E. REGULATORY PROTEINS –
HORMONES
F. PROTECTIVE PROTEINS
80. CLASSIFICATION BASED ON
SHAPE
1. GLOBULAR PROTEINS :
Eg. a. ALBUMIN
b.GLOBULINS
c.HEMOGLOBIN
2. FIBROUS PROTEINS : Eg. COLLAGEN
ELASTIN
FIBRINOGEN
81. CLASSIFICATION BASED ON
NUTRITIONAL VALUE
1. NUTRITIONALLY RICH PROTEINS :
COMPLETE PROTEINS
CONTAIN ALL ESSENTIAL
AMINO ACIDS
EG. CASEIN OF MILK,
EGG ALBUMIN
82. INCOMPLETE PROTEINS
THEY LACK ONE ESSENTIAL AMINO
ACID
Eg. PULSES DEFICIENT IN METHIONINE
CEREALS LACK LYSINE
( MUTUAL SUPPLEMENTATION )
83. POOR PROTEINS
THEY LACK MANY ESSENTIAL
AMINO ACIDS.
Eg. CORN LACKS TRYPTOPHAN
AND LYSINE.
84. STRUCTURE OF
COLLAGEN
COLLAGEN TYPE 1 : SKIN & BONE
TYPE II : CARTILAGE
STRUCTURE:
POLYPEPTIDE CHAINS.
EACH CHAIN IS TWISTED INTO A
LEFT HANDED HELIX OF 3
RESIDUES PER TURN,
85. STRUCTURE OF COLLAGEN:
3 OF THESE ALPHA CHAINS ARE
THEN WOUND INTO A RIGHT
HANDED SUPER HELIX FORMING A
ROD LIKE STRUCTURE 1.4nm IN
DIAMETER & 300nm LONG.
GLYCINE RESIDUES ARE
PRESENT AT EVERY 3RD POSITION
OF THE TRIPLE HELIX.
86. .
THE RECURRING AMINO ACIDS
ARE REPRESENTED AS (GLY-X-Y)n.
X & Y CAN BE ANY OTHER AMINO
ACIDS .
ABOUT (100/1000) OF X POSITIONS
ARE PROLINE
ABOUT ( 100/1000) OF Y
POSITIONS ARE LYSINE.
87. .
COLLAGEN UNDERGOES POST
TRANSLATIONAL MODIFICATION.
HYDROXYLATION OF PROLINE AND
LYSINE RESIDUES , TO CONFER
RIGIDITY ON THE COLLAGEN
MOLECULE.
88.
89. STRUCTURE OF
MYOGLOBIN
COMPACT, ROUGHLY SPHERICAL
GLOBULAR PROTEIN.
Surface is polar and interior is nonpolar.
EXCEPTION: 2 HISTIDINE Residues
are in centre & help in binding of oxygen
molecule.
MOLECULAR WT.: 17,000 Daltons
153 Aminoacyl residues
90. STRUCTURE OF MYOGLOBIN
75% of amino acid residues are
present in EIGHT RIGHT
HANDED ALPHA Helices.
Each helix contains 7-20
Aminoacids.
Myoglobin stores Oxygen with
the help of its prosthetic group
haeme.
98. PLASMA PROTEINS
Proteins of the plasma are a complex
mixture containing :
Simple proteins
Conjugated proteins ( eg. Glycoproteins)
Concentration of Total Protein in plasma:
6.5g/dl -- 7.5g/dl.
101. FUNCTIONS OF PLASMA PROTEINS
INVOLVEMENT IN
INFLAMMATORY
RESPONSES
C-REACTIVE
PROTEIN
ONCO FETAL ALPHA 1
FETOPROTEIN
TRANSPORT OR
BINDING PROTEINS
1. ALBUMIN– Binds
bilirubin, fatty
acids, steroids etc.
2. Caeruloplasmin
3. Thyroid binding
globulin
4. Transferrin
102. ALBUMIN:
Major protein of human plasma.
3.4 –4.7g/dl
Liver produces 12g of Albumin/day.
Consists of a single polypeptide
chain of 585 Amino acids &
contains 17 disulfide bonds.
Molecular Weight: 69kDa.
103. Functions of Albumin:
1. Maintains osmotic pressure
2. Binds to various ligands like ;
Free Fatty Acids
Calcium
Bilirubin
Steroid Hormones
Drugs ; Sulphonamides, penicillin,
Aspirin.
104. ALPHA 1 ANTITRYPSIN
ALPHA 1 ANTITRYPSIN is also
called alpha 1 antiproteinase.
Single polypeptide chain
containing 3 Oligosaccharide
chains.
Synthesized by hepatocytes.
Inhibits trypsin , elastase.
105. CLINICAL SIGNIFICANCE:
ROLE IN EMPHYSEMA:
ALPHA 1 ANTITRYPSIN prevents
proteolytic damage of lung.
Its deficiency causes EMPHYSEMA.
ROLE IN LIVER DISEASE:
Its deficiency causes damage to
hepatocytes and Cirrhosis of liver.
106. ALPHA 2 MACROGLOBULIN
Large plasma glycoprotein
Mol Wt. –720 kDa
Forms 8-10% of Total Plasma Protein
Transports 10% of Zinc in the Plasma.
SITE OF SYNTHESIS:
Liver
Monocytes
Astrocytes
107. FUNCTION OF ALPHA 2
MACROGLOBULIN:
Major member of C3 and C4
group of Complement Proteins.
It is a PANPROTEINASE
inhibitor.
108. HAPTOGLOBIN—alpha2
Glycoprotein
Binds Extra corpuscular Hemoglobin.
Hb + Haptoglobin- Catabolized by liver,
(65kDa) (90kDa) Iron is reused.
Prevents loss of free Hemoglobin into the
kidney.
109. CERULOPLASMIN---ALPHA 2
GLOBULIN
BINDS 90% OF COPPER PRESENT IN THE
PLASMA.
EACH MOLECULE BINDS 6 ATOMS OF
COPPER.
LOW LEVELS OF CERULOPLASMIN ARE
SEEN IN WILSON’S DISEASE.
110. TRANSFERRIN ---BETA 1 GLOBULIN
1. IT IS A GLYCOPROTEIN SYNTHESIZED IN
THE LIVER .
2. IT TRANSPORTS IRON FROM GUT TO
BONE MARROW & OTHER ORGANS.
3. ONE MOLE OF TRANSFERRIN BINDS
TWO MOL OF FE3+. ( FERRIC IRON).
111. IMMUNOGLOBULINS
1) CIRCULATING , HUMORAL ANTIBODIES
SYNTHESIZED BY THE PLASMA CELLS
WHICH ARE SPECIALIZED CELLS OF
‘B’ CELL LINEAGE.
2) SYNTHESIZED IN RESPONSE TO
EXPOSURE TO ANTIGENS.
112. STRUCTURE OF IMMUNOGLOBULIN:
AMINO TERMINAL END OF
BOTH L & H CHAINS
CARBOXYL TERMINAL END OF
LIGHT CHAINS
DISULPHIDE BONDS
CARBOXYL TERMINAL END
OF H CHAINS
118. STRUCTURE OF IMMUNOGLOBULIN
a. IMMUNOGLOBULINS ARE
GLYCOPROTEINS CONSISTING OF TWO
IDENTICAL LIGHT CHAINS &
TWO IDENTICAL HEAVY CHAINS HELD
TOGETHER AS A TETRAMER (L2H2), BY
DISULFIDE BONDS.
b. IT IS Y SHAPED.
119. STRUCTURE OF IMMUNOGLOBULIN
i. LIGHT CHAINS:
MOL.WT.: 23 kDa
HALF OF THE LIGHT (L) CHAIN
TOWARDS THE CARBOXYL TERMINAL
IS CONSTANT REGION ( CL).
ii. AMINO TERMINAL HALF IS REFERED
TO AS THE VARIABLE REGION (VL).
120. LIGHT CHAIN :
a) ALL LIGHT CHAINS ARE EITHER KAPPA
(k) OR LAMBDA , BASED ON
STRUCTURAL DIFFERENCES IN THEIR
CONSTANT REGIONS.
b) THE VARIABLE (VL) REGIONS FORM
ANTIGEN BINDING SITE ALONG WITH
VARIABLE REGIONS OF HEAVY CHAINS.
121. HEAVY CHAINS:
a) MOLWT: 53-75kDa
b) ONE QUARTER OF HEAVY CHAIN
TOWARDS AMINO TERMINAL IS
VARIABLE REGION.
c) THE REMAINING 3 QUARTERS
TOWARDS CARBOXYL TERMINAL END
IS THE CONSTANT REGION DIVIDED
INTO CH1, CH2, CH3.
122. HEAVY CHAINS:
HINGE REGION :
THE REGION BETWEEN CH1 & CH2 .
IT CONFERS FLEXIBILITY TO
IMMUNOGLOBULIN HELPING THEM TO
BIND TO ANTIGENIC SITES.
123. .
THE ANTIGEN BINDING SITE IS FORMED
BY THE VARIABLE REGIONS OF BOTH
HEAVY & LIGHT CHAINS.,
& IS SPECIFIC FOR A PARTICULAR
ANTIGEN.
124. FIVE TYPES OF HEAVY CHAIN DETERMINE
THE IMMUNOGLIBULIN CLASS.
FIVE DIFFERENT TYPES OF ‘H’ CHAINS
ARE SEEN BASED ON DIFFERENCES IN
THEIR ‘CH’ REGIONS.
IgG: H CHAIN IS GAMMA
IgA: H CHAIN IS ALPHA
IgM:
Ig D: H CHAIN IS DELTA
Ig E : H CHAIN IS EPSILON
130. IMMUNOGLOBULIN E:
MEDIATES IMMEDIATE
HYPERSENSTIVITY REACTIONS.
DEFENDS AGAINST WORM
INFESTATIONS BY CAUSING RELEASE OF
ENZYMES FROM EOSINOPHILS.
DOES NOT FIX COMPLEMENT