This document outlines a biochemistry course for dental students. It provides details about the course objectives, which are to provide students with basic biochemistry knowledge related to dentistry and medicine. The course will cover topics like protein structure and metabolism, carbohydrate digestion and metabolism, lipid chemistry and metabolism, and DNA structure and protein synthesis. It lists the lecture topics, reading assignments, and assessment details. The course will involve lectures, practical sessions, exams, assignments, and a student research project on enzymes.
The chemical elements that form most of living biological matter are oxygen, carbon, hydrogen and nitrogen. These elements form the basic molecules that make up living organisms, including glucose, fructose and proteins which are made of amino acids. DNA and RNA are examples of nucleic acids that control cellular activity and store genetic information. Proteins, carbohydrates, lipids and nucleic acids are the four major macromolecules or classes of biological molecules.
This document provides an overview of a biochemistry course for nursing students. The course aims to enhance students' understanding of general biochemistry basics. It will cover topics like biomolecules, metabolism, and gene expression. The course involves lectures, practical sessions, assignments, and exams. Recommended textbooks and a lecture schedule are provided. Key concepts that will be covered include amino acids, protein structure, carbohydrate metabolism, and lipid metabolism.
The document discusses amino acids, which are the building blocks of proteins. It describes that amino acids contain both an amino group and a carboxyl group and exist in different ionized forms depending on pH. There are 20 standard amino acids that make up proteins in humans. Amino acids can undergo various chemical reactions due to these functional groups and are also classified based on the polarity of their side chains.
Some reagents or conditions that can cause protein denaturation include:
- High or low pH (acids and bases)
- Heat
- Detergents
- Organic solvents (alcohol, acetone)
- Heavy metals (salts of heavy metals like copper, mercury)
- Radiation (UV light, X-rays)
This document discusses the structure and properties of amino acids and proteins. It begins by defining amino acids as the building blocks of proteins and discusses their various classifications including essential vs non-essential amino acids, polarity, and metabolic fate. It then covers the physical properties of amino acids such as solubility, melting point, and their amphoteric nature. Finally, it discusses protein structure, describing the primary, secondary, tertiary and quaternary levels as well as different types of proteins classified by their function.
The document discusses amino acids, which are the basic building blocks of proteins and peptides. It describes the common amino acids found in proteins, including their structures and properties. Key points covered include the formation of peptide bonds between amino acids, the properties of different amino acid side chains, and several small peptides and polypeptides that serve important biological functions. The goal is to educate on the fundamentals of amino acid and protein chemistry.
Lec.3protein chem.classification new microsoft powerpoint presentationDrShamimAkram
Proteins are complex biomolecules composed of amino acid chains that perform essential functions in the human body. They can be classified based on their composition, structure, and function. Some key types of proteins include structural proteins like collagen and keratin; transport proteins like hemoglobin; catalytic proteins which include enzymes; and regulatory proteins such as hormones. There are approximately 50,000 to 200,000 different proteins present in the human body, performing vital roles such as oxygen transport, muscle movement, immune defense, and metabolic processes.
The document provides an overview of amino acids including:
- The goals of learning about amino acid structures, properties, stereochemistry, and relationships between pH and charge.
- The general structure of amino acids including common pKa values and the condensation reaction forming peptide bonds.
- Descriptions of the 20 standard amino acids including their structures, properties in tables and figures.
- Concepts of stereochemistry, chirality, enantiomers, and the chirality and stereochemistry of amino acids.
- Examples of calculations involving amino acid properties like isoelectric points and pH.
- Nomenclature and conventions used in describing peptides and amino acids.
The chemical elements that form most of living biological matter are oxygen, carbon, hydrogen and nitrogen. These elements form the basic molecules that make up living organisms, including glucose, fructose and proteins which are made of amino acids. DNA and RNA are examples of nucleic acids that control cellular activity and store genetic information. Proteins, carbohydrates, lipids and nucleic acids are the four major macromolecules or classes of biological molecules.
This document provides an overview of a biochemistry course for nursing students. The course aims to enhance students' understanding of general biochemistry basics. It will cover topics like biomolecules, metabolism, and gene expression. The course involves lectures, practical sessions, assignments, and exams. Recommended textbooks and a lecture schedule are provided. Key concepts that will be covered include amino acids, protein structure, carbohydrate metabolism, and lipid metabolism.
The document discusses amino acids, which are the building blocks of proteins. It describes that amino acids contain both an amino group and a carboxyl group and exist in different ionized forms depending on pH. There are 20 standard amino acids that make up proteins in humans. Amino acids can undergo various chemical reactions due to these functional groups and are also classified based on the polarity of their side chains.
Some reagents or conditions that can cause protein denaturation include:
- High or low pH (acids and bases)
- Heat
- Detergents
- Organic solvents (alcohol, acetone)
- Heavy metals (salts of heavy metals like copper, mercury)
- Radiation (UV light, X-rays)
This document discusses the structure and properties of amino acids and proteins. It begins by defining amino acids as the building blocks of proteins and discusses their various classifications including essential vs non-essential amino acids, polarity, and metabolic fate. It then covers the physical properties of amino acids such as solubility, melting point, and their amphoteric nature. Finally, it discusses protein structure, describing the primary, secondary, tertiary and quaternary levels as well as different types of proteins classified by their function.
The document discusses amino acids, which are the basic building blocks of proteins and peptides. It describes the common amino acids found in proteins, including their structures and properties. Key points covered include the formation of peptide bonds between amino acids, the properties of different amino acid side chains, and several small peptides and polypeptides that serve important biological functions. The goal is to educate on the fundamentals of amino acid and protein chemistry.
Lec.3protein chem.classification new microsoft powerpoint presentationDrShamimAkram
Proteins are complex biomolecules composed of amino acid chains that perform essential functions in the human body. They can be classified based on their composition, structure, and function. Some key types of proteins include structural proteins like collagen and keratin; transport proteins like hemoglobin; catalytic proteins which include enzymes; and regulatory proteins such as hormones. There are approximately 50,000 to 200,000 different proteins present in the human body, performing vital roles such as oxygen transport, muscle movement, immune defense, and metabolic processes.
The document provides an overview of amino acids including:
- The goals of learning about amino acid structures, properties, stereochemistry, and relationships between pH and charge.
- The general structure of amino acids including common pKa values and the condensation reaction forming peptide bonds.
- Descriptions of the 20 standard amino acids including their structures, properties in tables and figures.
- Concepts of stereochemistry, chirality, enantiomers, and the chirality and stereochemistry of amino acids.
- Examples of calculations involving amino acid properties like isoelectric points and pH.
- Nomenclature and conventions used in describing peptides and amino acids.
1. Vitamins are organic molecules that serve as cofactors for enzyme reactions and must be obtained through diet as they cannot be synthesized by the body.
2. Vitamins are classified as either water-soluble or fat-soluble, with water-soluble vitamins including all B vitamins and vitamin C, and fat-soluble vitamins being vitamins A, D, E, and K.
3. Each vitamin has a specific biochemical function, such as vitamin C serving as an antioxidant and cofactor for collagen synthesis, vitamin B12 acting as a cofactor for fatty acid and amino acid metabolism, and vitamin K being required for blood clotting through gamma-carboxylation of glutamate residues.
The document summarizes a biochemistry group project on proteins. The group, led by Mohammad Raes, discussed the definition, chemistry, structure, classification, properties, and functions of proteins. Key points included that proteins are polymers of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. Proteins perform important roles such as enzymes, hormones, antibodies, and structure.
This document discusses biomolecules and amino acids. It outlines key topics like the properties of amino acids, their pKa values and titration curves. At physiological pH, both the carboxyl and amino groups of amino acids are charged. Only L-amino acids are found in proteins. Some examples of clinical aminoacidurias caused by metabolic or absorption defects are also provided. The document further discusses post-translational modifications, peptide bonds, and the different conformations and restrictions placed on protein structure by the planar nature of peptide bonds.
This document discusses amino acids, which are the building blocks of proteins. It defines the basic structure of an amino acid and notes that the 20 standard amino acids are the monomer units that make up proteins. The document then categorizes amino acids based on different properties like their structure, side chains, nutritional requirements, and metabolic fate. It also discusses acid-base properties and isoelectric points of different amino acids.
This document provides an overview of organic compounds and macromolecules. It discusses the four major classes of macromolecules - carbohydrates, lipids, proteins, and nucleic acids. For each class, it describes the monomer units, examples, functions, and how the monomers polymerize to form larger molecules through condensation reactions. It also covers topics like DNA replication, protein structure and folding, and the roles of these macromolecules in biological processes.
This document provides an overview of amino acids and peptide bonds. It defines amino acids as organic compounds containing amino and carboxyl groups that are the building blocks of proteins. There are 20 standard amino acids that make up proteins in the human body. The document discusses the structures, properties, classifications, and importance of amino acids. It also defines peptide bonds as covalent bonds formed between the amino group of one amino acid and the carboxyl group of another amino acid, linking them together in a polypeptide chain. Key reactions and tests for identifying amino acids are also outlined.
This document summarizes key chemistry concepts related to the building blocks of life. It covers the elements, atoms, and molecules that make up living organisms. It also describes the four main types of organic compounds - carbohydrates, lipids, proteins, and nucleic acids - and provides examples of each. Water is highlighted for its importance as a solvent and in biological processes and reactions.
This document provides an overview of basic metabolic pathways in plants. It discusses primary and secondary metabolism, the role of enzymes and co-enzymes, and several key pathways such as the shikimic acid, acetate, and mevalonate pathways. Primary metabolites such as starch, cellulose, and chlorophyll are synthesized through basic metabolic pathways and are essential for plant growth and function. Secondary metabolites are derived from primary metabolites and have pharmacological activities. Enzymes help catalyze biochemical reactions in metabolic pathways, while co-enzymes assist enzymes and participate in reactions. Biosynthesis converts carbon dioxide into carbohydrates through photosynthesis.
Vitamins serve as cofactors or coenzymes that are essential for many enzymatic reactions in the body. Most B vitamins act as coenzymes by facilitating the transfer of atoms or groups between molecules during metabolism. Coenzymes work with enzymes to carry out the enzymes' activity, often by transporting chemical groups from one reactant to another. Vitamins are organic molecules that the body needs but cannot synthesize in adequate amounts, so they must be obtained through the diet.
Bacterial metabolism involves catabolic and anabolic processes. Catabolism breaks down nutrients to release energy through reactions like aerobic respiration, anaerobic respiration, and fermentation. Anabolism uses this energy to build macromolecules. Bacteria take in nutrients like sugars, lipids, nitrogen, and oxygen and break them down extracellularly before transporting subunits into cells for energy generation and biosynthesis through various pathways. Aerobic respiration is most efficient, while anaerobic respiration and fermentation are less efficient in the absence of oxygen.
Lec 1 level 3-de (chemistry of amino acids)dream10f
This document outlines the course objectives, schedule, and content for a biochemistry course for dental students, including introducing basic biomolecules, protein structure and function, enzyme kinetics, carbohydrate, lipid, and nucleic acid metabolism. The course is taught over 19 weeks with lectures, practical sessions, assignments, quizzes, and exams assessed by two instructors. Recommended textbooks and office hours are also provided.
This document provides an overview of basic biochemistry concepts. It discusses that all matter is composed of elements, which form compounds and molecules through bonding. The six most important elements that make up 98% of organisms are carbon, hydrogen, nitrogen, oxygen, phosphorus, and sulfur. It then focuses on organic chemistry, explaining that carbon can form many combinations with other atoms. The four main classes of organic molecules that make up living things are carbohydrates, lipids, proteins, and nucleic acids. It provides details on the structure and functions of these molecules, including monomers, polymers, and important examples. Secondary metabolites are also discussed.
Amino acids are organic compounds that form the building blocks of proteins. They contain an amino group, a carboxyl group, and a side chain that allows for variation. There are three levels of protein structure: primary structure refers to the amino acid sequence; secondary structure involves regular sub-structures like alpha helices and beta sheets; tertiary structure describes the overall 3D shape of a protein formed by interactions between secondary structures. Proteins fold into unique tertiary structures to perform their functions, and some require molecular chaperones to fold correctly.
The key chemical elements that make up living organisms are oxygen, carbon, hydrogen, and nitrogen. Organic substances like proteins and carbohydrates are complex molecules composed of carbon chains, whereas inorganic substances like water and mineral salts contain fewer atoms. Mineral salts contain metallic and non-metallic elements and can be found dissolved in cells or as part of structures. Organic molecules perform important structural, energetic, control, and enzymatic functions for living beings through roles like storing energy, transmitting genetic information, and facilitating chemical reactions. Water has properties like polarity and high heat capacity that make it uniquely suited to support life.
Biomolecules are organic compounds that serve as the building blocks of living organisms. The four most abundant elements in the human body are carbon, hydrogen, oxygen and nitrogen. Biomolecules are typically carbon-based and have specific three-dimensional shapes defined by bonds between carbon atoms. Functional groups on biomolecules, such as hydroxyl, amino and carboxyl groups, determine their chemical properties. Carbohydrates are an important class of biomolecules that serve as energy stores. They are made of carbon, hydrogen and oxygen and can exist as monosaccharides, disaccharides or polysaccharides.
This document summarizes the chemistry of enzymes, including their classification and chemical composition. It discusses that enzymes are proteins that act as biological catalysts and speed up reactions. Enzymes are classified in multiple ways, including based on their site of action as intracellular endoenzymes or extracellular exoenzymes, and based on the reaction they control using the EC system of six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The document also describes several key enzyme terminology concepts, such as cofactors, coenzymes, prosthetic groups, and substrates.
Proteins are polymers of amino acids and perform a variety of essential functions in living cells. They can be classified based on their structure, composition, and properties. The main types are globular and fibrous proteins. Globular proteins are spherical and soluble, while fibrous proteins are elongated and form connections between tissues. Proteins are also classified as simple proteins containing only amino acids, or conjugated proteins which contain non-amino acid groups like carbohydrates, lipids, or metals. Amino acids polymerize to form peptide bonds, linking them into protein chains.
This document provides an overview of a biochemistry course for nursing students. It outlines the course objectives, which include understanding biomolecules, metabolic processes, gene function, and the scientific basis of disease. The course will be taught through lectures, practical sessions, assignments, and exams. Topics to be covered include amino acids, protein structure, carbohydrate metabolism, lipid metabolism, vitamins, and gene expression. Recommended textbooks are provided, and the lecture schedule lists the weekly topics and assigned readings.
BIOCHEMISTRY. Presentation slides for the group ptxyakemichael
This document provides an overview of biochemistry. It defines biochemistry as the chemistry that occurs within living organisms. The document outlines the major biomolecules like carbohydrates, lipids, proteins, and nucleotides that serve as building blocks for larger macromolecules. It also describes some of the key properties of amino acids like their central carbon atom, amino group, carboxyl group, and variable side chains. Additionally, the document explains how amino acids combine through peptide bonds to form polypeptides and proteins, and how the properties of the side chains influence protein structure and function.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, which includes an amino group, carboxyl group, and side chain. The document then classifies amino acids according to their side chains and discusses their optical, acid-base, and buffer properties. It also distinguishes between standard and non-standard amino acids, and essential vs non-essential amino acids which must be obtained through diet.
Proteins are made up of amino acids and perform important functions in the body. They can act as enzymes, hormones, antibodies, and structures. Amino acids are the building blocks of proteins, containing an amino group, a carboxyl group, and an R group that determines their properties. Amino acids can be classified based on their R group, charge, and essential/nonessential status. Key amino acid properties include acid-base behavior, isoelectric point, and ability to form zwitterions. Common reactions used to identify amino acids include ninhydrin, FDNB, Dansyl, and Edman reactions.
1. Vitamins are organic molecules that serve as cofactors for enzyme reactions and must be obtained through diet as they cannot be synthesized by the body.
2. Vitamins are classified as either water-soluble or fat-soluble, with water-soluble vitamins including all B vitamins and vitamin C, and fat-soluble vitamins being vitamins A, D, E, and K.
3. Each vitamin has a specific biochemical function, such as vitamin C serving as an antioxidant and cofactor for collagen synthesis, vitamin B12 acting as a cofactor for fatty acid and amino acid metabolism, and vitamin K being required for blood clotting through gamma-carboxylation of glutamate residues.
The document summarizes a biochemistry group project on proteins. The group, led by Mohammad Raes, discussed the definition, chemistry, structure, classification, properties, and functions of proteins. Key points included that proteins are polymers of amino acids and have four levels of structure - primary, secondary, tertiary, and quaternary. Proteins perform important roles such as enzymes, hormones, antibodies, and structure.
This document discusses biomolecules and amino acids. It outlines key topics like the properties of amino acids, their pKa values and titration curves. At physiological pH, both the carboxyl and amino groups of amino acids are charged. Only L-amino acids are found in proteins. Some examples of clinical aminoacidurias caused by metabolic or absorption defects are also provided. The document further discusses post-translational modifications, peptide bonds, and the different conformations and restrictions placed on protein structure by the planar nature of peptide bonds.
This document discusses amino acids, which are the building blocks of proteins. It defines the basic structure of an amino acid and notes that the 20 standard amino acids are the monomer units that make up proteins. The document then categorizes amino acids based on different properties like their structure, side chains, nutritional requirements, and metabolic fate. It also discusses acid-base properties and isoelectric points of different amino acids.
This document provides an overview of organic compounds and macromolecules. It discusses the four major classes of macromolecules - carbohydrates, lipids, proteins, and nucleic acids. For each class, it describes the monomer units, examples, functions, and how the monomers polymerize to form larger molecules through condensation reactions. It also covers topics like DNA replication, protein structure and folding, and the roles of these macromolecules in biological processes.
This document provides an overview of amino acids and peptide bonds. It defines amino acids as organic compounds containing amino and carboxyl groups that are the building blocks of proteins. There are 20 standard amino acids that make up proteins in the human body. The document discusses the structures, properties, classifications, and importance of amino acids. It also defines peptide bonds as covalent bonds formed between the amino group of one amino acid and the carboxyl group of another amino acid, linking them together in a polypeptide chain. Key reactions and tests for identifying amino acids are also outlined.
This document summarizes key chemistry concepts related to the building blocks of life. It covers the elements, atoms, and molecules that make up living organisms. It also describes the four main types of organic compounds - carbohydrates, lipids, proteins, and nucleic acids - and provides examples of each. Water is highlighted for its importance as a solvent and in biological processes and reactions.
This document provides an overview of basic metabolic pathways in plants. It discusses primary and secondary metabolism, the role of enzymes and co-enzymes, and several key pathways such as the shikimic acid, acetate, and mevalonate pathways. Primary metabolites such as starch, cellulose, and chlorophyll are synthesized through basic metabolic pathways and are essential for plant growth and function. Secondary metabolites are derived from primary metabolites and have pharmacological activities. Enzymes help catalyze biochemical reactions in metabolic pathways, while co-enzymes assist enzymes and participate in reactions. Biosynthesis converts carbon dioxide into carbohydrates through photosynthesis.
Vitamins serve as cofactors or coenzymes that are essential for many enzymatic reactions in the body. Most B vitamins act as coenzymes by facilitating the transfer of atoms or groups between molecules during metabolism. Coenzymes work with enzymes to carry out the enzymes' activity, often by transporting chemical groups from one reactant to another. Vitamins are organic molecules that the body needs but cannot synthesize in adequate amounts, so they must be obtained through the diet.
Bacterial metabolism involves catabolic and anabolic processes. Catabolism breaks down nutrients to release energy through reactions like aerobic respiration, anaerobic respiration, and fermentation. Anabolism uses this energy to build macromolecules. Bacteria take in nutrients like sugars, lipids, nitrogen, and oxygen and break them down extracellularly before transporting subunits into cells for energy generation and biosynthesis through various pathways. Aerobic respiration is most efficient, while anaerobic respiration and fermentation are less efficient in the absence of oxygen.
Lec 1 level 3-de (chemistry of amino acids)dream10f
This document outlines the course objectives, schedule, and content for a biochemistry course for dental students, including introducing basic biomolecules, protein structure and function, enzyme kinetics, carbohydrate, lipid, and nucleic acid metabolism. The course is taught over 19 weeks with lectures, practical sessions, assignments, quizzes, and exams assessed by two instructors. Recommended textbooks and office hours are also provided.
This document provides an overview of basic biochemistry concepts. It discusses that all matter is composed of elements, which form compounds and molecules through bonding. The six most important elements that make up 98% of organisms are carbon, hydrogen, nitrogen, oxygen, phosphorus, and sulfur. It then focuses on organic chemistry, explaining that carbon can form many combinations with other atoms. The four main classes of organic molecules that make up living things are carbohydrates, lipids, proteins, and nucleic acids. It provides details on the structure and functions of these molecules, including monomers, polymers, and important examples. Secondary metabolites are also discussed.
Amino acids are organic compounds that form the building blocks of proteins. They contain an amino group, a carboxyl group, and a side chain that allows for variation. There are three levels of protein structure: primary structure refers to the amino acid sequence; secondary structure involves regular sub-structures like alpha helices and beta sheets; tertiary structure describes the overall 3D shape of a protein formed by interactions between secondary structures. Proteins fold into unique tertiary structures to perform their functions, and some require molecular chaperones to fold correctly.
The key chemical elements that make up living organisms are oxygen, carbon, hydrogen, and nitrogen. Organic substances like proteins and carbohydrates are complex molecules composed of carbon chains, whereas inorganic substances like water and mineral salts contain fewer atoms. Mineral salts contain metallic and non-metallic elements and can be found dissolved in cells or as part of structures. Organic molecules perform important structural, energetic, control, and enzymatic functions for living beings through roles like storing energy, transmitting genetic information, and facilitating chemical reactions. Water has properties like polarity and high heat capacity that make it uniquely suited to support life.
Biomolecules are organic compounds that serve as the building blocks of living organisms. The four most abundant elements in the human body are carbon, hydrogen, oxygen and nitrogen. Biomolecules are typically carbon-based and have specific three-dimensional shapes defined by bonds between carbon atoms. Functional groups on biomolecules, such as hydroxyl, amino and carboxyl groups, determine their chemical properties. Carbohydrates are an important class of biomolecules that serve as energy stores. They are made of carbon, hydrogen and oxygen and can exist as monosaccharides, disaccharides or polysaccharides.
This document summarizes the chemistry of enzymes, including their classification and chemical composition. It discusses that enzymes are proteins that act as biological catalysts and speed up reactions. Enzymes are classified in multiple ways, including based on their site of action as intracellular endoenzymes or extracellular exoenzymes, and based on the reaction they control using the EC system of six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The document also describes several key enzyme terminology concepts, such as cofactors, coenzymes, prosthetic groups, and substrates.
Proteins are polymers of amino acids and perform a variety of essential functions in living cells. They can be classified based on their structure, composition, and properties. The main types are globular and fibrous proteins. Globular proteins are spherical and soluble, while fibrous proteins are elongated and form connections between tissues. Proteins are also classified as simple proteins containing only amino acids, or conjugated proteins which contain non-amino acid groups like carbohydrates, lipids, or metals. Amino acids polymerize to form peptide bonds, linking them into protein chains.
This document provides an overview of a biochemistry course for nursing students. It outlines the course objectives, which include understanding biomolecules, metabolic processes, gene function, and the scientific basis of disease. The course will be taught through lectures, practical sessions, assignments, and exams. Topics to be covered include amino acids, protein structure, carbohydrate metabolism, lipid metabolism, vitamins, and gene expression. Recommended textbooks are provided, and the lecture schedule lists the weekly topics and assigned readings.
BIOCHEMISTRY. Presentation slides for the group ptxyakemichael
This document provides an overview of biochemistry. It defines biochemistry as the chemistry that occurs within living organisms. The document outlines the major biomolecules like carbohydrates, lipids, proteins, and nucleotides that serve as building blocks for larger macromolecules. It also describes some of the key properties of amino acids like their central carbon atom, amino group, carboxyl group, and variable side chains. Additionally, the document explains how amino acids combine through peptide bonds to form polypeptides and proteins, and how the properties of the side chains influence protein structure and function.
This document discusses amino acids, which are the building blocks of proteins. It defines amino acids and their basic structure, which includes an amino group, carboxyl group, and side chain. The document then classifies amino acids according to their side chains and discusses their optical, acid-base, and buffer properties. It also distinguishes between standard and non-standard amino acids, and essential vs non-essential amino acids which must be obtained through diet.
Proteins are made up of amino acids and perform important functions in the body. They can act as enzymes, hormones, antibodies, and structures. Amino acids are the building blocks of proteins, containing an amino group, a carboxyl group, and an R group that determines their properties. Amino acids can be classified based on their R group, charge, and essential/nonessential status. Key amino acid properties include acid-base behavior, isoelectric point, and ability to form zwitterions. Common reactions used to identify amino acids include ninhydrin, FDNB, Dansyl, and Edman reactions.
Amino acids & Proteins for Ist MBBS edited.pptxDeepAnrAj901320
Proteins are composed of amino acids and perform many essential functions in the body. There are over 300 known amino acids but only 20 are used to build mammalian proteins through protein synthesis. Amino acids contain an amino group, a carboxyl group, a hydrogen atom, and a variable side chain. They are distinguished by their side chains and can be classified based on structure, nutritional requirements, metabolic fate, and solubility. Proteins serve as enzymes, hormones, structural elements, transporters, and more, playing a vital role in the structure and function of the human body.
This document provides an overview of a biochemistry course taught by Dr. Asmaa Saleh Ali. The course covers topics like amino acids and protein structure, lipids, carbohydrates, enzymes, vitamins, and metabolism over 11 weeks. Students will be assessed through two exams, class participation, and a final cumulative exam which together will make up 100% of their grade. The first lecture will introduce biochemistry and the basic biomolecules found in living organisms including an in-depth discussion of amino acids and protein structure.
This document classifies and describes amino acids. It discusses how amino acids can be classified based on the polarity and charge of their side chains, their structure, catabolic fate, and whether the human body can synthesize them. It also describes the unique properties of different amino acid categories, including those with nonpolar, proline, uncharged polar, acidic, and basic side chains. Proline forms a rigid ring structure. Nonpolar amino acids cluster inside proteins. Polar amino acids form hydrogen bonds and cysteine forms disulfide bonds.
This document discusses amino acids, which are organic compounds that contain amino and carboxyl groups and form proteins by binding together via peptide bonds. Amino acids are classified based on their structure, polarity, and nutritional requirements. There are essential and non-essential amino acids. Amino acids can undergo reactions like decarboxylation, amide formation, transamination, and oxidative deamination. They have amphoteric properties due to acidic and basic groups and exist as zwitterions at their isoelectric pH. Peptide bonds between amino acids are planar and rigid.
Proteins are composed of chains of amino acids and perform essential functions in the body. There are 20 standard amino acids, some of which are essential and must be obtained through diet. Amino acids link together through peptide bonds to form polypeptide chains or proteins. Proteins have four levels of structure and take on complex shapes that enable their many functions like structure, movement, hormones, and enzymes. A deficiency or excess of proteins can cause health issues.
Biomolecules are organic compounds that are present in living organisms. The four primary types of biomolecules are carbohydrates, lipids, proteins, and nucleic acids. Carbon is the most important element in biomolecules as it can form diverse and complex organic compounds through its ability to form bonds with four other atoms. Proteins are polymers of amino acids, while nucleic acids are polymers of nucleotides. Amino acids and nucleotides are the basic monomeric units that join together through condensation reactions to form the larger macromolecules. There are 20 standard amino acids that make up proteins in living organisms.
B.Sc. Biochem II Biomolecule I U 2 ProteinsRai University
1. Proteins are composed of chains of amino acids linked together by peptide bonds. There are 20 standard amino acids that make up proteins.
2. Amino acids can be classified as essential or nonessential based on whether the human body can synthesize them. They also have different physical and chemical properties depending on their structure.
3. Peptide bonds form when the amino group of one amino acid reacts with the carboxyl group of another, linking the amino acids into polypeptide chains. The specific order and linking of amino acids determines a protein's structure and function.
This document provides information on proteins and amino acids. It discusses that proteins are the most abundant organic molecules in living systems and are composed of amino acids. It then describes the 20 standard amino acids, how they are classified based on structure and properties. The document also discusses the nutritional classification of amino acids as essential or non-essential and their metabolic roles as being glucogenic, ketogenic or both.
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
Proteins are the most abundant organic molecules in living systems and perform a variety of important structural and functional roles. They are polymers of 20 different amino acids, which are linked together via peptide bonds. 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 twisting or folding of the polypeptide chain into alpha helices or beta sheets. Tertiary structure refers to the three-dimensional structure of a functional protein, while quaternary structure involves proteins composed of multiple polypeptide subunits.
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.
1) Amino acids can be classified based on their source, side chain structure, amphoteric properties, nutritional requirements, and metabolic fate. 2) The 20 standard amino acids are incorporated into proteins during translation based on codon sequences, while non-standard amino acids play other important biological roles. 3) Selenocysteine is the 21st amino acid encoded by UGA codons when accompanied by a selenocysteine insertion sequence in mRNA.
Lec2 amino.a.classification microsoft powerDrShamimAkram
Amino acids can be classified in several ways:
1. Based on their source as either standard/primary amino acids that are incorporated into proteins or non-standard amino acids that do not participate in protein synthesis.
2. By the properties of their side chains as non-polar, polar uncharged, acidic, or basic. Non-polar amino acids cluster inside proteins while polar ones interact through hydrogen bonding.
3. According to their roles in metabolism as either glycogenic, ketogenic, or both glycogenic and ketogenic.
Selenocysteine, containing the element selenium, is now recognized as the 21st standard amino acid despite being incorporated via a unique genetic mechanism during translation.
Proteins are composed of amino acids, which are the basic structural units. There are 20 amino acids that make up mammalian proteins. Amino acids contain an amino group, a carboxyl group, a hydrogen atom, and a distinctive side chain. They can be classified based on properties like charge, polarity, and nutritional properties. Amino acids join together via peptide bonds to form polypeptides and proteins. Dietary proteins are broken down into amino acids through digestion before being used for various metabolic functions in the body.
This document discusses the classification of amino acids. It summarizes that amino acids can be classified into different categories based on their R-group structure, polarity, nutritional requirements, and catabolism. The key classifications covered include non-polar vs polar amino acids, essential vs non-essential amino acids based on nutritional needs, and glucogenic, ketogenic, or mixed amino acids based on their metabolic fates. The document also provides examples of amino acids that fall into each of these different classification groups.
Similar to Lec1 level3-dechemistryofaminoacids-130204015753-phpapp02 (20)
This document discusses suffixes and terminology used in medicine. It begins by listing common combining forms used to build medical terms and their meanings. It then defines several noun, adjective, and shorter suffixes and provides their meanings. Examples are given of medical terms built using combining forms and suffixes. The document also examines specific medical concepts in more depth, such as hernias, blood cells, acromegaly, splenomegaly, and laparoscopy.
The document is a chapter from a medical textbook that discusses anatomical terminology pertaining to the body as a whole. It defines the structural organization of the body from cells to tissues to organs to systems. It also describes the body cavities and identifies the major organs contained within each cavity, as well as anatomical divisions of the abdomen and back.
This document is from a textbook on medical terminology. It discusses the basic structure of medical words and how they are built from prefixes, suffixes, and combining forms. Some key points:
- Medical terms are made up of elements including roots, suffixes, prefixes, and combining vowels. Understanding these elements is important for analyzing terms.
- Common prefixes include hypo-, epi-, and cis-. Common suffixes include -itis, -algia, and -ectomy.
- Dozens of combining forms are provided, such as gastro- meaning stomach, cardi- meaning heart, and aden- meaning gland.
- Rules are provided for analyzing terms, such as reading from the suffix backward and dropping combining vowels before suffixes starting with vowels
This document is the copyright information for Chapter 25 on Cancer from the 6th edition of the textbook Molecular Cell Biology published in 2008 by W. H. Freeman and Company. The chapter was authored by a team that includes Lodish, Berk, Kaiser, Krieger, Scott, Bretscher, Ploegh, and Matsudaira.
This document is the copyright information for Chapter 24 on Immunology from the 6th edition of the textbook Molecular Cell Biology published in 2008 by W. H. Freeman and Company. The chapter was authored by Lodish, Berk, Kaiser, Krieger, Scott, Bretscher, Ploegh, and Matsudaira.
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This document is the copyright page for Chapter 16 from the 6th edition of the textbook "Molecular Cell Biology" published in 2008 by W. H. Freeman and Company. The chapter is titled "Signaling Pathways that Control Gene Activity" and is authored by a group of scientists including Lodish, Berk, Kaiser, Krieger, Scott, Bretscher, Ploegh and Matsudaira.
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2. Biochemistry BCH 261
This course Prepared by
Dr.Eman Saqr
2
Course Directors
***********
Associate Prof. Dr. Ehab(Male)
Assistant Prof.Dr. Eman Saqr (Female)
3. Course Objectives
To give the dental student the basic
knowledge of biochemistry which
is related to dentistry and
medicine.
3
4. The study of biochemistry is essential
to understand:
Basic functions of the body.
How the food that we eat is digested, absorbed, and used
to make ingredients of the body?
How does the body derive energy for normal day to day
work?
How are the various metabolic processes interrelated?
What is the function of genes?
The study of biochemistry is necessary to give the
scientific basis for disease and is useful for intelligent
treatment of patients.
4
5. Lectures schedule-Male/Female
Week Date/Saturday Subject
Reading
assignment
Quizzes
1
26/1/2013
Registration
2 2/2/2013
Introduction of
biochemistry and
explain the course
syllabus
Amino acids
Text book of
Biochemistry for
Dental Students 2th
edition
Chapter 2 pp. 7-12
3
9/2/2013 A Chemistry of
Proteins
Chapter 2 pp. 12-18
4 16/2/2013
Protein metabolism Chapter 12 pp. 107-109 Quiz 1 in the time of
practical session
5
23/2/2013
- urea cycle
- Introduction to
enzyme
Chapter 12 pp. 110-111
Chapter 3 pp. 19-22
6 2/3/2013
Enzymes and coenzyme Chapter 3 pp. 23-29 Quiz 2 in the time of
practical session
7
9/3/2013
Chemistry and
digestion of
carbohydrates
Chapter 4 pp. 31-41
5
6. 10 30/3/2013
Carbohydrate
metabolism I
[Glycolysis, citric acid
cycle and
gluconeogenesis]
Chapter 5 pp. 42-50
Chapter 14 pp. 128-132
11 6/4/2013
Carbohydrate
metabolism II
[Glycogen metabolism
and pentose shunt]
Chapter 5 pp. 50-53
Chapter 7 pp. 61-62
12
13/4/2013 Chemistry of lipids Chapter 9 pp. 76-82 Quiz 3 in the time of
practical session
13
20/4/2013 Lipid metabolism. Chapter 10 pp. 83-95
14 27/4/2013
DNA: Structure and
replication
Chapter 24 pp. 209-214 Quiz 4 in the time of
practical session
15 6/5/2013
Genetic code and
Protein biosynthesis
Chapter 25 pp. 215-221
16 13/5/2013 Practical Exam
17
20/5/2013 Oral Exam
18
27/5/2013
Final Exam
19
1/6/2013
5/6/2013
Summer Vacation
6
7. Recommended Books, References &
Teaching Materials
•Textbook of biochemistry for dental students by DM
Vasudevan, Sreekumari S and Kannan
Vaidyanathan, 2nd Edition 2011.
•Biochemistry by P.C. Champe, R.A. Harvey and D.R.
Ferrier 3rd Edition 2005 Lippincott’s Illustrated Reviews
•Handbook of biochemistry (For allied and nursing
students) by Shivananda Nayak B 1st Edition 2007.
7
8. Teaching Methodology:
• Lecture. 1hours
•Practical Sessions. 2 hours
Assessment Tools for each semester:
20% - Mid-Exam
40% - Final Exam
20% - Assignments
20% - Practical
Assignments are:
• 5 marks for each of Research project, Oral, and
Quizzes.
• 5 marks for attendance, attitude and participation
during lecture session.
8
9. Research Project
• Each one can choose one type of enzyme as
a subject of the project.
• Five students from each group will discuss
their project weekly starting from the third
week according to their presence in the
attendance sheet.
• The only excuse is by recommended medical
certificate.
9
10. Time Table for Female
Group One Group Two
Theoretical
Sunday Sunday
11-12 8-9
Class 17 Class 11
Practical
Sunday Sunday
12-2 9-11
Office Hours Saturday 10-12
10
11. Time Table for Male
Group One Group Two
Theoretical
Sunday Sunday
7-8 4-5
Class 15 Class 15
Practical
Sunday Sunday
8-10 5-7
Office Hours Saturday 5-7
11
12. Biomolecules
The human body is composed of 6 elements, oxygen,
carbon, hydrogen, nitrogen, calcium and phosphorus.
Human body is composed of about 60% water, 15%
proteins, 15% lipids, 2% carbohydrates and 8% minerals.
Biomolecules are covalently linked to each other to form
macromolecules of the cell, eg. Glucose to glycogen and
amino acids to proteins.
Major complex biomolecules are proteins,
polysaccharides, lipids and nucleic acids.
The macromolecules associate with each other to form
supramolecular systems, e.g. ribosomes, lipoproteins.
12
13. Protein
Definition:
• Proteins are group of organic compounds
composed of carbons, hydrogen, oxygen and
nitrogen (sulphur and phosphorus may also
present).
• They are the most important of all biologic
substances .
• They are polymers of L-amino acids linked
together by peptide bonds.
13
14. Amino acids
Definition:
• They are the building blocks of proteins.
• They are organic compounds, which contain two
functional groups, amino group (-NH2) and
carboxyl group (-COOH).
• The amino group is usually attached to the α-
carbon atom (next to the -COOH group).
• Amino acids present in proteins are of the α-L-type
i.e. the amino (H2N-) group is present on the left
side of the vertical formula.
14
16. Classifications of amino acids
• Classification according to structure
• Classification according to side chain
• Classification according to metabolic fate
• Classification according to nutritional requirement
•
16
20. 5- Derived amino acid
• Derived amino acids found in protein. Some
amino acids modified after protein synthesis
such as hydroxy proline and hydroxy lysine which
are important component of collagen. Gamma
crboxylation of glutamic acid residues of proteins
is important for clotting process.
• Derived amino acids not seen in protein. Some
derived amino acids are seen free in cells as
ornithine. Others produced during the
metabolism of amino acids as citrulline and
homocysteine. All of these amino acids called
Non-protein amino acids.
20
21. Classification according to side chain
1- Amino acids having nonpolar side chain:
• These groups are hydrophobic and lipophilic.
• These include, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline,
Phenylalanine and Tryptophan.
2- Amino acids having uncharged or nonionic polar side chain:
• These groups are hydrophilic in nature.
• These include, Glycine, Serine, Threonine, Cysteine, Tyrosine, Glutamine
and Asparagine.
3- Amino acids having charged or ionic polar side chain:
• These groups are hydrophilic in nature.
• Acidic amino acids: They have a negative charge on the R group include,
Aspartic acid and Glutamic acid (Tyrosine is midly acidic).
• Basic amino acids: They have a positive charge on the R group include,
Lysine, Arginine and Histidine.
21
22. Classification according to metabolic
fate1- Purely Ketogenic:
• Leucine is purely ketogenic because it will enter into the
metabolic pathway of ketogenesis.
2- Ketogenic and Glucogenic:
• Lysine, Isoleucine, Phenylalanine, Tyrosine and Tryptophan are
partially ketogenic and partially glucogenic.
• During metabolism, part of the carbon skeleton of these amino
acids will enter the fatty acid metabolic pathway and the other
part into glucose pathway.
3- Purely Glucogenic:
• All the remaining 14 amino acids are purely glucogenic as they
enter only into the glucogenic pathway.
22
23. Classification according to nutritional
requirement
1- Essential or indispensable:
• These groups are essential for growth.
• Their carbon skeleton of these amino acids
cannot be synthesized by human being.
• These include, Isoleucine, Leucine, Threonine,
Lysine, Methionine, Phenylalanine,
Tryptophan and Valine.
23
24. 2- Partially essential or semi-essential:
• Growing children require them in food, but they
are not essential for the adult individual.
• These include, Histidine and Arginine.
2- Nonessential or dispensable:
• The remaining 10 amino acids are nonessential.
• They also required for normal protein synthesis.
• Their carbon skeleton can be synthesized by
metabolic pathways.
24
25. Properties of amino acids:
I. Physical properties
1- .Amphoteric properties:
• _ In solution, amino acids behave as acids and alkalis due
to the presence of acidic group (-COOH) and basic group
(-NH2). On complete ionization of neutral amino acids it
acts as dipolar ions (Zwitterions or hybrid), they carry both
negative and positive charges, which are equal. This
explains the amphoteric
• property of amino acid, i.e. they can react with acids and
bases.
• At isoelectric point, the amino acid carry no net charge; all
the groups are ionized but the charges will cancel each
other. Therefore, at iso-electric points, there is no mobility
in an electrical field. Also solubility and buffering capacity
will be minimum.
25
26. 2- Optical activity ;
• _ All amino acids except glycine are optically
active. Each optically active amino acid contains
one asymmetric α-C atom attached to four
different groups.
• They occur in D and L forms.
• The naturally occurring amino acids in proteins
are of the L-α amino acid form.
• D-amino acids are found in some antibiotics and
bacteria.
26
28. II. Chemical properties
1- Reactions due to carboxyl group:
A. Decarboxylation
• The amino acids will undergo alpha decarboxylation to
form the corresponding amine.
• Ex. Histidine ---------- Histamine +CO2
Tyrosine ---------- Tyramine +CO2
Tryptophan------- Tryptamine +CO2
Glutamic acid --- Gamma aminobutyric acid +CO2
28
30. B. Amide formation:
• The –COOH group of dicarboxylic acids (other
than alpha carboxyl) can combine with ammonia
to form the corresponding amide.
• Ex. Aspartic acid + NH3 ------- Asparagine
Glutamic acid + NH3 ------- Glutamine
• These amides are components of protein
structure.
• The amide group of glutamine serves as the
source of nitrogen for nucleic acid synthesis.
30
32. 2- Reactions due to amino group
A.Transamination
• The alpha amino group of amino acid can be
transferred to alpha keto acid to form the
corresponding new amino acid and alpha keto
acid.
• This is an important reaction in the body for the
inter conversion of amino acids and for synthesis
of nonessential amino acids.32
34. B. Oxidative deamination
• The alpha amino group is removed from
the amino acid to form the corresponding
keto acid and ammonia.
• In the body, Glutamic acid is the most
common amino acid to undergo oxidative
deamination.
34
36. Reaction due to amino group
Transamination and oxidative deamination
36
37. 3- Reactions due to side chains:
A. Ester formation by OH group
• The hydroxyl amino acids can form esters with
phosphoric acid.
• In this manner the Serine and Threonine
residues of proteins are involved in the
formation of phosphoproteins.
• Similarly these hydroxyl groups can form O-
glycosidic bonds with carbohydrate residues to
form glycoproteins.
37
38. B. Reaction of the amide group
The amide groups of Glutamine and Asparagine can
form N-glycosidic bonds with carbohydrate residues
to form glycoproteins.
C. Reactions of SH group
• Cysteine has a sulfhydryl (SH) group and it can form
a disulphide (S-S) bond with another Cysteine
residue.
• The two Cysteine residues can connect to
polypeptide chains by the formation of inter-chain
disulfide bonds or link.
• The dimer formed by two Cysteine residues is called
Dicysteine or cystine.38
40. 4- Special functions of amino acids:
• Gamma aminobutyric acid (GABA), a derivative
of glutamic acid) and dopamine (derived from
tyrosine) are neuro-transmitters.
• Histamine (synthesized from histidine) is the
mediator of allergic reactions.
• Thyroxine (from tyrosine) is an important
thyroid hormone.
40
41. 5- Peptide bond:
• Alpha carboxyl group of one amino acid reacts
with alpha amino group of another amino acid to
form a peptide bond or CO-NH bridge. Proteins
are made by polymerization of amino acids
through peptide bonds.
• Two amino acids combined to form dipeptide.
Three amino acids form tripeptide. Four will
make a tetrapeptide.
41
45. • A few amino acids together will make an
oligopeptide. Combination of 10 to 50 amino acids
is called a polypeptide.
• Big polypeptide chains containing more than 50
amino acids are called proteins.
• Acid hydrolysis (hydrochloric acid at higher
temperature) of peptides bonds will break the
proteins into amino acids. But hydrochloric acid at
body temperature will not break the peptide bonds.
• Thus in the stomach, HCL alone will not be able to
digest proteins; it needs enzymes.
45