This document discusses the four major types of organic compounds found in living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the structure and functions of each compound. Carbohydrates such as glucose provide energy, while lipids store energy and form cell membranes. Proteins have a variety of functions including maintaining cell shape and catalyzing reactions. Nucleic acids like DNA and RNA pass on traits by coding for amino acids and assembling proteins. Carbon is essential to life because it can form the large complex molecules that make up living organisms.
1) Enzymes are biological catalysts that regulate specific metabolic functions in the body. They are water soluble, colloidal proteins that speed up biochemical reactions without being consumed in the process.
2) Enzymes can be classified based on their chemistry. Pure protein enzymes are called apoenzymes, while conjugated protein enzymes contain both an apoenzyme portion and a non-protein cofactor or prosthetic group to form the active holoenzyme.
3) Enzyme activity is affected by substrate concentration, temperature, pH, and enzyme concentration according to Michaelis-Menten kinetics and induced fit or lock-and-key mechanisms of enzyme-substrate binding.
Lipids are a heterogeneous group of organic compounds that are insoluble in water but soluble in organic solvents. They serve many important functions in the body including as structural components of cell membranes, storage of metabolic energy, transport of fat-soluble vitamins and hormones, and protection and insulation. Lipids are classified based on the presence or absence of glycerol and other components. Major classes of lipids include fatty acids, triglycerides, phospholipids, sphingolipids, sterols such as cholesterol and vitamin D, and other compounds like prostaglandins.
Here I have tried to cover the following terms--Enzymes, Definition of enzymes, properties of enzymes, substrates, cofactors, coenzymes, functions of cofactors and coenzmes, water soluble vitamins as coenzymes, definition of active site, features of active site, unit of enzyme
The document defines key terms related to enzymes including substrate, active site, and cofactors. It describes the lock and key and induced fit models of how enzymes bind to substrates. Environmental factors like temperature, pH, and substrate concentration can affect the rate of enzymatic reactions. Cofactors and coenzymes are required for some enzymatic reactions. Competitive and noncompetitive inhibitors can regulate enzyme activity. Examples are given of enzymatic uses in industry, detergents, food, and diagnosing/treating diseases.
Enzymes are biological catalysts that increase the rate of chemical reactions without being used up. They are proteins folded into complex shapes with active sites that substrates fit into like locks and keys. Enzymes are usually named for their substrates with the ending "-ase", such as lipase and proteases. Enzymes have five key characteristics: they are always proteins, are specific to reactions, can be reused, are denatured at 50°C, and have optimal pH levels. They are made inside cells and can work inside or outside of cells to speed chemical reactions. Enzymes are widely used in industry due to their ability to work at low temperatures and only be needed in small amounts.
Enzymes have several key properties including their catalytic property, specificity, reversibility, and sensitivity to heat and pH. They act as catalysts in biochemical reactions, only affecting their specific substrates, and can operate reversibly or irreversibly depending on conditions. An enzyme's activity is also dependent on factors like temperature and acidity levels.
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They work by lowering the activation energy of reactions. Enzymes have specific active sites that bind substrates and induce a conformational change through induced fit. This allows the enzyme to accelerate the reaction and produce products. The rate of enzyme reactions can be affected by environmental factors like temperature, pH, and concentrations of enzymes and substrates.
This document discusses enzymes and enzyme kinetics. It defines enzymes as biological catalysts that accelerate biochemical reactions. Enzymes have three main properties - catalytic power, specificity, and regulation. The document describes enzyme classification systems, cofactors, factors that affect enzyme activity like temperature and pH, enzyme inhibition, and models of enzyme action including lock-and-key and induced fit. It also discusses enzyme kinetics concepts such as Michaelis-Menten kinetics, activation energy, and Gibbs free energy.
1) Enzymes are biological catalysts that regulate specific metabolic functions in the body. They are water soluble, colloidal proteins that speed up biochemical reactions without being consumed in the process.
2) Enzymes can be classified based on their chemistry. Pure protein enzymes are called apoenzymes, while conjugated protein enzymes contain both an apoenzyme portion and a non-protein cofactor or prosthetic group to form the active holoenzyme.
3) Enzyme activity is affected by substrate concentration, temperature, pH, and enzyme concentration according to Michaelis-Menten kinetics and induced fit or lock-and-key mechanisms of enzyme-substrate binding.
Lipids are a heterogeneous group of organic compounds that are insoluble in water but soluble in organic solvents. They serve many important functions in the body including as structural components of cell membranes, storage of metabolic energy, transport of fat-soluble vitamins and hormones, and protection and insulation. Lipids are classified based on the presence or absence of glycerol and other components. Major classes of lipids include fatty acids, triglycerides, phospholipids, sphingolipids, sterols such as cholesterol and vitamin D, and other compounds like prostaglandins.
Here I have tried to cover the following terms--Enzymes, Definition of enzymes, properties of enzymes, substrates, cofactors, coenzymes, functions of cofactors and coenzmes, water soluble vitamins as coenzymes, definition of active site, features of active site, unit of enzyme
The document defines key terms related to enzymes including substrate, active site, and cofactors. It describes the lock and key and induced fit models of how enzymes bind to substrates. Environmental factors like temperature, pH, and substrate concentration can affect the rate of enzymatic reactions. Cofactors and coenzymes are required for some enzymatic reactions. Competitive and noncompetitive inhibitors can regulate enzyme activity. Examples are given of enzymatic uses in industry, detergents, food, and diagnosing/treating diseases.
Enzymes are biological catalysts that increase the rate of chemical reactions without being used up. They are proteins folded into complex shapes with active sites that substrates fit into like locks and keys. Enzymes are usually named for their substrates with the ending "-ase", such as lipase and proteases. Enzymes have five key characteristics: they are always proteins, are specific to reactions, can be reused, are denatured at 50°C, and have optimal pH levels. They are made inside cells and can work inside or outside of cells to speed chemical reactions. Enzymes are widely used in industry due to their ability to work at low temperatures and only be needed in small amounts.
Enzymes have several key properties including their catalytic property, specificity, reversibility, and sensitivity to heat and pH. They act as catalysts in biochemical reactions, only affecting their specific substrates, and can operate reversibly or irreversibly depending on conditions. An enzyme's activity is also dependent on factors like temperature and acidity levels.
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They work by lowering the activation energy of reactions. Enzymes have specific active sites that bind substrates and induce a conformational change through induced fit. This allows the enzyme to accelerate the reaction and produce products. The rate of enzyme reactions can be affected by environmental factors like temperature, pH, and concentrations of enzymes and substrates.
This document discusses enzymes and enzyme kinetics. It defines enzymes as biological catalysts that accelerate biochemical reactions. Enzymes have three main properties - catalytic power, specificity, and regulation. The document describes enzyme classification systems, cofactors, factors that affect enzyme activity like temperature and pH, enzyme inhibition, and models of enzyme action including lock-and-key and induced fit. It also discusses enzyme kinetics concepts such as Michaelis-Menten kinetics, activation energy, and Gibbs free energy.
This document provides an overview of carbohydrate chemistry. It defines carbohydrates and discusses their classification, including monosaccharides, disaccharides, and polysaccharides. Key topics include the structures of common monosaccharides like glucose and fructose, as well as their properties including isomerism, stereoisomerism, and mutarotation. Common reactions of monosaccharides such as reduction, oxidation, and glycoside formation are also summarized. The document concludes with brief discussions of important disaccharides like sucrose and lactose, as well as polysaccharides including starch, glycogen, and cellulose.
This document provides an overview of carbohydrate structure and metabolism. It defines carbohydrates and discusses their classification as monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Key monosaccharides like glucose, fructose and galactose are described. The document also covers carbohydrate isomerism, glycosidic linkages in disaccharides and polysaccharides, and structural features of important polysaccharides like starch, glycogen and cellulose. Carbohydrate metabolism and roles in the body are also summarized.
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They have binding sites called active sites that substrates fit into, forming enzyme-substrate complexes. All known enzymes are proteins except for some RNA enzymes. Enzymes require cofactors like coenzymes, prosthetic groups, or metal ions to function and exhibit varying degrees of specificity. They are named based on their substrates or reactions and have standardized EC numbers denoting their class and function. The first isolated and characterized enzyme was urease in 1926, proving enzymes are proteins.
Enzymes are biological molecules (typically proteins) that significantly speed up the rate of virtually all of the chemical reactions that take place within cells. They are vital for life and serve a wide range of important functions in the body, such as aiding in digestion and metabolism
Enzymes are proteins that act as biological catalysts, speeding up chemical reactions without being used up. They work via a "lock and key" mechanism, though the induced fit model suggests enzymes are flexible. Enzyme activity can be measured by looking at reaction rates under different temperatures, pH levels, enzyme and substrate concentrations. Heating an enzyme above its optimal temperature can cause it to denature, changing its shape so the active site no longer fits the substrate. Many enzymes are used industrially in washing powders, food processing, and antibiotic production.
Enzymes are proteins that catalyze chemical reactions by lowering activation energy. They are not consumed in reactions and can catalyze numerous reaction cycles. Nearly all biological reactions require enzyme catalysis. Enzymes contain active sites that bind specific substrates. The binding forms an enzyme-substrate complex that undergoes reaction, producing products. Cofactors like vitamins and ions can bind enzymes and are required for catalytic activity. The active site is a pocket formed by spatially distant amino acids that binds substrates and performs catalysis. Enzymes are measured in units describing their catalytic activity rate.
1. Enzymes are biologic catalysts that are proteins and increase the rate of chemical reactions without being consumed.
2. Enzymes act through specific active sites and have optimal temperatures, pH levels, and substrate concentrations for activity.
3. Enzyme activity can be regulated by activators or inhibited by various types of inhibitors like competitive or irreversible inhibitors.
This document provides an introduction to biochemistry. It begins by defining biochemistry as the science concerned with the chemical nature of living matter. Biochemistry has two branches - descriptive biochemistry which qualitatively and quantitatively characterizes cell components, and dynamic biochemistry which elucidates the nature and mechanisms of reactions between these components. The document then discusses the hierarchy of molecular organization within cells from basic precursors to macromolecules and organelles. It provides details on the structure and functions of prokaryotic and eukaryotic cells as well as some of the major organelles found in eukaryotic cells like the plasma membrane, cytoskeleton, and cytoplasm.
This slide share is related to the "ENZYMES" and explains all the features of enzyme, characteristics, properties, types ,factors affecting, inhibitors, and functioning of enzymes. it is a great effort i hope u will get benefit.
Enzymes are proteins that act as biological catalysts, regulating the rate of chemical reactions in living organisms. They accelerate reactions by lowering the activation energy without being consumed in the process. Enzymes are highly specific and each enzyme catalyzes only one type of reaction. They are affected by factors like temperature, pH, and substrate concentration. The active site of the enzyme binds specifically to substrates and catalyzes the conversion of substrates to products. Enzymes play essential roles in processes like digestion, cellular metabolism, and protection against pathogens.
This document provides an overview of enzymes. It discusses that enzymes are biological catalysts that speed up chemical reactions without being used up. The active site of the enzyme is responsible for its catalytic action. Enzymes are highly specific and their activity is closely regulated. Enzyme activity depends on factors like temperature, pH, substrate and inhibitor concentrations. Measurement of plasma enzyme levels can help diagnose conditions like heart attacks and liver disease. Isozymes are variants of the same enzyme that serve diagnostic purposes.
Nucleic acids like DNA and RNA are composed of nucleotides, which contain a nitrogenous base (purine or pyrimidine), a 5-carbon sugar (ribose or deoxyribose), and one or more phosphate groups. Friedrich Miescher first isolated nucleic acids in 1869. DNA exists as a double-stranded helical structure, with the bases on one strand bonding with complementary bases on the other strand. The sugar-phosphate backbone of DNA contains alternating sugar and phosphate groups and runs in the same direction on both strands.
Monosaccharides are simple sugars with 3 to 7 carbons that are sweet in taste and cannot be further broken down. They include trioses like glyceraldehyde, pentoses that form the backbone of nucleic acids and polysaccharides, and hexoses such as glucose and fructose. Glucose is an important energy source for the body and precursor to cellulose, glycogen and starch. Fructose is sweeter than glucose and found naturally in fruits.
This document discusses amino acids, peptides, and proteins. It begins by defining them as monomers (amino acids), polymers of a few monomers (peptides), and polymers of many monomers (proteins). It then covers the structures and properties of amino acids, including the 20 that are found in proteins. Peptide bond formation is explained as linking amino acids together. Various proteins are classified and examples given, including simple proteins like albumins and globulins, and structural proteins like keratins, collagens, and elastins. The roles and importance of proteins in the body are also summarized.
Enzymes are proteins that act as biological catalysts to speed up biochemical reactions. They are classified based on the type of reaction they catalyze and have a complex three-dimensional globular structure. Enzymes specifically bind to substrates through their active sites to lower the activation energy of reactions, speeding up the formation of products. The mechanism of enzyme action was originally proposed to be lock-and-key binding, but is now understood to involve induced fit, where the enzyme and substrate mutually adjust their shapes for catalysis. Enzymes can be regulated by various factors like substrate concentration, temperature, pH, inhibitors, and activators.
Isomers are compounds that have the same molecular formula but different structural or spatial arrangements. There are several types of isomers including structural isomers, stereoisomers, and optical isomers. Structural isomers have the same atoms bonded differently. Stereoisomers have the same bonding but different 3D orientations. Optical isomers cannot be superimposed and rotate plane-polarized light in opposite directions. Isomers are important in drug development and biological processes because evolution favors specific isomer forms for functions. The structures and positions of groups in isomers strongly influence chemistry and pharmaceutical manufacturing.
Enzymes are protein catalysts that lower the activation energy of biochemical reactions without being consumed. They achieve specificity by fitting substrates into their active sites. Enzyme activity is regulated through various mechanisms including feedback inhibition, cofactors, pH, temperature, and allosteric regulation. Inhibitors bind enzymes to reduce their activity, either reversibly or irreversibly. Enzymes have many applications in medicine including diagnostics, analytical tests, and enzyme replacement therapy.
Enzymes (Definition, characteristics, mechanism action, activity, stability) ...Saad Bin Hasan
Definition of enzyme, characteristics of enzyme, function of enzyme, mechanism action of enzyme, differences between enzyme and catalyst, activity of enzymes, stability of enzymes
This document provides information about fatty acids and triglycerides. It discusses the structure, properties, and reactions of fatty acids, including their length, degree of saturation, and location of double bonds. Triglycerides are introduced as esters composed of glycerol and three fatty acid chains. Their physical properties depend on the fatty acid components, and they undergo hydrolysis, saponification, and hydrogenation reactions. The learning outcomes are to understand fatty acids and triglycerides, and distinguish between their physical and chemical properties.
The document discusses the four major organic macromolecules that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the monomers (sugar, fatty acids and glycerol, amino acids, nucleotides) that make up each macromolecule, their structures, functions in the body (energy storage, structure, catalysis etc.), and examples of each type. Carbon is highlighted as the key element in organic compounds due to its ability to form diverse and complex molecules essential for life.
The Chemical Basis for Life---ORGANIC COMPOUNDS (1).pptxMaAnnFuriscal3
This document discusses the four major types of organic compounds that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the monomers (simple units) that make up each type of compound, their structures, functions, and examples. Carbohydrates are made of monosaccharides and function to store and provide energy. Lipids contain fatty acids and glycerol and form cell membranes and store energy. Proteins comprise amino acids and are essential for cell structure, movement, and chemical reactions. Nucleic acids DNA and RNA contain nucleotides and carry genetic instructions.
This document provides an overview of carbohydrate chemistry. It defines carbohydrates and discusses their classification, including monosaccharides, disaccharides, and polysaccharides. Key topics include the structures of common monosaccharides like glucose and fructose, as well as their properties including isomerism, stereoisomerism, and mutarotation. Common reactions of monosaccharides such as reduction, oxidation, and glycoside formation are also summarized. The document concludes with brief discussions of important disaccharides like sucrose and lactose, as well as polysaccharides including starch, glycogen, and cellulose.
This document provides an overview of carbohydrate structure and metabolism. It defines carbohydrates and discusses their classification as monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Key monosaccharides like glucose, fructose and galactose are described. The document also covers carbohydrate isomerism, glycosidic linkages in disaccharides and polysaccharides, and structural features of important polysaccharides like starch, glycogen and cellulose. Carbohydrate metabolism and roles in the body are also summarized.
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They have binding sites called active sites that substrates fit into, forming enzyme-substrate complexes. All known enzymes are proteins except for some RNA enzymes. Enzymes require cofactors like coenzymes, prosthetic groups, or metal ions to function and exhibit varying degrees of specificity. They are named based on their substrates or reactions and have standardized EC numbers denoting their class and function. The first isolated and characterized enzyme was urease in 1926, proving enzymes are proteins.
Enzymes are biological molecules (typically proteins) that significantly speed up the rate of virtually all of the chemical reactions that take place within cells. They are vital for life and serve a wide range of important functions in the body, such as aiding in digestion and metabolism
Enzymes are proteins that act as biological catalysts, speeding up chemical reactions without being used up. They work via a "lock and key" mechanism, though the induced fit model suggests enzymes are flexible. Enzyme activity can be measured by looking at reaction rates under different temperatures, pH levels, enzyme and substrate concentrations. Heating an enzyme above its optimal temperature can cause it to denature, changing its shape so the active site no longer fits the substrate. Many enzymes are used industrially in washing powders, food processing, and antibiotic production.
Enzymes are proteins that catalyze chemical reactions by lowering activation energy. They are not consumed in reactions and can catalyze numerous reaction cycles. Nearly all biological reactions require enzyme catalysis. Enzymes contain active sites that bind specific substrates. The binding forms an enzyme-substrate complex that undergoes reaction, producing products. Cofactors like vitamins and ions can bind enzymes and are required for catalytic activity. The active site is a pocket formed by spatially distant amino acids that binds substrates and performs catalysis. Enzymes are measured in units describing their catalytic activity rate.
1. Enzymes are biologic catalysts that are proteins and increase the rate of chemical reactions without being consumed.
2. Enzymes act through specific active sites and have optimal temperatures, pH levels, and substrate concentrations for activity.
3. Enzyme activity can be regulated by activators or inhibited by various types of inhibitors like competitive or irreversible inhibitors.
This document provides an introduction to biochemistry. It begins by defining biochemistry as the science concerned with the chemical nature of living matter. Biochemistry has two branches - descriptive biochemistry which qualitatively and quantitatively characterizes cell components, and dynamic biochemistry which elucidates the nature and mechanisms of reactions between these components. The document then discusses the hierarchy of molecular organization within cells from basic precursors to macromolecules and organelles. It provides details on the structure and functions of prokaryotic and eukaryotic cells as well as some of the major organelles found in eukaryotic cells like the plasma membrane, cytoskeleton, and cytoplasm.
This slide share is related to the "ENZYMES" and explains all the features of enzyme, characteristics, properties, types ,factors affecting, inhibitors, and functioning of enzymes. it is a great effort i hope u will get benefit.
Enzymes are proteins that act as biological catalysts, regulating the rate of chemical reactions in living organisms. They accelerate reactions by lowering the activation energy without being consumed in the process. Enzymes are highly specific and each enzyme catalyzes only one type of reaction. They are affected by factors like temperature, pH, and substrate concentration. The active site of the enzyme binds specifically to substrates and catalyzes the conversion of substrates to products. Enzymes play essential roles in processes like digestion, cellular metabolism, and protection against pathogens.
This document provides an overview of enzymes. It discusses that enzymes are biological catalysts that speed up chemical reactions without being used up. The active site of the enzyme is responsible for its catalytic action. Enzymes are highly specific and their activity is closely regulated. Enzyme activity depends on factors like temperature, pH, substrate and inhibitor concentrations. Measurement of plasma enzyme levels can help diagnose conditions like heart attacks and liver disease. Isozymes are variants of the same enzyme that serve diagnostic purposes.
Nucleic acids like DNA and RNA are composed of nucleotides, which contain a nitrogenous base (purine or pyrimidine), a 5-carbon sugar (ribose or deoxyribose), and one or more phosphate groups. Friedrich Miescher first isolated nucleic acids in 1869. DNA exists as a double-stranded helical structure, with the bases on one strand bonding with complementary bases on the other strand. The sugar-phosphate backbone of DNA contains alternating sugar and phosphate groups and runs in the same direction on both strands.
Monosaccharides are simple sugars with 3 to 7 carbons that are sweet in taste and cannot be further broken down. They include trioses like glyceraldehyde, pentoses that form the backbone of nucleic acids and polysaccharides, and hexoses such as glucose and fructose. Glucose is an important energy source for the body and precursor to cellulose, glycogen and starch. Fructose is sweeter than glucose and found naturally in fruits.
This document discusses amino acids, peptides, and proteins. It begins by defining them as monomers (amino acids), polymers of a few monomers (peptides), and polymers of many monomers (proteins). It then covers the structures and properties of amino acids, including the 20 that are found in proteins. Peptide bond formation is explained as linking amino acids together. Various proteins are classified and examples given, including simple proteins like albumins and globulins, and structural proteins like keratins, collagens, and elastins. The roles and importance of proteins in the body are also summarized.
Enzymes are proteins that act as biological catalysts to speed up biochemical reactions. They are classified based on the type of reaction they catalyze and have a complex three-dimensional globular structure. Enzymes specifically bind to substrates through their active sites to lower the activation energy of reactions, speeding up the formation of products. The mechanism of enzyme action was originally proposed to be lock-and-key binding, but is now understood to involve induced fit, where the enzyme and substrate mutually adjust their shapes for catalysis. Enzymes can be regulated by various factors like substrate concentration, temperature, pH, inhibitors, and activators.
Isomers are compounds that have the same molecular formula but different structural or spatial arrangements. There are several types of isomers including structural isomers, stereoisomers, and optical isomers. Structural isomers have the same atoms bonded differently. Stereoisomers have the same bonding but different 3D orientations. Optical isomers cannot be superimposed and rotate plane-polarized light in opposite directions. Isomers are important in drug development and biological processes because evolution favors specific isomer forms for functions. The structures and positions of groups in isomers strongly influence chemistry and pharmaceutical manufacturing.
Enzymes are protein catalysts that lower the activation energy of biochemical reactions without being consumed. They achieve specificity by fitting substrates into their active sites. Enzyme activity is regulated through various mechanisms including feedback inhibition, cofactors, pH, temperature, and allosteric regulation. Inhibitors bind enzymes to reduce their activity, either reversibly or irreversibly. Enzymes have many applications in medicine including diagnostics, analytical tests, and enzyme replacement therapy.
Enzymes (Definition, characteristics, mechanism action, activity, stability) ...Saad Bin Hasan
Definition of enzyme, characteristics of enzyme, function of enzyme, mechanism action of enzyme, differences between enzyme and catalyst, activity of enzymes, stability of enzymes
This document provides information about fatty acids and triglycerides. It discusses the structure, properties, and reactions of fatty acids, including their length, degree of saturation, and location of double bonds. Triglycerides are introduced as esters composed of glycerol and three fatty acid chains. Their physical properties depend on the fatty acid components, and they undergo hydrolysis, saponification, and hydrogenation reactions. The learning outcomes are to understand fatty acids and triglycerides, and distinguish between their physical and chemical properties.
The document discusses the four major organic macromolecules that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the monomers (sugar, fatty acids and glycerol, amino acids, nucleotides) that make up each macromolecule, their structures, functions in the body (energy storage, structure, catalysis etc.), and examples of each type. Carbon is highlighted as the key element in organic compounds due to its ability to form diverse and complex molecules essential for life.
The Chemical Basis for Life---ORGANIC COMPOUNDS (1).pptxMaAnnFuriscal3
This document discusses the four major types of organic compounds that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the monomers (simple units) that make up each type of compound, their structures, functions, and examples. Carbohydrates are made of monosaccharides and function to store and provide energy. Lipids contain fatty acids and glycerol and form cell membranes and store energy. Proteins comprise amino acids and are essential for cell structure, movement, and chemical reactions. Nucleic acids DNA and RNA contain nucleotides and carry genetic instructions.
Carbon is essential to life as it can form strong bonds with many other elements, allowing it to combine into the large, complex organic molecules that make up living things. These molecules include carbohydrates, lipids, proteins and nucleic acids. Carbohydrates, lipids and proteins provide energy and structure, while nucleic acids carry genetic instructions and code for proteins.
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS.pptLAZAROAREVALO1
Carbon is essential to life as it can form strong bonds with many other elements, allowing it to combine into the four major organic macromolecules that make up living things: carbohydrates, lipids, proteins, and nucleic acids. Carbohydrates, lipids, and proteins provide energy storage and structural roles, while nucleic acids store and transmit genetic information through DNA and protein synthesis via RNA.
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS.pptWaseemAnwar26
The document summarizes the key organic compounds that make up living things: carbohydrates, lipids, proteins, and nucleic acids. It describes the monomers (simple sugars, fatty acids, amino acids, nucleotides) that combine to form these important macromolecules, and explains their functions in energy storage, structure, and genetic inheritance. Specifically, it outlines the roles of carbohydrates in energy storage and structure, lipids in energy storage and cell membranes, proteins in structure, catalysis and transport, and nucleic acids in coding genetic information.
B.sc. biochemistry sem 1 introduction to biochemistry unit 2 biomoleculesRai University
Proteins, carbohydrates, and lipids are the three main types of biomolecules. Proteins are made of amino acid chains and perform most bodily functions. Carbohydrates are the main energy source and come in simple and complex forms. Lipids include fats, oils, waxes, and other fatty substances that serve as energy stores and membrane components. Nucleic acids DNA and RNA carry genetic information and aid in protein synthesis. Enzymes are protein catalysts that speed up biochemical reactions and have various roles in industrial and biological processes.
Fats and lipids are a diverse group of organic compounds that are insoluble in water but soluble in organic solvents. They incorporate fatty acids, which are long carbon chains with an acidic end. There are several major lipid groups including fats, phospholipids, steroids, and waxes. Fats are lipids with fatty acid tails attached to glycerol, and are solid or liquid depending on whether they are saturated or unsaturated. Phospholipids have two fatty acid tails and a phosphate head, making up cell membranes. Steroids have four carbon rings but no fatty acid tails, and include cholesterol. Waxes are lipids with long fatty acid and alcohol chains that pack tightly.
I have prepare this slide thinking that it will help students .I have collected different photos and videos from internet please comment and if you need any slides for a topics . i will prepare the slide .
Sphingolipids are a class of lipids that contain sphingoid bases like sphingosine. They are found in cell membranes, particularly in brain and nerve tissues. Sphingolipids have a sphingosine backbone connected to a fatty acid and a head group. They play roles in cell signaling and recognition. Types include simple sphingolipids like ceramides and complex glycosphingolipids. Sphingolipids help protect and stabilize cell membranes and may reduce cancer and cholesterol risks.
biological macromolecules large cellular components abundantly obtained naturally and are responsible for varieties of essential functions for the growth and survival of living organisms.
Lipids are organic compounds that are insoluble in water but soluble in organic solvents. They include fats, oils, waxes, sterols and phospholipids. Fats and oils are triglycerides composed of glycerol and fatty acids. Fatty acids are classified as saturated, monounsaturated, or polyunsaturated. Phospholipids are a major component of cell membranes and lipoproteins transport lipids in the blood. Lipids serve important functions as energy stores, insulation, and as precursors to other compounds like hormones and vitamins.
1. The basic chemical components that make up protoplasm, the substance of life, are water, inorganic compounds, carbohydrates, lipids, proteins, and nucleic acids.
2. Water is the most abundant component, making up 60-90% of living organisms. It is crucial for transport and as a universal solvent.
3. Carbohydrates, lipids, proteins, and nucleic acids are organic compounds that contain carbon and provide structure and energy through molecules like glucose, fatty acids, amino acids, and nucleotides.
4. These organic molecules form complex macromolecules through condensation reactions, and carry out essential functions like energy storage, structure, catalysis, and heredity
Carbon compounds are the primary components of living things. There are four main classes: carbohydrates, lipids, proteins, and nucleic acids. Carbohydrates include sugars and starches and are a key energy source. Lipids include fats and phospholipids and function in energy storage and cell membranes. Proteins have many functions including enzymes, structure, and transport. Nucleic acids DNA and RNA contain genetic information and aid in protein production. ATP temporarily stores energy to power cellular functions.
Organic molecules like carbohydrates, lipids, proteins, and nucleic acids are made up of carbon chains and functional groups that allow for great diversity. Carbon forms the backbone of these biomolecules and its ability to form single, double, or triple bonds with other elements allows it to link together into large complex structures. These molecules carry out essential functions in cells like energy storage, structure, metabolism, and information transfer. The specific sequences and structures of proteins and nucleic acids are vital to their roles.
Lipids serve several important functions in the body. They are the structural components of cell membranes and help store energy. Lipids can be classified as simple lipids like fats, oils, and waxes, or complex lipids like phospholipids, glycolipids, and sterols. Membrane lipids include glycerophospholipids, ether lipids, sphingolipids, and cholesterol. Some lipids act as signals, like steroid hormones, eicosanoids, and phospholipid-derived intracellular messengers. Others serve as enzyme cofactors in electron transfer and glycosylation reactions.
Lipids are organic compounds that include fatty acids, glycerides, sphingolipids, and steroids. They can be classified as saponifiable or nonsaponifiable and polar or nonpolar. Saponifiable lipids include triglycerides, phospholipids, and sphingolipids. Nonpolar lipids like triglycerides are used for energy storage while polar lipids form cell membranes. Lipids serve important functions like energy storage, cell signaling, and as structural components of cell membranes. They are broken down into fatty acids and glycerol during digestion and absorbed into the bloodstream within lipoproteins like chylomicrons and HDL/LDL for transport.
- Carbon atoms can form chains and complex structures, allowing for the creation of macromolecules in living things. The four main types of macromolecules are carbohydrates, lipids, nucleic acids, and proteins.
- Carbohydrates and lipids are used to store energy, while nucleic acids store and transmit genetic information in the forms of RNA and DNA. Proteins have a variety of functions including catalyzing reactions, forming structures, and transporting materials.
- All macromolecules are polymers formed via polymerization reactions that link smaller monomer units together. They provide structure, energy storage, heredity, and catalysis essential for life.
Similar to The chemical_basis_for_life---organic_compounds (20)
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His expertise extends across a diverse spectrum of reporting, database, and web development applications, underpinned by an exceptional grasp of data storage and virtualization technologies. His proficiency in application testing, database administration, and data cleansing ensures seamless execution of complex projects.
What sets Denis apart is his comprehensive understanding of Business and Systems Analysis technologies, honed through involvement in all phases of the Software Development Lifecycle (SDLC). From meticulous requirements gathering to precise analysis, innovative design, rigorous development, thorough testing, and successful implementation, he has consistently delivered exceptional results.
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Date: May 29, 2024
Tags: Information Security, ISO/IEC 27001, ISO/IEC 42001, Artificial Intelligence, GDPR
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2. Lesson Objectives
• Explain why carbon is essential to life on Earth.
• Describe the structure and function of
carbohydrates.
• Describe the structure and function of lipids.
• Describe the structure and function of proteins.
• Describe the structure and function of nucleic
acids.
3. Introduction
• Organic compounds are
chemical substances that:
– Make up organisms
– Help organisms carry out life
processes
• All contain the elements carbon & hydrogen
– Carbon is the major element
• Without carbon, life as we know it would cease to exist
4. THE SIGNIFICANCE OF CARBON
• Nearly 10 million carbon-containing organic
compounds are known
• Types of carbon compounds in organisms
include carbohydrates, lipids, proteins, and
nucleic acids
• Carbon can bond with a wide variety of other
elements forming a variety of very large and
complex molecules
– including hydrogen, oxygen, and nitrogen
• Carbon can also bond to other carbons
– may form single, double, or even triple bonds
5. CARBOHYDRATES
• Contain only carbon, hydrogen, and
oxygen
• The most common of the four major types
of organic compounds
• All consist of one or more smaller units
called monosaccharides.
6. Monosaccharides and Disaccharides
(Simple Carbohydrates)
• Common Monosaccharides:
– glucose (C6 H12 O6), fructose (C6 H12 O6)
• Two monosaccharides bonded together form a
disaccharide.
– Sucrose (table sugar)
Both monosaccharides and disaccharides
are known as simple sugars and provide
energy to living cells…
7. Polysaccharides
(Complex Carbohydrates)
• Two or more monosaccharides bond
together, form a carbohydrate called a
polysaccharide
– May contain a few monosaccharides to several
thousand monosaccharides
– Main functions are to store energy and form
structural tissues (cell walls, exoskeletons)
8. The Compounds of Life
Composition
(elements
present)
Function Examples Monomer
Carbohy-
drates
Carbon,
Hydrogen,
and Oxygen
C,H,O
Provide
energy to
living cells;
form
structural
tissue
Glucose
Fructose
Sucrose
Glycogen
Cellulose
Mono-
saccharides
Lipids
Proteins
Nucleic acids
9.
10. “From Sugar to Energy” ;
page 5 of packet
http://
www.kqed.org/quest/television/bio
fuels-beyond-ethanol
11. LIPIDS
• Contain carbon, hydrogen, and oxygen
– include substances such as fats and oils
• Lipid molecules consist of glycerol & 3 fatty acids
– Other types of lipids can contain additional molecules.
• All lipids are hydrophobic; non-polar
• Are they soluble in water???? NO
12. Saturated Fatty Acids
• Saturated fatty acids are solids at room temperature
• Saturated refers to the placement of hydrogen atoms
around the carbon atoms
• Saturated fatty acid, have a COOH group; all the C
atoms (other than the C in the -COOH group) are
bonded to two or more H atoms with single bonds
– they form straight chains
• Structure allows saturated fatty acids to be packed
together tightly; dense storage of chemical energy
– fatty tissues of animals contain mainly saturated fatty acids
13. Unsaturated Fatty Acids
• Unsaturated fatty acids are liquids at room
temperature
• Unsaturated fatty acid, also have a COOH group;
some carbon atoms are not bonded to as many
hydrogen atoms as possible because they are bonded
to one or more additional groups, including double and
triple bonds between carbons
– they cause the chain to bend - do not form straight chains
• Unsaturated fatty acids are found mainly in plants,
especially in fatty tissues such as nuts and seeds.
-- monounsaturated
14. Types of Lipids
• Lipids may consist of fatty acids alone or in
combination with other compounds; several
types of lipids consist of fatty acids combined
with a molecule of alcohol:
– Triglycerides are the main form of stored energy in
animals. This type of lipid is commonly called fat
– Phospholipids are a major component of the
membranes surrounding the cells of all organisms
– Steroids (or sterols) have several functions. The
sterol cholesterol is an important part of cell
membranes and plays other vital roles in the body.
Other steroids are male and female sex hormones
15. Lipids and Diet
• Humans need lipids for many vital functions, such as storing
energy and forming cell membranes; also supply cells with
energy
– a gram of lipids supplies more than twice as much energy as a gram of
carbohydrates or proteins
• Human body can manufacture most of the lipids it needs
• Essential fatty acids, must be consumed in food
– include omega-3 and omega-6 fatty acids
• Excess dietary lipids can be harmful
– lead to unhealthy weight gain
– increase the risk for health problems such
as cardiovascular disease
16. Type of Lipid Characteristics Where found
Triglycerides Main form of stored
energy in animals
vegetable oil (typically more
unsaturated)
animal fats (typically more saturated)
Saturated Form straight chains
b/c carbon atoms are
bonded to as many H
atoms as possible;
store energy in
compact form; solid
at room temperature
Animals use these to store energy
Unsaturated Form bent chains b/c
some C atoms are not
bonded to as many H
atoms as possible;
store energy; liquid at
room temperature
Plants use these to store energy
Phospholipids Major component of
cell membranes
Liver, peanuts
Steroids Serve as chemical
messengers and have
other roles
found in plants, animals, and fungi
17. The Compounds of Life
Composition
(elements
present)
Function Examples Monomer
Carbohy-
drates-
Carbon,
Hydrogen,
and Oxygen
C,H,O
Provide
energy to
living cells;
form
structural
tissue
Glucose
Fructose
Sucrose
Glycogen
Cellulose
Mono-
saccharides
Lipids Carbon,
hydrogen,
and Oxygen
C,H,O
Hydrophobic
--form cell
membranes
Store energy
Fats, Oils,
Waxes,
Steroids
Glycerol &
3 Fatty Acids
(for fats &
oils)
Proteins
Nucleic
acids
18. PROTEINS
• Contain carbon, hydrogen, oxygen, nitrogen
• Made of smaller units called amino acids.
– 20 different common amino acids make proteins
– Small proteins can contain just a few hundred amino
acids.
• Yeast proteins average 466 amino acids.
– The largest known proteins are the titins, found in
muscle, which are composed from almost 27,000 amino
acids.
19. Amino Acid Structure
• Same basic structure
– ‘R’ group; amino
group (NH2); and
carboxyl group
(COOH)
20. Protein Structure
• Amino acids can bond together to form short
chains called peptides or longer chains called
polypeptides
• Protein consists of one or more polypeptide
chains
http://www.stolaf.edu/people/giannini/flashanimat/proteins
/protein%20structure.swf
21. Functions of Proteins
• Essential part of all organisms; that serve many
functions
– provide a scaffolding that maintains the shape of cells
– make up the majority of muscle tissues
– some are enzymes that speed up chemical reactions in cells
– others are antibodies
– Still other help carry messages or materials in and out of cells or
around the body
• Most important traits of proteins, allowing them to carry
out these functions, is their ability to bond with other
molecules. They can bond with other molecules very
specifically and tightly
22. Proteins and Diet
• Proteins in the diet are necessary for life
– Dietary proteins are broken down into their
component amino acids when food is digested
– Cells can then use the components to build new
proteins
• Humans are able to synthesize all but eight of
the twenty common amino acids.
• These eight amino acids, called essential
amino acids, must be consumed in foods
23. Protein Denaturation
• http://www.youtube.com/watch?
v=3IL_Df5ouUc
Definition: the change in the shape of protein
molecules_without _denaturation we could not
eat many delicious foods; _is _necessary for
survival so we can break down proteins we eat
into components our bodies can use;
_changes or halts _the shape of the protein
molecule/cellular function.
Is caused by _extreme conditions—heat, acid
(change of pH), or force____40◦
C________
24. The Compounds of Life
Composition
(elements
present)
Function Examples Monomer
Proteins Carbon,
Hydrogen,
Oxygen, and
Nitrogen
C,H,O,N
Maintain cell
shape; Make
muscle
tissue;
Speed up
chemical
reactions;
Carry
messages
Enzymes
Antibodies
Amino Acid
Nucleic
acids
25. NUCLEIC ACIDS
• Contain carbon, hydrogen, oxygen, nitrogen,
and phosphorus
– made of smaller units called nucleotides.
• Nucleic acids are found not only in all living
cells but also in viruses
• Types of nucleic acids include:
– deoxyribonucleic acid (DNA)
– ribonucleic acid (RNA).
26. Structure of Nucleic Acids
• Consists of one or two chains of nucleotides held together by chemical
bonds
• Each individual nucleotide unit consists of three parts:
• a base (containing nitrogen)
- four bases: Adenine, Guanine, Cytosine, and
Thymine in DNA, or Uracil in RNA
• a sugar
(deoxyribose in DNA, ribose in RNA)
• a phosphate group (containing phosphorus)
• RNA consists of a single chain of nucleotides,
DNA consists of two chains of nucleotides
27. Role of Nucleic Acids
• Order of bases in nucleic acids is highly
significant
– bases are like the letters of a four-letter alphabet
– ‘‘letters” can be combined to form ‘‘words”
– groups of three bases form words of the genetic code
– each code word stands for a different amino acid
– series of many code words spells out the sequence of
amino acids in a protein
• Information is passed from a body cell to its
daughter cells when the cell divides. It is also
passed from parents to their offspring when
organisms reproduce.
28. How RNA codes for Proteins
• DNA and RNA have different functions relating
to the genetic code and proteins
• Like a set of blueprints, DNA contains the
genetic instructions for the correct sequence of
amino acids in proteins
• RNA uses the information in DNA to assemble
the amino acids and make the proteins.
29. The Compounds of Life
Composition
(elements
present)
Function Examples Monomer
Nucleic
acids
Carbon,
Hydrogen,
Oxygen,
Phosphorus,
and Nitrogen
C,H,O,P,N
Pass on
traits
Code for
amino acids
Deoxyribo-
nucleic acid
(DNA)
Ribonucleic
acid (RNA)
Nucleotides
30. Lesson Summary
• Carbon’s exceptional ability to form bonds with other elements and with itself allows it to form
a huge number of large, complex molecules called organic molecules. These molecules make
up organisms and carry out life processes.
• Carbohydrates are organic molecules that consist of carbon, hydrogen, and oxygen. They are
made up of repeating units called saccharides. They provide cells with energy, store energy,
and form structural tissues.
• Lipids are organic compounds that consist of carbon, hydrogen, and oxygen. They are made
up of fatty acids and other compounds. They provide cells with energy, store energy, and help
form cell membranes.
• Proteins are organic compounds that consist of carbon, hydrogen, oxygen, nitrogen, and, in
some cases, sulfur. They are made up of repeating units called amino acids. They provide
cells with energy, form tissues, speed up chemical reactions throughout the body, and perform
many other cellular functions.
• Nucleic acids are organic compounds that consist of carbon, hydrogen, oxygen, nitrogen, and
phosphorus. They are made up of repeating units called nucleotides. They contain genetic
instructions for proteins, help synthesize proteins, and pass genetic instructions on to
daughter cells and offspring.
Editor's Notes
Handout Charts to fill in…..
Another monosaccharide, fructose, has the same chemical formula as glucose, but the atoms are arranged differently. Molecules with the same chemical formula but with atoms in a different arrangement are called isomers.
Compare the glucose and fructose molecules can you identify their differences?.... The only differences are the positions of some of the atoms. These differences affect the properties of the two monosaccharides.
Table 1.2: Complex Carbohydrates
____________________________________________________________________________
Complex Carbohydrate Function Organism
____________________________________________________________________________
Amylose Stores energy Plants
Glycogen Stores energy Animals
Cellulose Forms cell walls Plants
Chitin Forms external skeleton Some animals
These complex carbohydrates play important roles in living organisms.
One double carbon bond means monounsaturated fatty acid
Two or more double bonds means polyunsaturated fatty acid
Omega- 3 in (Coldwater fish like tuna, salmon, lake trout, mackerel, shrimp are rich sources of omega3. Plant sources include flaxseed oil and pumpkin seed oil. Omega 3 fatty acids are highly concentrated in the brain and appear to be particularly important for cognitive and behavioral function. In fact, infants who do not get enough omega 3 fatty acids from their mothers during pregnancy are at risk for developing vision and nerve problems. Omega-3 fatty acids are good for heart. They reduce triglyceride levels, raise levels of HDL (”good”) cholesterol, and manage blood pressure.); Omega- 6 in (Omega-6 fatty acids are beneficial as well. They help regulate inflammation and blood pressure as well as heart, gastrointestinal, and kidney functions. Good dietary sources of omega-6 fatty acids include cereals, eggs, poultry, most vegetable oils, whole-grain breads, baked goods, and margarine.)
The dietary lipids of most concern are saturated fatty acids, trans fats, and cholesterol. For example, cholesterol is the lipid mainly responsible for narrowing arteries and causing the disease atherosclerosis.
Amino acids are molecules containing an amino group (shown here as H2N), a carboxylic acid group and a side chain “R” group that varies between different amino acids
Polypeptides may have as few as 40 amino acids or as many as several thousand.
The order of amino acids, together with the properties of the amino acids, determines the shape of the protein, and the shape of the protein determines the function of the protein. KEY: H = hydrogen, N = nitrogen, C = carbon, O = oxygen, R = variable side chain.
Figure on left: Polypeptide. This polypeptide is a chain made up of many linked amino acids. The amino acid sequence is the primary structure of a protein.
Figure on right: a protein may have up to four levels of structure, from primary to quaternary. The complex structure of a protein allows it to carry out its biological functions.