Podcast
Questions and Answers
What type of bond is formed between monosaccharides during the creation of disaccharides?
What type of bond is formed between monosaccharides during the creation of disaccharides?
What is the primary sugar found in milk, and what is its composition?
What is the primary sugar found in milk, and what is its composition?
In the context of oligosaccharides, what does the prefix 'oligo' signify?
In the context of oligosaccharides, what does the prefix 'oligo' signify?
Which of the following is NOT a type of disaccharide?
Which of the following is NOT a type of disaccharide?
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What type of glycosidic bond is present in sucrose?
What type of glycosidic bond is present in sucrose?
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Which molecule serves as an intermediate product during the hydrolysis of starch?
Which molecule serves as an intermediate product during the hydrolysis of starch?
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What is the function of oligosaccharides in cells?
What is the function of oligosaccharides in cells?
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Which of the following correctly describes a trisaccharide?
Which of the following correctly describes a trisaccharide?
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Which component is not a part of the structure of starch?
Which component is not a part of the structure of starch?
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What type of bonding is found in both amylose and amylopectin?
What type of bonding is found in both amylose and amylopectin?
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Which is the primary storage polysaccharide in animals?
Which is the primary storage polysaccharide in animals?
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Which of the following statements about glycogen is true?
Which of the following statements about glycogen is true?
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Which of the following best describes glycosaminoglycans (GAGs)?
Which of the following best describes glycosaminoglycans (GAGs)?
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What is chitin primarily composed of?
What is chitin primarily composed of?
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In the context of polysaccharides, what distinguishes structural polysaccharides from storage polysaccharides?
In the context of polysaccharides, what distinguishes structural polysaccharides from storage polysaccharides?
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Which of the following polysaccharides is used as an anticoagulant?
Which of the following polysaccharides is used as an anticoagulant?
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Which describes the structure of proteins?
Which describes the structure of proteins?
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Which of the following is an example of a heteropolysaccharide?
Which of the following is an example of a heteropolysaccharide?
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Which amino acid sequence is classified as a peptide?
Which amino acid sequence is classified as a peptide?
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What type of sugar unit is found in chitin?
What type of sugar unit is found in chitin?
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What is the main function of hyaluronic acid in the body?
What is the main function of hyaluronic acid in the body?
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What distinguishes glycogen from other polysaccharides?
What distinguishes glycogen from other polysaccharides?
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Which function does lipids serve in the body?
Which function does lipids serve in the body?
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What is the structure of chondroitin 6-sulphate made of?
What is the structure of chondroitin 6-sulphate made of?
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What are the main components of verbascose?
What are the main components of verbascose?
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How do oligosaccharides determine blood group types?
How do oligosaccharides determine blood group types?
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What distinguishes storage polysaccharides from structural polysaccharides?
What distinguishes storage polysaccharides from structural polysaccharides?
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Describe the structure of starch.
Describe the structure of starch.
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What defines an aldotetrose?
What defines an aldotetrose?
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What is the primary role of glycogen in the body?
What is the primary role of glycogen in the body?
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Describe one key difference between aldoses and ketoses.
Describe one key difference between aldoses and ketoses.
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Identify a characteristic feature of glycosaminoglycans (GAGs).
Identify a characteristic feature of glycosaminoglycans (GAGs).
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What is the composition of chitin, and why is it significant?
What is the composition of chitin, and why is it significant?
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What is the significance of chiral carbon atoms in monosaccharides?
What is the significance of chiral carbon atoms in monosaccharides?
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How are the names of four and five carbon ketoses formed from their corresponding aldoses?
How are the names of four and five carbon ketoses formed from their corresponding aldoses?
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Can you explain the difference between amylose and amylopectin?
Can you explain the difference between amylose and amylopectin?
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What is the primary function of glucose in human metabolism?
What is the primary function of glucose in human metabolism?
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What are the four major types of macromolecules?
What are the four major types of macromolecules?
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Describe the classification of monosaccharides based on the number of carbon atoms.
Describe the classification of monosaccharides based on the number of carbon atoms.
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Explain the structural difference between glucose and fructose.
Explain the structural difference between glucose and fructose.
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What is the general empirical formula for carbohydrates?
What is the general empirical formula for carbohydrates?
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What role does D-glyceraldehyde play in stereochemistry?
What role does D-glyceraldehyde play in stereochemistry?
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Which monosaccharide has no chiral carbon?
Which monosaccharide has no chiral carbon?
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What characterizes aldo sugars and keto sugars?
What characterizes aldo sugars and keto sugars?
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What is the most common monosaccharide and its formula?
What is the most common monosaccharide and its formula?
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Differentiate between homopolysaccharides and heteropolysaccharides.
Differentiate between homopolysaccharides and heteropolysaccharides.
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What is the primary role of carbohydrates in the body?
What is the primary role of carbohydrates in the body?
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How does the suffix '-ose' relate to carbohydrates?
How does the suffix '-ose' relate to carbohydrates?
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What role do amino acids play in protein formation?
What role do amino acids play in protein formation?
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How does hyaluronic acid contribute to joint function?
How does hyaluronic acid contribute to joint function?
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What is the significance of chitin in crustaceans and insects?
What is the significance of chitin in crustaceans and insects?
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Describe the function of heparin in the human body.
Describe the function of heparin in the human body.
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What are the primary functions of proteins in the body?
What are the primary functions of proteins in the body?
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What distinguishes essential amino acids from non-essential amino acids?
What distinguishes essential amino acids from non-essential amino acids?
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Explain the role of lipids in cellular structure.
Explain the role of lipids in cellular structure.
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What is the structure of chondroitin 6-sulphate composed of?
What is the structure of chondroitin 6-sulphate composed of?
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What are the two main classes of nucleic acids and their primary functions?
What are the two main classes of nucleic acids and their primary functions?
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What distinguishes ribose from deoxyribose in nucleic acids?
What distinguishes ribose from deoxyribose in nucleic acids?
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List the four main types of non-covalent bonding interactions relevant to biological systems.
List the four main types of non-covalent bonding interactions relevant to biological systems.
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What is the basic structure of a nucleotide and its components?
What is the basic structure of a nucleotide and its components?
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Explain why carbon is a crucial element in biological macromolecules.
Explain why carbon is a crucial element in biological macromolecules.
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How do covalent bonds differ from non-covalent interactions in biological macromolecules?
How do covalent bonds differ from non-covalent interactions in biological macromolecules?
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What role do nucleotides play as components of coenzymes?
What role do nucleotides play as components of coenzymes?
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Identify the main types of covalent bonds found in macromolecules.
Identify the main types of covalent bonds found in macromolecules.
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What are the two primary functions of chitin in biological systems?
What are the two primary functions of chitin in biological systems?
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How does hyaluronic acid function in the body, particularly in connective tissues?
How does hyaluronic acid function in the body, particularly in connective tissues?
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What structural units make up chondroitin 6-sulphate and what are its primary applications?
What structural units make up chondroitin 6-sulphate and what are its primary applications?
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What role does heparin play in the human body?
What role does heparin play in the human body?
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Describe how proteins are constructed at a molecular level.
Describe how proteins are constructed at a molecular level.
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What distinguishes essential amino acids from non-essential amino acids?
What distinguishes essential amino acids from non-essential amino acids?
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Explain the process of peptide bond formation.
Explain the process of peptide bond formation.
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How do lipids compare to carbohydrates in terms of energy content?
How do lipids compare to carbohydrates in terms of energy content?
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What are the two main types of polysaccharides and how do they differ in composition?
What are the two main types of polysaccharides and how do they differ in composition?
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Describe the structure and composition of starch with respect to its components.
Describe the structure and composition of starch with respect to its components.
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What is the primary structural feature of glycogen compared to amylopectin?
What is the primary structural feature of glycogen compared to amylopectin?
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Explain what glycosaminoglycans are and give two examples.
Explain what glycosaminoglycans are and give two examples.
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How do oligosaccharides contribute to determining blood group types?
How do oligosaccharides contribute to determining blood group types?
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What characterizes the composition of chitin and its significance in nature?
What characterizes the composition of chitin and its significance in nature?
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What role does fucose play in the composition of the blood group oligosaccharides?
What role does fucose play in the composition of the blood group oligosaccharides?
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Identify the main difference between amylose and amylopectin in terms of structure.
Identify the main difference between amylose and amylopectin in terms of structure.
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What is the significance of hydrogen bonding in proteins?
What is the significance of hydrogen bonding in proteins?
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How do hydrophobic interactions contribute to protein folding?
How do hydrophobic interactions contribute to protein folding?
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Describe the role of hydrogen bonds in the stabilization of DNA's double helix.
Describe the role of hydrogen bonds in the stabilization of DNA's double helix.
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What is the concept of the hydrophobic effect in aqueous solutions?
What is the concept of the hydrophobic effect in aqueous solutions?
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How do van der Waals forces contribute to protein structure?
How do van der Waals forces contribute to protein structure?
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What types of chemical bonds are involved in forming the tertiary structure of proteins?
What types of chemical bonds are involved in forming the tertiary structure of proteins?
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In what way do hydrophilic biomolecules interact with water?
In what way do hydrophilic biomolecules interact with water?
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What is the primary contribution of hydrogen bonds in stabilizing biological molecules?
What is the primary contribution of hydrogen bonds in stabilizing biological molecules?
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What are the basic units of nucleic acids and their significance?
What are the basic units of nucleic acids and their significance?
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Explain the difference between ribose and deoxyribose.
Explain the difference between ribose and deoxyribose.
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What types of chemical bonds are most important in biological macromolecules?
What types of chemical bonds are most important in biological macromolecules?
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What role does carbon play in forming biological macromolecules?
What role does carbon play in forming biological macromolecules?
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What distinguishes covalent bonds from non-covalent interactions in biological systems?
What distinguishes covalent bonds from non-covalent interactions in biological systems?
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Identify two biological roles of nucleotides.
Identify two biological roles of nucleotides.
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Describe the two main classes of nucleic acids.
Describe the two main classes of nucleic acids.
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What is the significance of biological macromolecules in living systems?
What is the significance of biological macromolecules in living systems?
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What type of bond is essential for linking amino acids in proteins?
What type of bond is essential for linking amino acids in proteins?
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How do disulfide bonds contribute to protein structure?
How do disulfide bonds contribute to protein structure?
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What role do non-covalent interactions play in biomolecules?
What role do non-covalent interactions play in biomolecules?
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What is the significance of ionic bonds in proteins?
What is the significance of ionic bonds in proteins?
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Explain the importance of hydrogen bonds in water's properties.
Explain the importance of hydrogen bonds in water's properties.
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What happens during the formation of ionic bonds between amino acids?
What happens during the formation of ionic bonds between amino acids?
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Describe a fundamental characteristic of van der Waals interactions.
Describe a fundamental characteristic of van der Waals interactions.
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In what way do non-covalent interactions assist in protein folding?
In what way do non-covalent interactions assist in protein folding?
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Study Notes
Carbohydrates
- Verbascose is a pentasaccharide made up of 3 galactose units, 1 glucose unit and 1 fructose unit
- ABO blood group substances are oligosaccharides found in most cells and some secretions
- ABO blood group substances are made up of 4 sugars - galactose, N-acetylglucosamine, galactose and fucose
- Fucose is a 6-carbon L-sugar.
Polysaccharides
- Polysaccharides are large molecules containing more than 10 monosaccharide units
- Polysaccharides are joined together by O-glycosidic linkages which can be in a continuous chain or branched
- Storage polysaccharides contain only α- glucose units, for example, starch and glycogen
- Structural polysaccharides contain only β- glucose units, for example, cellulose and chitin.
Starch - Storage Polysaccharide
- Starch is a main food storage molecule in plants
- Starch is a mixture of two polymers - amylose (20%) and amylopectin (80%)
- Amylose is made of glucose units linked by α-1,4 glycosidic bonds
- Amylose is long and unbranched
- Amylopectin is made of glucose units linked by α-1,4 glycosidic bonds in short chains
- Amylopectin is branched every 24–30 glucose units
- Amylopectin branches are formed by α-1,6 glycosidic bonds
Glycogen - Storage Polysaccharide
- Glycogen is a readily mobilized glucose storage form
- Glycogen is a large, branched polymer of glucose residues
- Glycogen can be broken down into glucose when the body needs energy
- Glycogen structure is similar to amylopectin except that α-(1,6) branching occurs every 12 glucose units
Heteropolysaccharides
- Heteropolysaccharides are long, unbranched chains composed of repeating disaccharide units
- Disaccharide units are made of an amino sugar and an acidic sugar
- Amino sugars are either D-acetyl glucosamine or D-galactosamine
- Acidic sugars are either D-glucuronic acid or L-iduronic acid
- Examples of heteropolysaccharides include chitin, hyaluronic acid, chondroitin sulfate, dermatan sulfate, keratan sulfate and heparin.
Chitin
- Chitin is the second most abundant polysaccharide in nature
- Chitin makes up the exoskeletons of crustaceans and insects
- Chitin forms β (1--4) glycosidic bonds between N-acetylglucosamine units
- Chitin is biodegradable and is used as surgical thread
Hyaluronic acid
- Hyaluronic acid is made of long chains of modified glucose units
- Hyaluronic acid is found in synovial fluid (joints), the eye and connective tissues (ligaments, cartilage, skin)
- Hyaluronic acid is viscous, provides lubrication and shock absorption
Chondroitin 6-sulphate
- Chondroitin 6-sulphate is made of repeating disaccharide units of glucuronic acid and N-acetylgalactosamine
- Chondroitin 6-sulphate is found in connective tissues (tendons and cartilage)
- Chondroitin 6-sulphate is used in artificial skin
- Chondroitin 6-sulphate is recommended for the prevention and management of osteoarthritis
Heparin
- Heparin is a polysaccharide polymer composed of 2 monosaccharides - uronic acid and glucosamine
- Heparin is an anticoagulant
- Heparin is used to prevent blood clotting after surgery and in blood sample tubes.
Proteins
- Proteins are large molecules composed of amino acids
- There are 20 different amino acids used to make proteins
- 9 amino acids are essential and must be supplied by food
- 11 amino acids are non-essential and can be made by the body
- Proteins have a wide variety of functions including structural support, enzymes, hormones, antibodies, transport and signal molecules.
Amino Acid Structure
- Amino acids contain an amino group, a carboxyl group and a side chain which differentiates each amino acid
Proteins
- Amino acids are joined together in a specific sequence by peptide bonds
- The sequence of amino acids is determined by DNA
- Two amino acids joined by a peptide bond form a dipeptide
- Short chains of amino acids containing <10 amino acids are called peptides
- Longer chains of amino acids containing up to 50 amino acids are called polypeptides
Peptide Bond Formation
- Peptide bonds are formed by a condensation reaction (removal of water)
Protein Structure
- Proteins have 4 levels of structure: primary, secondary, tertiary, and quaternary
- Primary structure refers to the linear sequence of amino acids
- Secondary structure refers to the local folding of the polypeptide chain, such as alpha-helices and beta-sheets
- Tertiary structure refers to the three-dimensional shape of the polypeptide chain
- Quaternary structure refers to the arrangement of multiple polypeptide chains in a protein complex
Lipids
- Lipids are usually non-polar, hydrophobic, and water insoluble
- Lipids have a diverse structure and a variety of functions
- Lipids contain less oxygen and more C-H bonds than carbohydrates
- Lipids are a significant source of energy, containing twice the energy density as carbohydrates
- Lipids are the constituents of cell membranes and regulate membrane permeability
- Lipids act as shock absorbers for internal organs
- Lipids provide thermal insulation
Galactose
- Galactose is a monosaccharide, a major source is dairy products
- Galactose is a component of lactose (a disaccharide) and glycoproteins
- Galactose is found in brain and nerve tissue
- Galactosemia is a genetic disorder where the body cannot properly metabolize galactose, leading to cataracts due to an enzyme deficiency
Biological Significance of Monosaccharide Stereochemistry
- Most monosaccharides in humans are D-sugars
- L-arabinose and L-fucose are important L-sugars found in plants and mammalian cells, respectively
- Only L-amino acids are used in protein synthesis
Disaccharides
- Disaccharides are formed by condensation/dehydration reactions where a water molecule is removed from two monosaccharides
- The bond formed between two monosaccharides is an O-glycosidic bond
- Disaccharides can be hydrolyzed to form monosaccharides (reverse reaction)
Sucrose
- Sucrose is commonly called table sugar
- Sucrose is composed of a glucose and a fructose unit linked through an α(12)β glycosidic bond
- Sucrose is highly sweet and soluble, not a reducing sugar
Maltose
- Maltose is formed by an α(14) glycosidic linkage between two glucose units
- Maltose is called malt sugar
- Maltose is an intermediate product of starch hydrolysis
Lactose
- Lactose is found exclusively in the milk of mammals
- Lactose is called milk sugar
- Lactose is composed of galactose and glucose units joined by a β (14) glycosidic bond
- Lactose is less sweet and less soluble than sucrose
Oligosaccharides
- Oligosaccharides contain 3 to 10 monosaccharide units
- Oligosaccharides function in cell recognition and cell adhesion
- Oligosaccharides are not commonly found free in cells, but rather covalently attached to proteins and therefore are said to be glycosylated
- Oligosaccharides are linked to proteins by N- or O-glycosidic bonds.
Trisaccharides
- Trisaccharides contain 3 monosaccharide units
- Raffinose is a trisaccharide containing fructose + galactose + glucose
Tetrasaccharides
- Tetrasaccharides contain 4 monosaccharide units
- Stachyose is a tetrasaccharide containing 2 (galactose) + glucose + fructose
Macromolecules
- Large, carbon-based organic molecules
- Created by polymerization of smaller subunits
- Four major types:
- Carbohydrates – monosaccharides
- Proteins – amino acids
- Nucleic acids – nucleotides
- Lipids- no true basic units = fatty acids + glycerol
Carbohydrates
- Primary source of energy
- Oxidation of carbohydrates during respiration yields energy which is stored in ATP and utilized whenever needed
- Structural components (cell membrane)
- Part of backbone of nucleic acids (DNA and RNA)
- Role in cell identification, signaling
Carbohydrate Structure
- Carbohydrates are carbon-based molecules rich in hydroxyl groups
- Most abundant carbohydrate is glucose, C6H12O6
- Glucose is the most important simple carbohydrate in human metabolism
Carbohydrate Classification
-
Monosaccharides: single sugar unit
- Trioses: 3 carbon atoms
- Tetroses: 4 carbon atoms
- Pentoses: 5 carbon atoms
- Hexoses: 6 carbon atoms
- Heptoses: 7 carbon atoms
- Octoses: 8 carbon atoms
- Disaccharides: 2 sugar units
- Oligosaccharides: 3 to 10 sugar units
- Polysaccharides: 10 or more sugar units
- Homopolysaccharides: consist of the same monosaccharides
- Heteropolysaccharides: different monosaccharides
Monosaccharide Structure
- Aldoses: monosaccharides containing aldehyde group
- Ketoses: monosaccharides containing ketone group
- The suffix –ose indicates that a molecule is a ‘sugar’- carbohydrate.
- The prefixes tri-, tetr-, pent- etc indicate the number of carbon atoms in the monosaccharide.
- Glyceraldehyde: an aldotriose
- Dihydroxyacetone: a ketotriose
- Most carbohydrates of interest in human biochemistry are aldohexoses or aldopentoses.
- Four and five carbon ketoses are designated by inserting “ul” into the name of the corresponding aldose. E.g. ribose becomes ribulose (ketose form).
Stereochemistry
- Monosaccharides possess stereogenic centres which are carbon atoms that bind four different groups
- All carbohydrates contain at least one asymmetrical (chiral) carbon, except for dihydroxyacetone
- Glyceraldehyde is used as the standard reference molecule
- Asymmetric carbon atoms confer optical activity
- Rotates polarized light to the right (D)- Dextrorotatory
- Rotates polarized light to the left (L)- Levorotatory
Important Monosaccharides
-
Glucose: Most important simple carbohydrate in human metabolism
- Regulation of blood glucose is important in human health
- Diabetes mellitus
-
Fructose: fruit sugar
- Structural isomer of glucose
- Sweeter than glucose
- Fructose intolerance leads to fructose accumulation and hypoglycaemia
Blood Groups
- ABO substances are oligosaccharides present in most cells of the body and in certain secretions
- On the surface of red blood cells, three different types of oligosaccharides may be found
- Help provide ABO blood group determinants
Polysaccharides
- Large molecules > 10 monosaccharide units
- Joined by O-glycosidic linkages in one continuous chain
- Storage polysaccharides: Contain only α- glucose units (e.g. starch and glycogen)
- Structural polysaccharides: Contain only β- glucose units (e.g. cellulose and chitin)
Starch
- Main food storage molecule of plants
- Mixture of 2 polymers:
- amylose: (20%) – glucose units linked by α-1,4 glycosidic bonds, long and unbranched
- amylopectin: (80%) – glucose units linked in short chains by α-1,4 glycosidic bonds, branched every 24 - 30 glucose units, branches formed by 1,6 glycosidic bonds
Glycogen
- Readily mobilized storage form of glucose
- Large, branched polymer of glucose residues that can be broken down to yield glucose molecules
- Structure is identical to amylopectin, except that the α-(1,6) branching occurs about every 12 glucose units
Heteropolysaccharides
- Commonly called glycosaminoglycans (GAGs) or mucopolysaccharides
- Long, unbranched chains generally composed of a repeating disaccharide unit (amino sugar-acidic sugar)
- Amino sugar: D-acetyl glucosamine or D-galactosamine
- Acidic sugar: D-glucuronic acid or L-iduronic acid
- Examples: chitin, hyaluronic acid, chondroitin sulfate, dermatan sulfate, keratan sulfate and heparin
Chitin
- Second most abundant polysaccharide in nature
- Exoskeleton of crustaceans and insects (e.g. lobsters, beetles and spiders)
- Made of N-acetylglucosamine containing β (1--4) glycosidic bonds
Hyaluronic Acid
- Long chains of modified glucose units are found in synovial fluid in joints, eye and in connective tissues (ligaments, cartilage, skin)
- Viscous molecule that provides lubrication and shock absorption
Chondroitin 6-sulfate
- Repeating disaccharide units composed of glucuronic acid and N-acetylgalactosamine
- Chains are found in connective tissues, tendons and cartilage
Heparin
- Polysaccharide polymer consisting of 2 types of monosaccharides: uronic acid and glucosamine
- Anticoagulant used in preventing blood clotting after surgery and in blood sample tubes.
Proteins
- Large complex molecules composed of amino acids
- 20 different amino acids used to make proteins:
- essential (9): must be supplied by food
- non-essential (11): can be made in the body
-
Functions:
- Structural components- building blocks of muscle, bone, skin and hair
- Enzymes, hormones, antibodies, transport and signal molecules
Amino Acid Structure
- All amino acids share a common structure with:
- A central carbon atom (alpha carbon)
- An amino group (-NH2)
- A carboxyl group (-COOH)
- A hydrogen atom (-H)
- A side chain (‘R’ group), which is unique to each amino acid.
Peptide Bonds
- Amino acids are linked together in a specific sequence by peptide bonds
- The sequence of amino acids is determined by DNA
- Dipeptide: 2 amino acids (1 peptide bond)
- Peptides: short chains of amino acids, generally containing fewer than 10 amino acids
- Polypeptides: Longer chains of amino acids up to 50 amino acids
Protein Structure
- Primary structure: Linear sequence of amino acids
- Secondary structure: Folding of the polypeptide chain, includes alpha helices and beta sheets
- Tertiary structure: 3D shape of the polypeptide chain, formed by interactions between side chains
- Quaternary structure: Arises from the association of two or more polypeptide chains
Lipids
- Usually non-polar, hydrophobic, water insoluble substances of diverse structure
- Significant source of energy: contain twice the energy content as carbohydrates
- Constituents of cell membranes
- Regulate membrane permeability
- Shock absorbers for internal organs
- Thermal insulation
Nucleic Acids
- Biopolymers that are essential to all forms of life
- Two main classes:
- DNA (deoxyribonucleic acid)
- RNA (ribonucleic acid)
- Basic units of nucleic acids are nucleotides
-
Biological Role of Nucleotides:
- Genetic information
- Energy carrier (eg.ATP and GTP)
- Components of co-enzymes (eg.NAD and FAD)
- Signal transduction
Nucleic Acid Building Blocks
- Nucleotide: consists of a phosphate group – sugar molecule – nitrogenous base
- DNA: sugar molecule is deoxyribose
- RNA: sugar molecule is ribose
Chemical Bonding
- All life forms are based on the bonding properties of carbon
- Carbon forms stable bonds with itself and other atoms such as hydrogen (H), nitrogen (N) and oxygen (O)
Types of Chemical Bonds
-
Covalent bonds: Atoms with relatively similar electronegativities share electrons between them
- Peptide (amide bonds): link amino acids in proteins
- Disulfide bonds: form between cysteine residues in proteins
-
Non-covalent bonds: Weaker than covalent bonds, important in maintaining structure and function
- Ionic bonds: occur between charged molecules
- Hydrogen bonds: interactions between a hydrogen atom and a highly electronegative atom (e.g. oxygen or nitrogen)
- Hydrophobic interactions: tendency of non-polar molecules to cluster together in aqueous environments
- van der Waals forces: weak, temporary attractions between molecules
### Importance of Chemical Bonding
- Macromolecules are held together by strong intramolecular forces such as covalent bonds
- Biological structures and processes depend on the interplay of these two interactions: covalent bonds and non-covalent interactions
Carbohydrates
- Verbascose is composed of 3 galactose molecules, 1 glucose molecule, and 1 fructose molecule.
- ABO substances are oligosaccharides found in most cells and secretions.
- ABO blood group determinants are formed by 3 different types of oligosaccharides, each with a chain of 4 sugars.
- All ABO blood group determinants are made up of galactose, N-acetylglucosamine, and fucose.
- Fucose is a 6-carbon L-sugar.
- Polysaccharides are large molecules containing 10 or more monosaccharides linked by O-glycosidic bonds.
- Starch is a storage polysaccharide composed of α -glucose units.
- Starch is a mixture of amylose (20%) and amylopectin (80%).
- Amylose is a long, unbranched chain of glucose units linked by α-1,4 glycosidic bonds.
- Amylopectin contains short chains of glucose units linked by α-1,4 glycosidic bonds with branches every 24-30 glucose units, formed by 1,6 glycosidic bonds.
- Glycogen is a storage form of glucose in animals and contains large, branched polymers of glucose residues.
- Glycogen's structure is similar to amylopectin but with α-(1,6) branching occurring every 12 glucose units.
- Heteropolysaccharides are composed of repeating disaccharide units.
- Common examples of heteropolysaccharides are glycosaminoglycans or mucopolysaccharides.
- Glycosaminoglycans are long, unbranched chains with a repeating disaccharide unit of an amino sugar (D-acetyl glucosamine or D-galactosamine) and an acidic sugar (D-glucuronic acid or L-iduronic acid).
- Examples of heteropolysaccharides include: chitin, hyaluronic acid, chondroitin sulfate, dermatan sulfate, keratan sulfate, and heparin.
- Chitin is the second most abundant polysaccharide in nature and makes up the exoskeletons of crustaceans and insects.
- Hyaluronic acid is found in synovial fluid, eyes, and connective tissues and provides lubrication and shock absorption.
- Chondroitin 6-sulphate is found in connective tissues, tendons, and cartilage and is used in artificial skin.
- Heparin is an anticoagulant used to prevent blood clotting.
Proteins
- Proteins are large, complex molecules made up of amino acids.
- There are 20 different amino acids used to make proteins.
- 9 amino acids are essential, meaning they must be obtained from food.
- 11 amino acids are non-essential, meaning they can be made by the body.
- Proteins have various functions including:
- Structural components of muscle, bone, skin, and hair.
- Act as enzymes, hormones, antibodies, transport, and signal molecules.
- Amino acids are linked together by peptide bonds, forming dipeptides, tripeptides, and polypeptides.
- The sequence of amino acids in a protein is determined by DNA.
- Peptide bonds are formed by a condensation reaction, meaning a water molecule is removed.
Lipids
- Lipids are non-polar, hydrophobic, water-insoluble molecules with diverse structures and functions.
- Lipids have fewer oxygen molecules and more C-H bonds than carbohydrates.
- Lipids are a significant source of energy, containing twice the energy content of carbohydrates.
- Lipids are components of cell membranes and regulate membrane permeability.
- Lipids act as shock absorbers for internal organs and provide thermal insulation.
Nucleic Acids
- Nucleic acids are biopolymers essential for all forms of life.
- Nucleic acids direct cellular activities such as cell division and protein synthesis.
- The two main classes of nucleic acids are DNA (deoxyribonucleic acid) and RNA (ribonucleic acid).
- The basic units of nucleic acids are nucleotides.
- Nucleotides have biological roles:
- Store genetic information.
- Carry energy (e.g., ATP, GTP).
- Components of coenzymes (e.g., NAD, FAD).
- Involved in signal transduction.
Chemical Bonding
- Carbon is an important element in biological systems due to its ability to form stable bonds with itself and other atoms such as hydrogen, nitrogen, and oxygen.
- Biological macromolecules are organic and contain carbon.
- Chemical bonding is the lasting attraction between atoms, ions, or molecules that enables the formation of chemical compounds.
- Chemical bonds result from electrostatic forces of attraction between oppositely charged ions (ionic bonds) or from the sharing of electrons (covalent bonds).
- Covalent bonds and non-covalent interactions are important in living systems.
Main Types of Chemical Bonding in Macromolecules
-
Covalent Bonds:
- Peptide (amide) bonds: Link amino acids together in proteins.
- Disulfide bonds: Formed between two cysteine residues, holding together polypeptide chains (inter-chain bonding) or within a single chain (intra-chain bonding).
-
Non-covalent Bonds:
- Ionic bonds: Result from the attraction between oppositely charged ions.
- Hydrogen bonds: Occur between a hydrogen atom of one molecule and an electronegative atom of another molecule (usually nitrogen, oxygen, or fluorine).
- Hydrophobic interactions: Non-polar molecules aggregate in an aqueous solution, excluding water molecules.
- van der Waals forces: Weak attractions between neutral molecules in close proximity.
Chemical Bonding in Proteins
- Proteins are held together by strong intramolecular forces such as covalent and non-covalent bonds.
- Peptide bonds create the primary structure of proteins.
- Hydrogen bonds contribute to secondary and tertiary structures.
- Ionic attractions/bonds contribute to tertiary structure.
- Hydrophobic and hydrophilic interactions contribute to tertiary structure.
- Disulfide bridges contribute to tertiary structure.
- Quaternary structure is dependent on tertiary structure.
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Explore the fascinating world of carbohydrates, including their structure and function. This quiz covers essential topics such as pentasaccharides, oligosaccharides, and the properties of starch and polysaccharides. Test your knowledge on molecular types and their biochemical roles.