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Questions and Answers
The ______ molecules are the small molecules with molecular weight less than 1000 daltons.
The ______ molecules are the small molecules with molecular weight less than 1000 daltons.
Micromolecules
The ______ are the large molecules that have molecular weight above 1000 daltons.
The ______ are the large molecules that have molecular weight above 1000 daltons.
Macromolecules
_______ are biomolecules that are produced in the metabolic reaction of the body.
_______ are biomolecules that are produced in the metabolic reaction of the body.
Metabolites
Which of the following are examples of primary metabolites?
Which of the following are examples of primary metabolites?
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Which of the following are examples of secondary metabolites?
Which of the following are examples of secondary metabolites?
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The experiment, to prove that living cells have inorganic elements uses the dry weight or wet weight of the tissue sample.
The experiment, to prove that living cells have inorganic elements uses the dry weight or wet weight of the tissue sample.
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Which of the following is a common feature of all amino acids?
Which of the following is a common feature of all amino acids?
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Based on the number of amino and carboxyl groups, amino acids can be divided into how many types?
Based on the number of amino and carboxyl groups, amino acids can be divided into how many types?
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Which type of amino acids cannot be synthesized by the human body?
Which type of amino acids cannot be synthesized by the human body?
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Which of the following is NOT an essential amino acid?
Which of the following is NOT an essential amino acid?
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Amino acids can act as amphoteric species.
Amino acids can act as amphoteric species.
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What is the simplest amino acid?
What is the simplest amino acid?
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Proteins are long chains of amino acids linked together by peptide bonds.
Proteins are long chains of amino acids linked together by peptide bonds.
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Which level of protein structure describes the linear sequence of amino acids?
Which level of protein structure describes the linear sequence of amino acids?
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Which of the following types of bonds is NOT involved in the formation of tertiary protein structure?
Which of the following types of bonds is NOT involved in the formation of tertiary protein structure?
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Quaternary structure is present in all proteins.
Quaternary structure is present in all proteins.
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Which type of protein structure is most stable?
Which type of protein structure is most stable?
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Carbohydrates are organic compounds made up of carbon, hydrogen, and oxygen in the ratio 1:2:1
Carbohydrates are organic compounds made up of carbon, hydrogen, and oxygen in the ratio 1:2:1
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Which of the following is NOT a monosaccharide?
Which of the following is NOT a monosaccharide?
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Which of the following is a disaccharide?
Which of the following is a disaccharide?
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Study Notes
Biomolecules
- Biomolecules are carbon-containing compounds found in living organisms
- Divided into inorganic (water, minerals, CO₂) and organic (carbohydrates, lipids, nucleic acids)
- Chemical analysis of living tissue involves grinding, filtering, and separating components into filtrate (acid-soluble) and residue (acid-insoluble) fractions
How to Analyze Chemical Composition of Living Tissue
- Grind the tissue to obtain a slurry.
- Filter the slurry through cheesecloth or cotton.
- Separate the filtrate and residue.
- Filtrate contains low-molecular-weight molecules (18-800 Daltons), including proteins, peptides, and sugars.
- Residue contains high-molecular-weight molecules (above 10,000 Daltons), including proteins, nucleic acids, polysaccharides, and lipids.
Types of Biomolecules based on Molecular Weight
- Micromolecules: Low molecular weight (less than 1000 Daltons), found in filtrate. Include amino acids, nucleotides, monosaccharides, and fatty acids.
- Macromolecules: High molecular weight (above 1000 Daltons), found in residue. Include carbohydrates, proteins, nucleic acids, and lipids
Metabolites
- Metabolites are biomolecules involved in metabolic reactions.
- Primary metabolites: Have identifiable functions in normal body processes (e.g., amino acids, proteins, nucleic acids).
- Secondary metabolites: Not directly involved in primary body functions, but can have roles in plant development, defense, or signaling (e.g., alkaloids, terpenoids, pigments).
Experiment to Prove Inorganic Elements in Living Cells
- Take a sample of living tissue (like a leaf).
- Dry the tissue sample.
- Burn the tissue (heat it until all water evaporates).
- The residue is the ash, which contains inorganic elements.
Amino Acids
- Amino acids are organic compounds containing an amino group (-NH₂) and a carboxyl group (-COOH).
- Twenty different amino acid types exist, each distinguished by the R group or side chain.
- Classified based on properties of R-group (basic, acidic, polar, nonpolar).
- 10 essential amino acids are not produced by the body and must be obtained through diet.
Properties of Amino Acids
- Amphoteric properties: Can act as either an acid or a base.
- Zwitterion formation: Can exist as dipolar ions (ionized form)
Types of Proteins
- Proteins are polymers of amino acids linked by peptide bonds.
- Primary structure: Linear sequence of amino acids.
- Secondary structure: Local folding of the polypeptide chain (alpha helix or beta sheet), stabilized by hydrogen bonds.
- Tertiary structure: 3D arrangement of the polypeptide chain, stabilized by various interactions (hydrogen bonds, disulfide bonds, hydrophobic interactions).
- Quaternary structure: Arrangement of multiple polypeptide chains in a protein.
Carbohydrates
- Carbohydrates are organic compounds composed of carbon, hydrogen, and oxygen with a general formula (CH₂O)ₙ.
- Classified into monosaccharides (single units), oligosaccharides (short chains), and polysaccharides (long chains).
- Monosaccharides: Simple sugars like glucose, fructose, and galactose.
- Oligosaccharides: Short chains of monosaccharides linked by glycosidic bonds(e.g., sucrose, lactose, maltose).
- Polysaccharides: Long chains of monosaccharides (e.g., starch, cellulose, glycogen).
Monosaccharides
- Have general formula (CH₂O)ₙ where n ranges from 3 to 7.
- Can be straight chain or ring structures.
- Examples include glucose, fructose, and ribose.
Oligosaccharides
- Formed by linking 2-8 monosaccharides.
- Examples include sucrose, lactose, and maltose.
Polysaccharides
- Formed by linking many monosaccharides via glycosidic bonds.
- Examples include starch, cellulose, and glycogen.
Nucleic Acids
- Nucleic acids are polymers of nucleotides, which are composed of a nitrogenous base, a pentose sugar, and a phosphate group.
- Two types exist: DNA and RNA.
- Structure includes: Pentose Sugar, N-base, PO₄.
Lipids
- Lipids are a diverse group of hydrophobic molecules, insoluble in water.
- Classified into simple lipids, conjugated lipids, and derived lipids.
- Simple lipids: Made up only of fatty acids and alcohol (e.g., triglycerides).
- Conjugated lipids: Contain additional groups like phosphate or carbohydrates (e.g. phospholipids, glycolipids).
- Derived lipids: Derived from other lipids (e.g., cholesterol, steroids).
Enzymes
- Enzymes are biological catalysts that accelerate chemical reactions in living organisms.
- Composed primarily of proteins (many are composed of protein as well as cofactors).
- Enzymes have specific active sites where substrates bind and reactions occur.
- Enzymes are essential for all the metabolic processes in a living organisms.
- Different factors, including temperature, pH, and substrate concentration, affect enzyme activity.
Rate of Reaction
- The rate of reaction is the speed at which products are formed or reactants are consumed per unit of time.
- Enzymes accelerate reactions by lowering the activation energy, the energy required for a reaction to proceed.
- The rate of reaction is affected by factors like temperature, pH, substrate concentration, and enzyme concentration.
Catalyzed Reaction
- Reaction where rate is enhanced by enzymes.
- Enzymes reduce the activation energy to enable a faster rate of reaction.
Enzyme Inhibition
- Enjyme inhibition is the decrease in the rate of catalysis by an enzyme as a result of the presence of an inhibitor.
- Competitive inhibition: Inhibitor competes with the substrate for the active site of the enzyme.
- Non-competitive inhibition: Inhibitor binds to a site other than the active site, changing the enzyme's conformation and reducing its activity.
Classification of Enzymes
- Oxidoreductases: Catalyze oxidation-reduction reactions.
- Transferases: Catalyze the transfer of a group from one molecule to another.
- Hydrolases: Catalyze the hydrolysis of a substrate.
- Lyases: Catalyze the breakage of a substrate.
- Isomerases: Catalyze the isomerization of a substrate.
- Ligases: Catalyze the joining of two molecules.
Co-factors
- Non-protein components that bind to enzymes to assist in catalysis.
- Prosthetic groups: Tightly bound, organic molecules.
- Co-enzymes: Loosely bound, organic molecules (e.g., vitamins).
- Metal ions: Inorganic ions (e.g., zinc, magnesium).
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