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SBI4U: Chapter 1 > The Molecules of Life > Flashcards

The Molecules of Life Flashcards

1
Q

What are the 7 organic compounds?

A
  1. Alcohol
  2. Aldehyde
  3. Ketone
  4. Carboxylic Acid
  5. Amine
  6. Thiol
  7. Organic Phosphate
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2
Q

What are the 3 classifications of carbohydrates?

A
  1. Monosaccharides
  2. Oligosaccharides
  3. Polysaccharides
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3
Q

What are monosaccharides and how are they structured? Give examples

A
  • A simple sugar, composed of 5 or more carbon molecules
  • Linear in a dry state
  • Ring structure when in a solution
  • Ex: Glucose, fructose
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4
Q

What are oligosaccharides? Give examples

A
  • 2 or 3 simple sugars linked together by a covalent, glycosidic linkage formed by condensation reactions
  • Ex: Sucrose, maltose
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5
Q

What are polysaccharides and their functions? Give examples

A
  • 100s-100s of monosaccharides held together by glycosidic linkages
  • Used for structural support and energy storage
  • Ex: Cellulose
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6
Q

What are the functions of carbohydrates?

A
  • Energy
  • Building materials
  • Cell identification and communication
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7
Q

glucose + glucose = ?

A

maltose + water

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8
Q

glucose + fructose = ?

A

sucrose + water

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9
Q

glucose + galactose = ?

A

lactose + water

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10
Q

Where is glucose found? Explain its structure

A
  • Commonly found in fruits and vegetables
  • Composed of a 1:2:1 ratio of carbon, hydrogen, and oxygen
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11
Q

What is the difference between alpha and beta glucose?

A
  • Alpha: 50% chance of the OH group of C1 being found below the plane of ring
  • Beta: 50% chance of the OH group being found above the plane of ring
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12
Q

Where is fructose found?

A
  • Commonly found in fruits
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13
Q

How is fructose different from glucose?

A
  • Fructose is an isomer from glucose
  • They have the same amount and type of atoms, but different structural arrangement
  • This causes them to have different chemical properties
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14
Q

What are the 2 subunits that form a covalent bond by linking?

A
  1. A molecule containing a hydroxyl group (OH)
  2. A molecule containing hydrogen
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15
Q

Explain the 3 steps in a linkage bond

A
  1. Dehydration reaction occurs where the hydroxyl group combines with hydrogen, removing water
  2. Catalysis occurs where energy positions the two subunits and breaks the bond between them
  3. A hydrolysis reaction occurs when the macromolecules are broken, water is added to separate the linkage groups
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16
Q

What is the structure of lipids?

A
  • Composed of glycerol and fatty acids
  • Is insoluble in water as it contains fewer OH bonds and more C-H bonds, making lipids hydrophobic
17
Q

What is esterification?

A

When the hydroxyl group of one glycerol reacts with the carboxyl group of 3 fatty acids, creating an ester linkage

18
Q

What is hydrogenation and why is it a harmful process?

A
  • An industrial process where hydrogen atoms are added to the double bonds of saturated liquids, making a semisolid material like margarine, to increase shelf-life and stability
  • This creates a trans fat, which increases the risk of heart disease and high cholesterol in the blood
19
Q

What is saturated fat? Give an example

A
  • Solid at room temperature due to increased van der Waals attractions
  • Usually comes from animals
  • Has no double bonds between carbon atoms
  • Ex: Butter
20
Q

What is unsaturated fat? Give an example

A
  • Liquid at room temperature
  • Comes from plant oils
  • Has one or more double bonds between carbon atoms
  • Rigid kinks reduce the amount of van der Waals attractions
  • Ex: Olive oil
21
Q

What is the structure and functions of proteins?

A

Structure: Has a unique 3-D conformation
Function: Storage, transport, hormonal, receptors

22
Q

What is a peptide bond formation?

A
  • When amino acids join together by peptide bonds
  • A condensation reaction between an amino group and a carboxyl group of the adjacent amino acid
23
Q

What is the difference between DNA and RNA?

A

DNA: Made of a deoxyribose sugar and stores hereditary information
RNA: Made of a ribose sugar and includes ATP and coenzyme which are used in energy transformations

24
Q

What are the 5 nitrogenous bases?

A
  1. Adenine
  2. Thymine
  3. Cytosine
  4. Guanine
  5. Uracil (only in RNA)
25
Q

What is the difference between purines and pyrimidines?

A

Purines: A double carbon-nitrogen ring (A and G)
Pyrimidines: A single carbon-nitrogen ring (T and C)

26
Q

Explain DNA bonding (purines and pyrimidines)

A
  • Purines only bind with pyrimidines
  • A binds with T with 2 hydrogen bonds
  • C binds with G with 3 hydrogen bonds
27
Q

What are enzymes and their functions?

A
  • Are specialized proteins that act as catalysts
  • They speed up chemical reactions by lowering the activation energy
  • Cannot be used up during a reaction because of a reactant
28
Q

Explain activation energy of enzymes

A
  • All reactions must require an EA that must be overcome for the reaction to occur
  • Catalysts reduce the EA but does not affect the free energy change
  • Catalysts only speed up a reaction that naturally occurs
29
Q

What is the hydrolysis of enzymes?

A
  • The catalysts cannot change the endergonic reaction into an exergonic reaction, but can decrease the potential energy of a transition state
30
Q

Explain the enzyme-substrate complex

A
  • The substrate binds to an activation site on the enzyme
  • The active site conforms to have an induced fit for the substrate
31
Q

What are the 3 factors that affect enzyme activity?

A
  1. Temperature
    - Reaction rate increases as temperature increases
    - Peaks at 37-40℃, then drops rapidly
  2. pH
    - The enzyme can only function under an optimal pH range
  3. Concentration of Substrate Molecules
    - The reaction rate increases as the substrate concentration increases up to a certain point
32
Q

What is a competitive inhibitor and what does it do? Give an example

A
  • Blocks the active site of an enzyme to prevent its regular substrate from binding
  • Is reversible by increasing the substrate concentration
  • Ex: Drugs
33
Q

What is a non-competitive inhibitor and what does it do? Give an example

A
  • Bind to the allosteric site of an enzyme
  • Causes a conformational change of the enzyme, preventing the normal substrate from binding
  • Ex: Loss of enzyme activity (DDT)
34
Q

What is allosteric regulation?

A

Cells control the enzyme activity to coordinate cellular activities

35
Q

What is feedback inhibition?

A

Used by cells to control metabolic pathways involving a series of reactions

36
Q

What is the function of lipids

A
  • Insulating layer
  • Building membranes
  • Stores energy
  • Hormones

SBI4U: Chapter 1 (1 decks)

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