Organic Molecules Review - Lipids, Proteins, Carbohydrates (Lecture Notes)

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A comprehensive set of Q&A flashcards covering lipids, proteins, carbohydrates, functional groups, and basic biochemical reactions based on the provided notes.

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40 Terms

1
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What characteristic binds lipids together as a group of organic molecules?

Hydrophobic, nonpolar.

2
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What is the fat-energy storage molecule composed of glycerol and three fatty acids?

Triglyceride (triacylglycerol).

3
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Which polysaccharide is used for energy storage in plants?

Starch (amylose/amylopectin); composed of alpha-glucose units.

4
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Which polysaccharide is used for energy storage in animals?

Glycogen; highly branched storage polymer of glucose.

5
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Which polysaccharide provides structural support in plants and is made of beta glucose?

Cellulose; beta-1,4 linkages; forms plant cell walls and is indigestible to most animals.

6
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Which polysaccharide forms exoskeletons in arthropods and fungal cell walls?

Chitin; made from N-acetylglucosamine; structural polymer.

7
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Which organism has a symbiotic relationship with bacteria to digest cellulose?

Termites; gut bacteria help break down beta-glucose cellulose.

8
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What feature of phospholipids makes the tails hydrophobic and the head hydrophilic?

Two fatty acid tails (nonpolar) and a phosphate-containing head group (polar).

9
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How does the structure of a steroid differ from other lipids?

Steroids have four fused carbon rings instead of long hydrocarbon chains.

10
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Name major steroids mentioned.

Cholesterol, testosterone, estrogen (and other steroid hormones).

11
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What makes cellulose difficult to digest for many animals?

Beta glucose linkages (beta-1,4) and lack of the enzyme to digest them.

12
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What are the three basic parts of an amino acid molecule? Which part differs among amino acids?

Amino group, carboxyl group, and side chain (R group); the side chain differs.

13
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What are the four structural levels of organization of polypeptide chains?

Primary, secondary, tertiary, and quaternary structure.

14
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Primary structure describes what?

The sequence of amino acids linked by peptide bonds.

15
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Secondary structure refers to what features?

Alpha helices and beta pleated sheets stabilized by hydrogen bonds between backbone atoms.

16
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Tertiary structure refers to what?

The overall 3D shape of a single polypeptide, formed by interactions among side chains.

17
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Quaternary structure refers to what?

The arrangement of multiple polypeptide chains into a functional protein.

18
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Name a functional category of proteins and an example.

Enzymatic — e.g., amylase; other examples: structural, transport, hormonal, defensive, contractile.

19
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What is an enzymatic protein and give an example?

A protein that catalyzes chemical reactions; example: amylase.

20
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What is a structural protein and give an example?

A protein that provides support and shape; example: collagen.

21
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What is a transport protein and give an example?

A protein that carries molecules; example: hemoglobin.

22
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What is a hormonal regulatory protein and give an example?

A protein involved in chemical signaling; example: insulin.

23
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What is a defensive protein and give an example?

A protein that protects the body; example: antibodies.

24
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What is a contractile/movement protein and give an example?

A protein that enables movement; example: actin (with myosin).

25
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What are the three R-group categories for amino acids?

Hydrophobic (nonpolar), Hydrophilic (polar), Ionic (charged).

26
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What is the significance of hydrophobic R groups in proteins?

They avoid water and cluster inside the protein core, helping stabilize folding.

27
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What is the significance of hydrophilic R groups in proteins?

They interact with water and other polar molecules, often on the protein surface to promote solubility.

28
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What is the significance of ionic R groups in proteins?

They can form ionic (salt) bridges with opposite charges, contributing to folding, stability, and active sites.

29
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What is the function of quaternary structure?

Assembly of multiple polypeptide chains into a functional protein; enables protein complexes and cooperative activity.

30
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What is a condensation (dehydration) reaction?

Removal of water to form covalent bonds (e.g., peptide bonds during protein formation).

31
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What is a hydrolysis reaction?

Addition of water to break covalent bonds (e.g., breaking peptide bonds in proteins).

32
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What is the basic building block of carbohydrates?

Monosaccharide.

33
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What is maltose and how is it formed?

A disaccharide formed by dehydration between two glucose units; glucose–glucose linked by an alpha-1,4 glycosidic bond.

34
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How do glucose, galactose, and fructose differ structurally?

Glucose and galactose are aldoses; fructose is a ketose; carbonyl placement differs (C1 vs C2).

35
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Name three disaccharides formed by dehydration synthesis.

Maltose (glucose-glucose), sucrose (glucose-fructose), lactose (galactose-glucose).

36
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Are methyl groups polar or nonpolar?

Nonpolar.

37
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What macromolecule contains methyl groups and what is their effect?

Lipids; methyl groups contribute to nonpolarity and energy storage, making molecules less soluble.

38
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Are carbonyl groups polar or nonpolar?

Polar.

39
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Name a macromolecule that contains carbonyl groups.

Nucleic acids and amino acids (carbonyl groups in peptide bonds and backbone).

40
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How does the carbonyl group contribute to a molecule's shape/function?

Part of the backbone; contributes to polarity and hydrogen bonding, aiding folding and structure.