Chemistry of Life - Study Guide

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CH 02 - Chemical Foundation of Life

OpenStax Biology 2e

1. Reading an organic structure

2. Valence Electrons & Number of Bonds

3. Covalent and Hydrogen Bonds

4. Acids and Bases

pH Scale

5. Polar vs. Nonpolar

6. Hydrophobic vs Hydrophilic

7. Most common elements of living things

Chemical Foundation of Life - Carbon

8. Organic Molecules and Compounds

9. Isomers

10. Functional groups

- hydroxyl (alcohols)

- carbonyl (ketone)

- carbonyl (aldehyde)

- carboxyl

- amino

- sulfhydryl

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Circle the functional group in the example

Type R Group Features Example

Hydroxyl Polar
(hydrophilic)
(alcohol)

Carbonyl Polar

(ketones)
(aldehydes)

Carboxyl Acidic

Amino Basic

(amino
acids in
DNA)

Sulfhydryl Polar

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Tripeptide (protein): Identify the groups *Why is this a tripeptide?

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Fructose is a common sugar, found in soft drinks and other sweets. Circle the functional groups

Leucine is an amino acid that plays an important role in muscle development. What functional groups can be
found in a leucine molecule?

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Name: _____________________________________

Biological Macromolecules (OpenStax Biology, Chapter 3) - Reinforcement

1. What are the four macromolecules important to life: ____________________________________________


2. Monomers combine with each other to create _____________________________
3. The creation of these large molecules releases water, the reaction is called: ________________________
4. What type of bond is created during this reaction? _______________________________
5. Polymers can be broken down into individual ___________________________
This process is called ________________________________
6. What can speed up these reactions? _________________________________________

3.2 Carbohydrates
7. What is the ratio of carbon, hydrogen and oxygen in carbohydrates? ___________________
8. What is an example of a pentose monosaccharide? __________________ Hexose? ____________
9. What is the chemical formula for glucose? ______________________________
10. In plants, excess glucose is stored as _____________________________.
11. . Examine each of the monosaccharides below identified as hexoses.

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a) What is the molecular formula for each of these monosaccharides?_________________________
b) Molecules with the same molecular formula but differ structurally are called ___________________
c) Why are these molecules called hexoses? ______________________________________

12. Two monosaccharides can combine to create ______________________________________


13. A covalent bond that forms between two monosaccharides is called a _______________________ bond.
14. The most common disaccharide is ____________________________ (table sugar)

15. Identify the monosaccharide monomers in each molecule.

16. A long chain of monosaccharides is called a _______________________________________


17. Starch is made from a mixture of __________________________ and ______________________
18. What is the animal equivalent of starch? _________________________________
19. Where is cellulose found? ________________________________________
20. How do grazing animals break down cellulose? _________________________________
21. What carbohydrate is found in insect exoskeletons? __________________________________

3.3 Lipids

22. What does nonpolar mean? ________________________________________


23. What are two functions of lipids? ____________________________________________
24. What are the two main components of a fat molecule? _____________________________
25. Saturated fats contain only [ single / double ] bonds.
26. Which type of fat is liquid at room temperature? _________________________
27. On the images below, identify the cis and the trans fat:

28. Why have many companies banned trans fats in their products? _____________________________
29. Where would a person get Omega-3 fatty acids in their diet? _______________________________
30. Why are leaf surfaces covered in wax? ____________________________________
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31. Where are phospholipids found? _____________________________
32. Why is it called an “amphipathic” molecule? ____________________________________

33. Label the phospholipid:

34. Why are steroids grouped with other lipids? _______________

35. What makes them different? _____________________________

36. What are two examples of steroids? __________________________

3.4 Proteins

37. Enzymes are ___________________________ for biochemical reactions.


38. What does amylase do? ___________________________________

39. Identify the protein by its function:


_____________________ transport substances in the blood
_____________________ construction of the cytoskeleton
_____________________ protects body from foreign pathogens
_____________________ muscle contraction

40. What monomers make up proteins? ____________________________________


41. What bond connects amino acids? ______________________________________
42. How many amino acids are there? ________________________

42. What are the four levels of protein structure? ___________________________________

43. What is denaturation? ____________________________________________


What can cause it? ________________________________________________

3.5 Nucleic Acids

44. DNA and RNA are made of what monomers? ___________________________


45. What are the 3 components of a nucleotide? ________________________________________
46. What are the two purines found in DNA? _____________________________
Pyrimidines? _____________________________

47. What is the shape of the DNA molecule? _____________________________


48. What is the rule for base pairing? ____________________________________

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49. What sugar is found in RNA? ____________________________

50. Label the DNA molecule:

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Name ______________________________________________Date:______

Analyzing Graphics: Enzymes

1. Enzymes act on substrates. Label the enzyme, substrate, active site, and products on diagram.

Answer true or false to the following statements based on the graphic:


a. _______ Enzymes interact with many different substrates.
b. _______ Enzymes change shape after a reaction occurs.
c. _______ An enzyme can be reused with a new substrate.
d. _______ The substrate is changed in the reaction.
e. _______ If the shape of the enzyme changed, it would no longer work.
f. _______ When all substrates are used, the reaction stops.

2. Enzymes speed up the reaction by lowering the activation


energy needed for the reaction to start. Compare the activation
energy with and without the enzyme.

Identify the part of the graph that shows:

___ Overall energy released during reaction


___ Activation energy with enzyme
___ Activation energy without enzyme

3. Enzymes work best at optimal temperature and pH


values. For example, the enzyme, pepsin, in your

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stomach must be able to function in a highly acidic environment to break peptide bonds found in proteins.

Acidic or basic conditions can disrupt the hydrogen bonds between the loops of the protein chains. If this disruption
occurs near the active site, the enzyme can become distorted and not fit the substrate perfectly. The rate of reaction is
reduced as more enzymes become denatured.

a) What is the optimal pH for pepsin? _______ For lipase? _______

b) Do you think lipase is an enzyme that is found in the stomach? Why or why not?

4. Enzymes can be inhibited. Inhibitors can slow down or stop enzymatic reactions. There are two types of inhibition:
competitive and allosteric.

Answer true or false to the following statements based on the graphic:


a) _____ Increasing the number of inhibitors will decrease the overall rate of reaction.
b) _____ Allosteric inhibitors block the active site.
c) _____ Allosteric inhibitors change the shape of the enzyme.
d) _____ Adding a competitive inhibitor will increase the number of products in the reaction.
e) _____ Competitive inhibitors bind to the substrates.

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