Bio chap 3 test

Question 1

Explain the difference between organic compounds and inorganic compounds.

Answer 1

Organic compounds: contain both hydrogen and carbon (build cells); Nonorganic compounds: does not contain both carbon and hydrogen

Question 2

Explain the difference between a monomer, a polymer, and a macromolecule

Answer 2

Monomer: single chemical molecule
Polymer: Molecule composed of many monomers
Macromolecule: large molecules composed of many polymers

Question 3

Explain the special properties of carbon that enable it to be the “essential element” of life

Answer 3

Forms strong covalent bonds with other elements
Forms strong covalent bonds with itself
Form single, double, or triple covalent bonds

Question 4

List the 4 major macromolecules found in living things

Answer 4

Nucleic acids
Carbohydrates
Lipids
Proteins

Question 5

Define proteins

Answer 5

organic compound made up of chains of amino acids

Question 6

Explain the structure of proteins, including its monomer

Answer 6

A long chain of amino acids with a folding protein (polypeptide)

Question 7

Identify the type of bond that forms between individual amino acids

Answer 7

Peptide bond

Question 8

Explain the difference between a protein’s primary structure and its secondary structure.

Answer 8

Primary: Order of amino acids
Secondary: Folding pattern of a protein

Question 9

Identify the type of bond that maintains the folded shape of the protein; this bond forms only when the protein has secondary structure

Answer 9

Hydrogen bonds

Question 10

Explain the structural difference between an alpha-helix protein and a beta-pleated protein.

Answer 10

Alpha helix: spiral shaped with amino acid (think pipe cleaner)
Beta Pleated: Zig-zag

Question 11

List and explain the roles of the 4 types of proteins I expect you to know

Answer 11

Enzymatic: selective acceleration of chemical molecules
transport: Transport of substances
contractile and motor: Movement
structural proteins: support

Question 12

Define metabolism

Answer 12

Combination of chemical reactions where an organism either breaks down or builds materials

Question 13

Define activation energy

Answer 13

The minimum amount of energy used to start a chemical reaction

Question 14

Define “enzyme”

Answer 14

The substance produced by an organism that acts as a catalyst to lower activation energy without being destroyed

Question 15

Describe what an enzyme does and how it works. Your answer must include the phrase “activation energy.”

Answer 15

Start reactions by lowering the activation energy required to start a chemical reaction

Question 16

Describe the function of salivary amylase in humans.

Answer 16

Enzymes found in saliva that starts the breakdown of starch

Question 17

Explain why someone with lactose intolerance is not able to digest milk. Be detailed!

Answer 17

In most people, lactose is broken from a DISACCHARIDE into two
MONOSACCHARIDES. Lactose intolerance is when they don’t have lactase to break down the lactose

Question 18

Describe the cause of Gaucher’s disease, including the names of important molecules

Answer 18

Because of the lack of glucocerebrosidase, there is nothing to break down lipids in the spleen and liver allowing fat to build up

Question 19

Explain what occurs to the cells of an individual with Gaucher’s disease.

Answer 19

Glucose/lipids build up in the cells due to the lack of glucocerebrosidase

Question 20

Explain in detail why Maria from our case study experienced the following symptoms:
1. Protruding stomach 2. Increased bruising
3. Tiredness

Answer 20

1. Expanded spleen and liver
2. Less blood cells are produced making bruising easier
3. Anmeia (low blood cells because of low blood marrow production along with spleen killing off) does not allow proper oxygen supply

Question 21

Describe how an enzyme works as it relates to the substrate and active site of the enzyme (the induced fit model)

Answer 21

The enzyme attracts the substrate and connect on the active site and mold to the model

Question 22

Describe the 3 ways in which an enzyme can be deactivated

Answer 22

1) Competitive inhibition – a molecule takes
up the active site so the substrate cannot
enter

2) Noncompetitive (or allosteric) inhibition – a
molecules takes up another space on the
enzyme that causes the active site to change
shape

3) Temperature or pH change – changes the
shape of the enzyme because it breaks
hydrogen bonds, which changes shape of
active site