Chapter 4

Question 1

a (alpha) carbon

Question 2

Amino Group

Question 3

Carboxyl Group

Question 4

Side Chain

Question 5

R Group

Question 6

Peptide Bond

Question 7

Amino End

Question 8

Carboxyl End

Question 9

Polypeptide

Question 10

Protein, residues

Question 11

Primary Structure

Question 12

Secondary Structures

Question 13

Tertiary Structures

Question 14

Quaternary Structure

Question 15

Alpha Helix

Question 16

Beta Sheet

Question 17

Denatured

Question 18

Chaperones

Question 19

Translation

Question 20

Messenger RNA (mRNA)

Question 21

Ribosomes

Question 22

A (aminoacyl) Site

Question 23

P (peptidyl) Site

Question 24

E (exit) Site

Question 25

Codon

Question 26

Reading Frames

Question 27

Anticodon

Question 28

Aminoacyl tRNA Synthetases

Question 29

Genetic Code

Question 30

Initiation

Question 31

Elongation

Question 32

Termination

Question 33

Initiation Factors

Question 34

Elongation Factors

Question 35

Release Factor

Question 36

Polycistronic mRNA

Question 37

What are the major groups of amino acids as categorized by the properties of their R groups? How do the chemical properties of each group affect protein shape?

Question 38

How do the peptide bonds, hydrogen bonds, ionic bonds, disulfide bridges, and noncovalent interactions (van der Waals forces and the hydrophobic effect) define a protein’s four levels of structure?

Question 39

What ultimately determines the three-dimensional shape of a protein?

Question 40

A mutation leads to a change in one amino acid in a protein. The result is that the protein no longer functions properly. How is this possible?

Question 41

Which polypeptide sequence would you expect to result from a synthetic mRNA with the sequence 5’- UUUCCGAUGGGGUUUGGGUUUGGG-3’?

Question 42

What are the steps of translation? Name and describe each one.