Chapter 4 Flashcards
1
Q
a (alpha) carbon
A
2
Q
Amino Group
A
3
Q
Carboxyl Group
A
4
Q
Side Chain
A
5
Q
R Group
A
6
Q
Peptide Bond
A
7
Q
Amino End
A
8
Q
Carboxyl End
A
9
Q
Polypeptide
A
10
Q
Protein, residues
A
11
Q
Primary Structure
A
12
Q
Secondary Structures
A
13
Q
Tertiary Structures
A
14
Q
Quaternary Structure
A
15
Q
Alpha Helix
A
16
Q
Beta Sheet
A
17
Q
Denatured
A
18
Q
Chaperones
A
19
Q
Translation
A
20
Q
Messenger RNA (mRNA)
A
21
Q
Ribosomes
A
22
Q
A (aminoacyl) Site
A
23
Q
P (peptidyl) Site
A
24
Q
E (exit) Site
A
25
Codon
26
Reading Frames
27
Anticodon
28
Aminoacyl tRNA Synthetases
29
Genetic Code
30
Initiation
31
Elongation
32
Termination
33
Initiation Factors
34
Elongation Factors
35
Release Factor
36
Polycistronic mRNA
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?
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?
39
What ultimately determines the three-dimensional shape of a protein?
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?
41
Which polypeptide sequence would you expect to result from a synthetic mRNA with the sequence 5’- UUUCCGAUGGGGUUUGGGUUUGGG-3’?
42
What are the steps of translation? Name and describe each one.
