Flashcards in AA_Molecules Deck (44):
1
How many different R groups are there?
20 different R groups
2
What are the property of R groups?
All chiral except Glycine
3
What are the different category of side chains?
- Hydrophobic
- Hydrophilic
4
What are the different divisions of hydrophobic side chains?
- Aliphatic
- Aromatic
5
What are the different divisions of hydrophilic side chains?
- Polar, uncharged
- Acidic, -ve charged
- Basic, +ve charged
6
Name the small AA
Glycine and Alanine
7
What group does the side chain of Glycine and Alanine fall under?
Hydrophobic, Aliphatic
8
What group does the side chain of Valine, Leucine, Isoleucine fall under?
Hydrophobic, Aliphatic
9
Name the branched chain amino acids
Valine, Leucine, Isoleucine
10
Name the aromatic amino acids
Phenylalanine, Tyrosine, Tryptophan
11
What category does the side chain of Phenylalanine, Tyrosine, Tryptophan fall under?
Mainly hydrophobic, aromatic
12
Name the sulphur amino acids
Cysteine, Methionine
13
What group does the side chain of Cysteine fall under?
Polar uncharged
14
What group does the side chain of Methionine fall under?
Hydrophobic
15
Name the Acidic amino acids and their derivatives
Aspartate, Asparagine, Glutamate, Glutamine
16
What category does the side chain of Aspartate and Glutamate fall under?
Negatively charged
17
What category does the side chain of Asparagine and Glutamine fall under?
Polar, uncharged
18
Name the basic amino acids
Lysine, Arginine, Histidine
19
What category does the side chain of Lysine, Arginine, Histidine fall under?
Positively charged
20
Name the cyclic amino acid
Proline
21
What are the two types of amino acids?
1) Essential
2) Non - essential (produced by the body)
22
What "other" amino acids is involved in metabolism?
- Ornithine
- Citrulline
23
What is the 21st amino acid?
Selenocysteine
24
What is post translational modifications?
Covalent modification of side chains in protein, usually it is the addition of functional group (e.g. phosphate or carbohydrate -> to help with signalling, structural reasons, catalytic reasons)
25
What is the peptide bond?
When 2 AA link covalently, the bond between them in the peptide bond
26
How is the peptide bond formed?
Condensation
27
What type of reaction are peptide bond formation?
Endergonic (accompanied by or requiring the absorption of energy)
28
What processed need peptide bond?
Peptide bonds are strong covalent bonds which keep the amino acids connected during and after Translation.
Also in ribosomes during translation
29
Do peptide bonds rotate?
No
30
Write the reaction of peptide bond formation.
Draw
31
What is a dipeptide?
Formed by the action between the alpha carbonyl and alpha amino group of two AA.
32
What are the other forms of polypeptides?
Dipeptide
Tripeptide
Oligopeptide
Polypeptide
33
What are polypeptides made from/
Protein and there is an N terminus ("start" - amino terminus) and a C terminus ("end" - carboxyl terminus)
34
What is phosphorylation
Reversible addition of phosphate by protein kinases
35
How are di-sulphide bridges formed?
Formed in a reductive reaction which the two H atoms of the sulfhydryl groups are transferred to an acceptor molecule
- 2 Cysteines link together (can be from same polypeptide or different polypeptide)
36
Where do di-sulphide bridge formation normally take place?
in ER therefore most secreted proteins and membrane proteins have disulphide bonds
37
What are the different structure category of proteins?
1) Primary structure
2) Secondary structure
3) Tertiary structure
4) Quaternary structure
38
What are primary structures?
AA residues
39
What are secondary structures?
alpha helix and beta sheet
40
What are tertiary structures?
polypeptide chain
41
What are quaternary structure?
assembled subunits
42
How are sequence unique to a specific bacteria?
Each has signature sequence
43
How are Amino acid sequence (protein) formed?
Amino acid sequence can be transcribed by DNA sequence (gene)
44