3.1.4.1 Proteins Flashcards
1
Q
What is the monomer of proteins
A
- amino acid
2
Q
What chemical properties in proteins change
A
- non-polar (hydrophobic)
- polar (hydrophilic)
- positive charge (hydrophilic)
- negative charge (hydrophilic)
3
Q
What is the polymer of proteins
A
- polypeptide
4
Q
How is a polypeptide formed
A
- condensation reaction
- between amine & carboxyl groups
- forms peptide bond
- water released
5
Q
How do you break a polypeptide
A
- hydrolysis
- requires water
6
Q
Describe the primary structure of proteins
A
- sequence of a.a joined by peptide bond
- controls the protein shape
- varied:
. Different length chains
. Different a.a in chain
. Amino aids in different sequences
7
Q
Describe the secondary structure of proteins
A
- folding of parts of chain - alpha helices or beta-pleated sheets
- due to H2 bonding
- between carboxyl & amino residues
8
Q
Describe the tertiary structure of proteins
A
- folding into complex, specific, shape
- due to IMF between R groups
- H2 bonds - between polar R groups
- ionic forces - between + and - R groups
- disulphide bridges - covalent bond between cysteine R groups
- London forces - between non-polar R groups
9
Q
describe the quaternary structure of proteins
A
- holds the polypeptide chains together
- due to IMF between R groups
10
Q
What are the 2 groups of structures in proteins
A
Globular:
- enzymes, signalling molecules, transport molecules. Have a specific shape for binding
Fibrous:
- structural. Strong & flexible
11
Q
What is the test for proteins
A
- buret test
- positive result: colour change from blue to purple