10 Ass 5 pt 2 Nucleotides & Genetic Control Flashcards
Describe how a polypeptide is produced through the process of translation? 6
The mRNA attaches to a ribosome,
then the tRNA molecule’s anticodon binds to the mRNA’s codon, holding the amino acid in place.
A second tRNA molecule enters the ribosome & holds the second amino acid in place, so both amino acids are side-by-side
this allows a polypeptide bind to form
and for the first tRNA to leave the ribosome
and the mRNA strand then moves onto the next codon
Describe the structure of a peptide bond formed during translation 3
It’s formed between the carboxyl group of 1 amino acid and the amine group of another
It’s strong
it’s covalent
What types of bonds are made during tertiary structure formation?
Hydrogen, Disulfide, ionic, and weak hydrophobic interactions
Describe hydrogen bonds 3
They’re formed between strongly polar R-groups
They’re very weak on their own
Can form a strong structure in large numbers
Describe disulfide bonds 3
Formed between cysteine R-groups
Strong and covalent
Broken by reducing agents
Describe Ionic bonds 2
Broken by changes in pH
Form between ionised amino groups and ionised carboxylic groups
Describe weak hydrophobic interactions 4
occur between non-polar R-groups, so hydrophobic
usually found in centre of protein, shielded by other amino acids
very weak
stay together bc they’re repelled by watery environment around them
Q 21 c) i) (read context) with reference to Fig 3.1, suggest & explain how the mechanism of action of HIV protease can be described as an induced fit 3
The enzyme is flexible, and so is able to change it’s shape
so the substrate can fit into the active site better
Flap region can open to let substrate enter and leave active site
Indinavir is one of the therapeutic drugs used in HIV anti-retroviral therapy (ART). It’s similar to the polyprotein substrate of HIV protease.
Suggest and explain how indinavir acts as a therapeutic drug. 3
It is a competitive inhibitor
that binds to the active site and prevents the substrate from binding
leading to less polyprotein products formed
Q22 Look at Fig 1.1 Name the stage of protein synthesis that is shown in Fig. 1.1.
translation
Q22 Look at Fig 1.1 identify A
mRNA
Q22 Look at Fig 1.1 identify B
tRNA
Q22 Look at Fig 1.1 identify C
polypeptide chain
Q22 Look at Fig 1.1 state the base sequences at D and E
AAA
GUG
Mutagenesis is a process that leads to a change in the amino acid sequences of proteins. Scientists
carry out mutagenesis to investigate the importance of particular amino acids in protein structure
and function.
Outline how changing one amino acid in the β-globin polypeptide of haemoglobin may change the
structure and function of a molecule of haemoglobin. 4
Changing one amino acid can prevent bonds forming between R-groups
because the R-group o the new amino acid will be different
this can also change the protein from polar to non-polar
this will lead to a change in the secondary, tertiary or quaternary structure