10 Ass 5 pt 2 Nucleotides & Genetic Control Flashcards

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1
Q

Describe how a polypeptide is produced through the process of translation? 6

A

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

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2
Q

Describe the structure of a peptide bond formed during translation 3

A

It’s formed between the carboxyl group of 1 amino acid and the amine group of another

It’s strong

it’s covalent

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3
Q

What types of bonds are made during tertiary structure formation?

A

Hydrogen, Disulfide, ionic, and weak hydrophobic interactions

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4
Q

Describe hydrogen bonds 3

A

They’re formed between strongly polar R-groups

They’re very weak on their own

Can form a strong structure in large numbers

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5
Q

Describe disulfide bonds 3

A

Formed between cysteine R-groups

Strong and covalent

Broken by reducing agents

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6
Q

Describe Ionic bonds 2

A

Broken by changes in pH

Form between ionised amino groups and ionised carboxylic groups

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7
Q

Describe weak hydrophobic interactions 4

A

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

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8
Q

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

A

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

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9
Q

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

A

It is a competitive inhibitor

that binds to the active site and prevents the substrate from binding

leading to less polyprotein products formed

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10
Q

Q22 Look at Fig 1.1 Name the stage of protein synthesis that is shown in Fig. 1.1.

A

translation

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11
Q

Q22 Look at Fig 1.1 identify A

A

mRNA

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12
Q

Q22 Look at Fig 1.1 identify B

A

tRNA

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13
Q

Q22 Look at Fig 1.1 identify C

A

polypeptide chain

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14
Q

Q22 Look at Fig 1.1 state the base sequences at D and E

A

AAA
GUG

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15
Q

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

A

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

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16
Q

Q23 Fig. 6.1 shows the formation of a polypeptide during translation in a eukaryotic cell. Name the pyrimidine bases

A

Uracil and Cytosine

17
Q

Fig. 6.1 shows the formation of a polypeptide during translation in a eukaryotic cell. Name the purine bases shown in Fig. 6.1

A

Adenine and guanine

18
Q

Fig. 6.1 shows the formation of a polypeptide during translation in a eukaryotic cell. State the name given to the group of three bases found at J on the tRNA molecule

A

Anticodon

19
Q

Fig. 6.1 shows the formation of a polypeptide during translation in a eukaryotic cell. Identify the three bases at J

A

CAG

20
Q

Fig. 6.1 shows the formation of a polypeptide during translation in a eukaryotic cell. State how the three bases at J on tRNA interact with the bases on mRNA.

A

Complementary bases are held together by hydrogen bonds

21
Q

Name the type of chemical reaction that occurs when two amino acids form a dipeptide

A

condensation

22
Q

Q 24 b) Fig. 3.1 shows two amino acids, glycine and valine.
Use the space below to make a drawing to show what happens when these two molecules join together to form a dipeptide.

A

See memo or written qp (i did corrections in written qp)