2B Flashcards

1
Q

Name the monomers that make DNA and RNA

A

Nucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Describe the basic structure of a nucleotide

A

A phosphate group, a pentose sugar and a base

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What do A, T, G, C and U stand for?

A

Adenine, cytosine, thymine, guanine, uracil

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

How do DNA and RNA nucleotides differ?

A

RNA has a ribose sugar whereas DNA has a deoxyribose sugar. RNA has a uracil base whereas DNA has Thymine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Describe the structure of RNA

A

Single polynucleotide strand of RNA nucleotides.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Describe how nucleotides join to form polynucleotides?

A

By condensation reactions between the sugar and phosphate groups to form phosphodiester bonds and a sugar phosphate backbone.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Which bases form complementary base pairs in DNA and RNA?

A

Adenine with Thymine (Uracil in RNA). Cytosine with Guanine.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Briefly outline the two main stages involed in protein synthesis.

A
  1. Transcription; reads DNA sequence and produces mRNA.
  2. Translation; reads mRNA sequence and orders amino acids to form polypeptide.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Describe the process of transcription.

A

DNA uncoils (DNA helicase) into two strands with exposed bases. One used as a template. Free RNA nucleotides form hydrogenn bonds with complementary bases. Nucleotides are joined together by RNA polymerase forming phospodiester bonds between the sugar and phosphate groups in a condensation reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What happens to mRNA after transcription?

A

It moves out of the nucleus into the cytoplasm and attaches to a ribosome, ready for translation.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Describe the process of translation.

A

The anti-codon of tRNA attaches to complementary bases on the mRNA codons.
Amino acids bonded to tRNA form peptide bonds in a condensation reaction, continuing to form a polypeptide chain until a stop codon is reached.
This process requires ATP.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Explain how bases code for amino acids

A

Three bases code for one amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Identify features of the genetic code

A

A triplet of bases codes for a particular amino acid.
Non-overlapping=each triplet is only read once.
Degenerate=more than one triplet codes for the same amino acid (64 possible triplets for 20 amino acids).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is a gene?

A

A sequence of bases on a DNA molecule that codes for a specific sequence of amino acids in a polypeptide chain.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Define dipeptide

A

Two amino acids joined by a peptide bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Define polypeptide

A

Two or more amino acids joined together by peptide bonds

17
Q

How are polypeptides formed from their monomers?

A

Amino acids join together in condensation reactions, forming a peptide bond.

18
Q

What is meant by the primary structure of a protein?

A

Primary = basic amino acid sequence.

19
Q

What is meant by the secondary structure of a protein?

A

Secondary = whether the polypeptide chain is arranged into a helix or pleated sheet. Held together by H bonds.

20
Q

What is meant by the tertiary structure of a protein?

A

Tertiary = 3D folding of the secondary structure into a complex shape held together by bonds between R groups of different amino acids e.g. ionic, hydrogen, disulfide bonds as well as hydrophobic and hydrophillic interactions.

21
Q

What is meant by the quarternary structure of a protein?

A

When more than one polypeptide chain in a tertiary structure bonds together

22
Q

How does the primary structure affect the tertiary (3D) structure?

A

Different amino acid sequence therefore different R groups that produce different bonds in the tertiary structure.

23
Q

Describe how the structure of fibrous proteins relates to their function.

A

Long polypeptide chains. Very little tertiary structure. Strong cross-linkages between polypeptide chains. Hydrophobic groups on outside. This makes them insoluble, and useful for providing structure.

24
Q

Give an example of a fibrous protein and explain how its properties relate to its use.

A

Collagen. Three polypeptide chains form a triple helix which creates fibres held together by strong crosslinks. This makes it useful in bones, cartilage and
other connective tissue.

25
Q

Describe how the structure of globular proteins relates to their function.

A

Compact, highly folded with complex tertiary/quaternary structures. Soluble due to hydrophillic groups on the outside. They are useful for hormones, antibodies, etc.

26
Q

Give an example of a globular protein and explain how its properties relate to its use.

A

Haemoglobin. Water-soluble, made of 4 polypeptide chains. Contains four haem groups that oxygen can bind to. It is therefore used to carry oxygen in the
blood to respiring tissues.

27
Q

What are enzymes?

A

Proteins that act as biological catalysts i.e. increase the rate of a reaction by lowering the activation energy.

28
Q

Describe the structure of enzymes

A

Globular therefore highly folded proteins with a specific active site that is complementary to a particular substrate

29
Q

How do enzymes that join two molecules together work?

A

The active site holds the two molecules in the right orientation to form new bonds.

30
Q

How do enzymes that break down molecules work?

A

A substrate molecule is held in the active site putting a strain on the bonds and breaking the two molecules apart.

31
Q

What is meant by a ‘specific’ active site?

A

That the active site is complementary to a particular substrate where a substrate bonds to form an enzyme substrate complex.

32
Q

What determines the shape of the active site of an enzyme?

A

The sequence of bases in the gene that determines the sequence of amino acids in the primary sequence of the protein. Different R groups on different amino acids form different bonds in the tertiary structure of the protein which determines the shape of the active site.

33
Q

Differentiate with examples between intracellular and extracellular enzymes.

A

Intracellular enzymes work within cells e.g. DNA helicase and extracellular work outside cells e.g. amylase