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Advanced Higher Biology > Proteins > Flashcards

Proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Describe the proteome.

A

The entire set of proteins that could be potentially expressed by the genome.

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2
Q

Describe the genome.

A

The complete set of DNA possessed by an organism.

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3
Q

Factors effecting expression (4).

A
  1. Metabolic activity of the cell.
  2. Cellular stress.
  3. Response to signal molecules.
  4. Diseased/healthy cells
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4
Q

Identify two reasons why the proteome is larger than the genome.

A
  1. Alternative RNA splicing
  2. Post translational modification
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5
Q

Where does post translational modification occur? (3)

A
  1. Endoplasmic reticulum
  2. Golgi Apparatus
  3. Target site.
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6
Q

Define the Human Genome.

A

All of the hereditary information contained within a persons DNA.

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7
Q

Identify 3 forms of RNA.

A
  1. tRNA
  2. rRNA
  3. microRNA
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8
Q

What is contained within the Cytosolic face of the Rough Endoplasmic Reticulum?

A

Ribosomes.

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9
Q

What is formed in the smooth endoplasmic reticulum?

A

Lipids.

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10
Q

Where are cytosolic proteins synthesised?

A

Cytosolic Ribosomes.

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11
Q

Transmembrane proteins carry a signal sequence which halts translation and triggers the direction to the ___________.

A

Endoplasmic reticulum.

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12
Q

Does the smooth endoplasmic reticulum contain ribosomes?

A

No.

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13
Q

What is the purpose of the Golgi Apparatus?

A

Responsible for transporting, modifying and packaging lipids and proteins.

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14
Q

What is the Golgi Apparatus composed of?

A

Flattened membrane discs.

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15
Q

When are vesicles formed? (2)

A
  1. When budding off the Endoplasmic reticulum.
  2. When budding off the Golgi Apparatus either to the membrane or cytoplasm to form lysosome.
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16
Q

How do vesicles move in the cytoplasm?

A

Vesicles move along microtubules, and are connected by Kinesin.

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17
Q

What is the purpose of a lysosome?

A

A lysosome contains various hydrolyses which digest proteins, lipids and carbohydrates into their constituant parts.

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18
Q

What are the constituant parts of an amino acids.

A
  1. Carboxyl group
  2. Amine group
  3. Variable R-group
  4. Central carbon
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19
Q

What do some secratory pathways reqiure in order for activation to occur?

A

Proteolytic cleavage.

20
Q

What are the four main classes of amino acid.

A

Polar, Non-polar, Basic and Acidic.

21
Q

Identify the nature of an acidic amino acid (2).

A

Negative and hydrophilic.

22
Q

Identify the nature of a basic amino acid (2).

A

Positive and hydrophilic.

23
Q

Identify the nature of a polar amino acid (1).

A

Hydrophilic.

24
Q

Identify the nature of a non-polar amino acid (1).

A

Hydrophobic.

25
Q

Describe the primary structure.

A

Polypeptide chain in a linear composition.

26
Q

What bond stabilises the secondary structure.

A

Hydrogen bond.

27
Q

What are the two types of secondary structures?

A

Alpha helix and beta pleated sheet.

28
Q

Describe the alpha helix.

A

Held together by hydrogen bonding at every 4th amino acid.

29
Q

Describe the beta pleated sheet.

A

Two parts of a polypeptide run parallel or anti-parrallel, held together by hydrogen bonding.

30
Q

What may be included in the secondary structure.

A

Turns.

31
Q

Identify a tertiary structure bond.

A
  1. London dispersion.
  2. Ionic.
  3. Hydrogen.
32
Q

What is the name given to a non-protein group found in a tertairy structure.

A

Prosthetic.

33
Q

Describe the tertiary structure.

A

Three dimensional folding due to side chain reactions.

34
Q

Describe the Quanternary structure.

A

Two or more polypeptide subunits joined together and defined by spacial arrangement of subunits.

35
Q

Describe the effect of pH on Haemoglobin.

A

As pH interactions decrease, ionic interactions between charged groups are lost.

36
Q

Describe the effect of pH on Haemoglobin.

A

Breaks weak bonds, therefore disrupting protein structure.

37
Q

What is a ligand.

A

A substance that can bind to a protein.

38
Q

Describe a positive modulator.

A

A positive modulator is a ligand that binds to a spatially distinct site, changing the conformation of the protein and increasing the affinity of the ligand for the protein.

39
Q

Describe a negative modulator.

A

A negative modulator is a ligand that binds to a spatially distinct site, changing the conformation of the protein and decreasing the affinity of the ligand for the protein.

40
Q

What is the positive modulator of ATcase?

A

ATP

41
Q

What is the negative modulator of ATCase?

A

CTP

42
Q

What occurs when there is an abundance of CTP (in the context of ATCase)?

A

Inhibition of CTP.

43
Q

What does an abundance of ATP (in the context of ATCase) suggest?

A

Nucleotides may be necessary for DNA replication.

44
Q

What is co-operativity?

A

The binding of a ligand to one active site increases affinity for a ligand in remaining subunits .

45
Q

What happens when temperature increases and pH decreases?

A

A right shift in the oxyhemoglobin dissociation curve, decreasing affinity of haemoglobin for oxygen.

Advanced Higher Biology (10 decks)

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