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AH Biology - Unit 1 > KA 2 > Flashcards

KA 2 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is the proteome?

A

The entire set of proteins expressed by a genome

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2
Q

Why is the proteome larger than the number of genes? particularly in eukaryotes.

A

Because more than one protein can be produced from a single gene as a result of alternative RNA splicing

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3
Q

What are all genes not expressed as?

A

Not all genes are expressed as proteins in a particular cell type.

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4
Q

What are Genes that do not code for proteins called? What do they include and do?

A

Non-coding RNA genes and include those that are transcribed to produce tRNA, rRNA, and RNA molecules that control the expression of other genes.

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5
Q

What can the set of proteins expressed by a given cell type do?

A

It can vary over time and under different conditions

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6
Q

Some factors affecting the set of proteins expressed by..

A

a given cell type are the metabolic activity of the cell, cellular stress, the response to signalling molecules, and diseased versus healthy cells.

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7
Q

What do Eukaryotic cells have? And what does this do because of..

A

A system of internal membranes, which increases the total area of membrane Because of their size, eukaryotes have a relatively small surface area to volume ratio.

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8
Q

The plasma membrane of eukaryotic cells is too small an area to carry out what?

A

All the vital functions carried out by membranes.

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9
Q

What does the endoplasmic reticulum (ER) do?

A

Forms a network of membrane tubules continuous with the nuclear membrane

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10
Q

What is the Golgi apparatus?

A

It is a series of flattened membrane discs

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11
Q

What are Lysosomes?

A

Membrane-bound organelles containing a variety of hydrolases that digest proteins, lipids, nucleic acids and carbohydrates

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12
Q

What do vesicles do?

A

Transport materials between membrane compartments

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13
Q

Where are lipids and proteins synthesised?

A

In the ER (endoplasmic reticulum)

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14
Q

What does Rough ER (RER) have? That Smooth ER (SER) lacks..

A

Ribosomes on its cytosolic face while smooth ER (SER) lacks ribosomes.

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15
Q

What is the exact location of the synthesis of lipids? What happens to these after synthesis?

A

Lipids are synthesised in the smooth endoplasmic reticulum (SER) and inserted into its membrane

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16
Q

Where does the synthesis of all proteins begin and complete and where do these remain after?

A

In cytosolic ribosomes. The synthesis of cytosolic proteins is completed there, and these proteins remain in the cytosol.

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17
Q

What do transmembrane proteins carry? And what does this do?

A

A signal sequence, which halts translation and directs the ribosome synthesising the protein to dock with the ER, forming RER

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18
Q

What is a signal sequence? And what does this determine?

A

A short stretch of amino acids at one end of the polypeptide that determines the eventual location of a protein in a cell.

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19
Q

What continues after docking? And what happens to the protein?

A

Translation and the protein is inserted into the membrane of the ER

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20
Q

Once the proteins are in the ER what are they transported by?

A

Vesicles that bud off from the ER and fuse with the Golgi apparatus

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21
Q

As proteins move through the Golgi apparatus what do they undergo?

A

Post-translational modification

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22
Q

When molecules move through the Golgi discs what happens to them?

A

They move along in vesicles that bud off from one disc and fuse to the next one in the stack.

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23
Q

Enzymes catalyse the addition of what?

A

Various sugars in multiple steps to form the carbohydrates.

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24
Q

What is the addition of carbohydrate groups?

A

A major modification

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25
Q

Where do vesicles that leave the Golgi apparatus take proteins?

A

To the plasma membrane and lysosomes

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26
Q

Vesicles move along what? To what?

A

Microtubules to other membranes and fuse with them within the cell

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27
Q

Secreted proteins are translated in what?

A

Ribosomes on the RER and enter its lumen.

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28
Q

Give 2 examples of secreted proteins

A

Peptide hormones and digestive enzymes

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29
Q

The proteins move through what and what happens to them after this?

A

The Golgi apparatus is then packaged into secretory vesicles.

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30
Q

Secretory vesicles move to and fuse with what? Which then releases…

A

The plasma membrane, releasing the proteins out of the cell

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31
Q

Many secreted proteins are synthesised as what? What do these require to become active?

A

Inactive precursors and require proteolytic cleavage to produce active proteins

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32
Q

Proteolytic cleavage is another type of?

A

Post translational modification.

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33
Q

Digestive enzymes are one example of ?

A

Secreted proteins that require proteolytic cleavage to become active.

34
Q

Amino acid sequence determines what?

A

Protein structure

35
Q

What can you use to distinguish between different amino acids?

A

Amino acid chromatography

36
Q

What are proteins?

A

Proteins are polymers of amino acid monomers

37
Q

What are Amino acids linked by?

A

peptide bonds to form polypeptides

38
Q

Amino acids have the same? What differs about them?

A

Basic structure, differing only in the R group present R groups of amino acids vary in size, shape, charge, hydrogen bonding capacity and chemical reactivity.

39
Q

How are amino acids classified?

A

According to their R groups: basic (positively charged); acidic (negatively charged); polar; hydrophobic

40
Q

What does the wide range of functions carried out by proteins result from?

A

The diversity of R groups

41
Q

The primary structure is…

A

The sequence in which the amino acids are synthesised into the polypeptide

42
Q

What does Hydrogen bonding along the backbone of the protein strand result in?

A

Regions of secondary structure — alpha helices, parallel or antiparallel beta-pleated sheets, or turns

43
Q

What does the polypeptide fold into?

A

A tertiary structure

44
Q

Tertiary structure is stabilised by?

A

Interactions between R groups: hydrophobic interactions; ionic bonds; London dispersion forces; hydrogen bonds; disulfide bridges

45
Q

What are Disulfide bridges?

A

Covalent bonds between R groups containing sulfur.

46
Q

Quaternary structure exists in proteins with?

A

Two or more connected polypeptide subunits

47
Q

Quaternary structure describes?

A

The spatial arrangement of the subunits.

48
Q

A prosthetic group is?

A

A non-protein unit tightly bound to a protein and necessary for its function

49
Q

The ability of haemoglobin to bind oxygen is dependent upon?

A

The non-protein haem group.

50
Q

Interactions of the R groups can be influenced by?

A

Temperature and pH.

51
Q

Increasing temperature disrupts? What does this do to the protein?

A

The interactions that hold the protein in shape; the protein begins to unfold, eventually becoming denatured.

52
Q

The charges on acidic and basic R groups are affected by?

A

pH

53
Q

As pH increases or decreases from the optimum, the normal ionic interactions between charged groups are?

A

Lost, which gradually changes the conformation of the protein until it becomes denatured.

54
Q

Ligand binding changes?

A

The conformation of a protein

55
Q

A ligand is?

A

A substance that can bind to a protein R groups not involved in protein folding can allow binding to ligands

56
Q

Binding sites will have?

A

complementary shape and chemistry to the ligand

57
Q

As a ligand binds to a protein-binding site?

A

The conformation of the protein changes

58
Q

This change in protein conformation causes?

A

a functional change in the protein

59
Q

Allosteric interactions occur between?

A

spatially distinct sites

60
Q

The binding of a substrate molecule to one active site of an allosteric enzyme increases?

A

The affinity of the other active sites for binding of subsequent substrate molecules.

61
Q

What is the biological importance of affinity changes after binding?

A

Because the activity of allosteric enzymes can vary greatly with small changes in substrate concentration.

62
Q

What do many allosteric proteins consist of?

A

Multiple subunits (have quaternary structure)

63
Q

Allosteric proteins with multiple subunits show?

A

Cooperativity in binding, in which changes in binding at one subunit alter the affinity of the remaining subunits

64
Q

Allosteric enzymes contain?

A

A second type of site, called an allosteric site

65
Q

Modulators regulate?

A

the activity of the enzyme when they bind to the allosteric site

66
Q

Following binding of a modulator what changes and alters?

A

The conformation of the enzyme changes and this alters the affinity of the active site for the substrate

67
Q

Positive modulators increase?

A

The enzyme’s affinity for the substrate

68
Q

Negative modulators reduce?

A

the enzyme’s affinity.

69
Q

The binding and release of oxygen in haemoglobin shows?

A

Cooperativity

70
Q

Changes in binding of oxygen at one subunit alter?

A

the affinity of the remaining subunits for oxygen.

71
Q

A decrease in pH or an increase in temperature does what to the affinity of haemoglobin for oxygen?

A

Lowers so the binding of oxygen is reduced.

72
Q

Reduced pH and increased temperature in actively respiring tissue will?

A

Reduce the binding of oxygen to haemoglobin promoting increased oxygen delivery to tissue

73
Q

The addition or removal of phosphate can cause? What is this a common form of?

A

Reversible conformational change in proteins. This is a common form of post-translational modification

74
Q

Protein kinases catalyse?

A

The transfer of a phosphate group to other proteins

75
Q

The terminal phosphate of ATP is transferred to?

A

Specific R groups

76
Q

Protein phosphatases catalyse?

A

The reverse reaction

77
Q

Phosphorylation brings about?

A

Conformational changes, which can affect a protein’s activity

78
Q

The activity of many cellular proteins, such as enzymes and receptors, is regulated?

A

By phosphorylation

79
Q

Some proteins are …. By phosphorylation while others are?

A

Activated, inhibited

80
Q

Adding a phosphate group adds?

A

Negative charges

81
Q

Ionic interactions in the unphosphorylated protein can be?

A

Disrupted and new ones created.

AH Biology - Unit 1 (5 decks)

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