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Advanced Higher Biology > Proteonomics > Flashcards

Proteonomics Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

What is a genome?

A

The genome is all of the hereditary information encoded in DNA

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2
Q

What is the proteome

A

the proteome is the entire set of proteins expressed by a genome

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3
Q

The proteome is larger than the number of genes, particularly in eukaryotes, because of?

A

Alternative RNA splicing (one gene many proteins)

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4
Q

Factors affecting the set of proteins expressed by a given cell type?

A

metabolic activity of the cell, cellular stress, the response to signalling molecules, and diseased versus healthy cells

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5
Q

What are genes not coding for a protein called? examples?

A

non-coding RNA genes
tRNA, rRNA and RNA

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6
Q

Why do eukaryotic cells have a system of internal membranes?

A

to increase total area of membranes and provides a larger surface area for vital functions to take place

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7
Q

Describe the ER

A

forms a network of membrane tubules continuous with the
nuclear membrane

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8
Q

Describe the Golgi apparatus

A

series of flattened membrane discs

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9
Q

Describe lysosomes and their function

A

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

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10
Q

Role of vesicles?

A

transport materials between membrane compartments

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11
Q

What is synthesised in the ER?

A

Lipids and proteins

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12
Q

Synthesis of lipids?

A

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

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13
Q

Where does the synthesis of all proteins start?

A

cytosolic ribosomes

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14
Q

Pathway of synthesis for cytosolic proteins?

A

Completed in the cytosolic ribosome and remain in the cytosol

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15
Q

Examples of cytosolic proteins?

A

Nucleus, mitochondria and chloroplasts

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16
Q

Pathway of synthesis for transmembrane protein

A

Cytosolic ribosome
Transmembrane proteins carry a signal sequence, which halts translation and directs the ribosome synthesising the protein to dock with the ER, forming RER
Translation continues after docking, and the protein is inserted into the membrane of the ER

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17
Q

How do proteins travel in the ER

A

they are transported by vesicles that bud off from the ER
and fuse with the Golgi apparatus

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18
Q

What happens as proteins move from the Golgi Apparatus?

A

they undergo post-translational modification

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19
Q

What are examples of post-translational modifications

A

addition of carbohydrate groups is the major modification
phosphorylation and a disulphide bond

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20
Q

Vesicles that leave the Golgi apparatus take proteins where?

A

plasma membrane and lysosomes

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21
Q

How do vesicles travel along a cell?

A

move along microtubules to other membranes and fuse with them within the cell

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22
Q

Pathway of secreted proteins

A

Secreted proteins are translated in ribosomes on the RER and enter its lumen
The proteins move through the Golgi apparatus and are then packaged into secretory vesicles
These vesicles move to and fuse with the plasma membrane, releasing the proteins out of the cell

23
Q

Many secreted proteins are synthesised as inactive precursors and require what to produce active proteins?

A

proteolytic cleavage

24
Q

Examples of secreted proteins?

A

insulin and trypsin

25
Q

Amino acids are linked by?

A

peptide bonds to form polypeptides

26
Q

What four R groups are present on amino acids

A

basic (positively charged); acidic (negatively charged); polar; hydrophobic

27
Q

Diversity of R groups lead to

A

The wide range of functions carried out by proteins

28
Q

What is primary structure?

A

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

29
Q

What is secondary structure and examples?

A

Hydrogen bonding along the backbone of the protein strand results in regions of secondary structure
alpha helices, parallel or anti-parallel beta-pleated sheets, or turns

30
Q

Tertiary structure?

A

folded polypeptide

31
Q

How is tertiary structure stabilised?

A

R group interactions like hydrophobic interactions;
ionic bonds; London dispersion forces; hydrogen bonds; disulfide bridges

32
Q

What is quaternary structure?

A

proteins with two or more connected polypeptide subunits

33
Q

What is a prosthetic group?

A

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

34
Q

How can pH and temperature influence R groups?

A

Increasing temperature disrupts the interactions that hold the protein in shape; the protein begins to unfold, eventually becoming denatured.
As pH increases or decreases from the optimum, the normal ionic interactions between charged groups are lost, which gradually changes the conformation of the protein until it becomes denatured.

35
Q

What is a ligand?

A

substance that can bind to a protein

36
Q

What can bind to a ligand?

A

R groups not involved in protein folding

37
Q

Describe binding site for a ligand?

A

complementary shape and chemistry to the ligand

38
Q

What happens when a ligand binds?

A

conformation of the protein changes which causes a functional change in the protein

39
Q

Allosteric interactions occur?

A

between spatially distinct sites

40
Q

Structure of many allosteric proteins?

A

consist of multiple subunits (have quaternary structure)

41
Q

Allosteric proteins with multiple subunits show co-operativity in binding which means?

A

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

42
Q

Allosteric enzymes contain a second type of site called?

A

an allosteric site

43
Q

Function of modulators?

A

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

44
Q

What happens when a modulator binds?

A

conformation of the enzyme changes and this alters
the affinity of the active site for the substrate. Negative modulators reduce the enzyme’s affinity for the substrate and positive modulators increase the enzyme’s affinity for the substrate.

45
Q

Example of protein that shows co-operativity?

A

haemoglobin

46
Q

Describe structure of haemoglobin?

A

demonstrates quaternary structure in that is made up of four polypeptide subunits, each of which contain a haem group capable of binding a molecule of oxygen

47
Q

What are the two main factors that affect haemoglobin’s ability to bind to oxygen

A

temperature - as temperature increases, affinity for oxygen decreases, curve shifts right
pH - as pH decreases, affinity for oxygen decreases, curve shifts right

48
Q

The addition and removal of phosphate can cause?

A

reversible conformational change in proteins

49
Q

Function of kinases?

A

catalyse the transfer of a phosphate group to other proteins

50
Q

the terminal phosphate of ATP is transferred to?

A

specific R groups

51
Q

Function of phosphotase

A

catalyses dephosphorylation

52
Q

What does adding a phosphate group do to amino acids?

A

adds negative charge

53
Q

How to regulate the activity of many cellular proteins, such as enzymes and receptors

A

Phosphorylation brings about conformational changes, which can affect a protein’s activity

54
Q

What 2 outcomes can happen by phosphorylation of a protein?

A

Some proteins are activated by phosphorylation while others are inhibited

Advanced Higher Biology (7 decks)

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