1.The proteome Flashcards

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1
Q

What is the Proteome?

A

The Proteome is the entire set of proteins expressed by a genome.

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2
Q

Why is it important to study the Proteome?

A

It allows a greater understanding of the complexity of life and process of evolution than study of the genetic code alone. It shows how cells react to different circumstances.

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3
Q

What are the genes that do not code for proteins known as?

A

Non-coding RNA genes

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4
Q

What are non-coding RNA genes used to transcribe?

A

Transfer RNA, ribosomal RNA and RNA molecules that control the expression of other jeans.

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5
Q

What are factors affecting the set of proteins expressed by a given cell type include?

A

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

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6
Q

What happens to the surface area to volume ratio is the cell size increases?

A

Asda sell size increases the surface area to volume ratio decreases

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7
Q

What do eukaryotic cells have that increases the total surface area of membrane?

A

They have a system of internal membranes.

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8
Q

What is the smooth and rough endoplasmic reticulum?

A

It forms a network of membranes tubules that link into the nuclear membrane. It is involved with membrane synthesis.

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9
Q

What is the Golgi apparatus?

A

It is a series of flat and discs involved in protein secretion

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10
Q

What are lysosomes?

A

They are membrane-bound organelles containing a variety of hydrolyses that digest, proteins, lipids, nucleic, acid and carbohydrates.

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11
Q

What are hydrolyses?

A

Hydrolases digest proteins, lipids, nucleic acid and carbohydrates

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12
Q

What are vesicles?

A

Physicals are small spheres of membrane and they transport substances between membrane compartments.

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13
Q

What organelle is involved with the synthesis of phospholipids and proteins?

A

Endoplasmic reticulum

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14
Q

How are lipids synthesised?

A

The precursor is for lipid production are found floating in the cytosol. They are collected by enzymes of the smooth endoplasmic reticulum and once slipped synthesis is completed. They are inserted into the SER.

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15
Q

How does protein synthesis occur?

A

The synthesis of a protein begins in free cytosolic ribosomes.If the protein is destined to remain in the cytosol, then it’s synthesis will be completed in a cytosolic ribosome, and it will remain in the cytosol of the cell.

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16
Q

How is the decision made of water Putin will end up in a cell?

A

It’s made by a signal sequence. A signal sequence is a short stretch of amino acid at one end of the polypeptide being synthesised.

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17
Q

What happens if the protein is a transmembrane protein?

A

The signal sequence will direct the ribosome during synthesis to dock with the endoplasmic reticulum, forming the rough endoplasmic reticulum.

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18
Q

Explain the movement of proteins between membranes

A

Once proteins are in the ER, they are transported by vesicles that, bud off from the ER and fuse with the Golgi apparatus. To move proteins from one Golgi disc to another in the stack physicals board from one and fuse with another as the protein moves through the Golgi apparatus, post translational modification takes place. The major modification is the addition of carbohydrates. Vesicles leaving the Golgi apparatus take proteins to the plasma membrane and lysosomes vesicles will move along microtubules to fuse with other internal membranes of the cell.

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19
Q

What is post translational modification?

A

Post translational modification is the alteration of the protein after translation

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20
Q

What can post translational modification involve?

A

The addition of chemical groups and proteolytic cleavage

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21
Q

What is the secretory pathway in detail?

A

The protein for secretion is translated in the ribosomes on the RER and enter its lumen examples include peptide, hormones and digestive enzymes. The proteins move through the Golgi apparatus and undergo post translational modification and are then packaged into secretory vesicles. These vesicles move to and fuse with the plasma membrane, releasing the proteins out of the cell by exocytosis.

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22
Q

What is proteolytic cleavage?

A

It is another form of post translational modification and involves removing some of the protein which causes changes in the folding of the protein and allows its active confirmation to be formed.

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23
Q

Why do they need to be released in activated and then activated?

A

An active form inside a cell would be damaging, and so it is activated at the site of action.

24
Q

What are proteins?

A

Proteins are polymers of amino acid monomers.

25
Q

What does each amino acid contain?

A

They contain a carboxylic acid group and an amine group, both of which are bonded to the alpha carbon. They also have a hydrogen in variable our group that is bonded to the alpha carbon.

26
Q

What are R groups?

A

R groups differ between amino acids giving them different properties are groups vary in size, shape, charge, hydrogen bonding capacity and chemical reactivity.

27
Q

How are amino acids join together?

A

Buy a condensation reaction which forms peptide bonds and removes water hydrolysis is the breakdown of condensation links.

28
Q

Where is the amino acid bond?

A

It’s between the amine acid group of one amino acid and a carboxylic group of another

29
Q

What is a peptide bond?

A

Peptide bond is covalent in there for a very strong. Several amino acids are linked by peptide bonds are called a polypeptide.

30
Q

What are the four amino acid classified groups?

A

Acidic, basic, polar and hydrophobic

31
Q

What is the acidic group containing?

A

It is negatively charged with carbonyl or carboxylic group.

32
Q

What does the basic group contain?

A

It is positively charged with ammonia or ammonium groups

33
Q

What does the polar group contain?

A

It has differing charges with a hydroxide group

34
Q

What does a hydrophobic group contain?

A

It repels water and has a hydrocarbon R group

35
Q

What is a primary protein structure?

A

The primary structure of the sequence in which amino acids are synthesised into the polypeptide. It is determined by the order of faces on the DNA via protein synthesis.

36
Q

Why is the protium larger than the genome?

A

More than one protein is produced by one gene, and also due to alternative RNA splicing and post translational modification

37
Q

What is the bonding is found in primary structure

A

Peptide bonds

38
Q

What is the bonding is found in the secondary protein structure?

A

Hydrogen bonding

39
Q

What are the structures that can be found in secondary proteins?

A

Alpha helices and beta sheets

40
Q

What are the types of beta sheets?

A

Anti parallel, parallel, and turns

41
Q

What is the bonding is found in tertiary protein structure

A

Interactions between R groups. This can include hydrophobic interactions, London dispersion forces, hydrogen, bonding,ion salt bridges, and disulphide bonds.

42
Q

What are quaternary protein structures?

A

They are proteins that have two or more polypeptide chains are connected. They describe the spatial arrangement of the subunits.

43
Q

What bonding occurs in quaternary structure

A

Subunits are linked by bonding between there are groups not involved in tertiary structure

44
Q

What are prosthetic groups?

A

These are proteins that have non-protein groups associated with them and results in the function of a protein.

45
Q

What are the interactions of the R groups influenced by?

A

Temperature and pH

46
Q

What would be affected if the shape of a protein was changed

A

Receptor site shape, enzyme active site, shape of binding ligand e.g. loss of prosthetic group

47
Q

What happens if there is a change in pH from the optimum?

A

The increase or decrease from the optimum pH will affect the charges on the charged acidic and basic R groups in a protein. This causes ionic interactions between charged groups to be lost and gradually change the confirmation of the protein until it becomes denatured.

48
Q

what is a ligand?

A

A ligand is a substance that can bind to a protein

49
Q

What effect does a link and have when binding to a protein

A

It changes the confirmation of the protein

50
Q

What happens when the confirmation of a protein is changed?

A

It causes a functional change in the protein

51
Q

What is the name of a ligand that is binding to an allosteric site?

A

It’s called a modulator

52
Q

What does the binding of a modulator do to the enzyme?

A

The binding of modulator to an Alistair excite regulates the activity of the enzyme.

53
Q

What does a confirmational change caused by the binding of a modulator do

A

It’s affinity of the active site for the substrate.

54
Q

What are positive modulators?

A

The increase the enzyme affinity for the substrate by stabilising the enzymes active form.

55
Q

What do negative modulators do

A

They reduce the enzymes affinity for the substrate by stabilising the enzymes inactive form

56
Q

What is cooperative binding?

A

“Is finding as when I ligand binding at one side effects, a ligand binding at another