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Adv. Higher Bio > Proteomics, Protein Structure, Binding And Conformational change > Flashcards

Proteomics, Protein Structure, Binding And Conformational change Flashcards

(67 cards)

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1
Q

Define the proteome?

A

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

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2
Q

Define the genome

A

All the hereditary information encoded in DNA

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3
Q

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

A

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

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4
Q

What factors affect the set of proteins expressed by a given cell?

A

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

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5
Q

Genes that do not Cade for proteins are called ??? And include those that are transcribed to produce ??? That control ???

A

Non - coding RNA
tRNA, rRNA, and RNA molecules
The expression of other genes.

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6
Q

The plasma membrane of eukaryotic cells is too small an area to carry out all the vital functions carried out by membranes, why?

A

Eukaryotic cells have a relatively small surface area to volume ratio

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7
Q

What do eukaryotic calls have to increase total membrane area

A

Eukaryotic cells have a system of internal membranes, which increases the total area of membrane and provides a larger surface area for vital functions to take place.

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8
Q

Describe the endoplasmic reticulum and what it forms.

A

Forms a network of membrane tales continuous with the nuclear membrane tubules continuous with the nuclear membrane. Rough ER has ribosomes on its cytosolic face while smooth ER lacks ribosomes.

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9
Q

What is the Golgi apparatus? What does it allow? And where is it?

A

Series of flattened membrane discs.
The discs are connected to allow molecules to more within the Golgi apparatus
Golgi apparatus is adjacent to the endoplasmic reticulum.

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10
Q

What are lysosomes

A

Hyosomes are membrane-bound organelles containing a variety of hydrolyses that digest proteins, lipids, nuclei’s acids and carbohydrates.

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11
Q

What are the conditions of the interior of lysosomes and what are these conditions optimal for?

A

The interior is acidic allowing optimal function of the enzymes it contains.

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12
Q

What are vesicles and what do they do?

A

Vesicles transport materials between membrane compartments. They consist of an aqueous solution enclosed by a lipid bilayer

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13
Q

What are vesicles, endoplasmic reticulii, lysosome, Golgi apparatus all a part of?

A

The eukaryotic endomembrane system.

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14
Q

Where are lipids and proteins synthesised?

A

Endoplasmic reticulum

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15
Q

Describe lipid synthesis

A

Lipids are synthesised in the SER and inserted into its membrane

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16
Q

Where does the synthesis of all proteins begin?

A

In cytosolic ribosomes

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17
Q

Where is the synthesis of cytocylic proteins completed

A

In the cytosilic ribosome, and these proteins remain in the cytosol

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18
Q

What is the function of transmembrane proteins

A

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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19
Q

What is the signal sequence

A

The signal sequence is 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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20
Q

What happens once the proteins are 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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21
Q

What happens as proteins move through the Golgi apparatus

A

They undergo post-translational modification

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22
Q

What does the term ‘post-translational modification’ refers to

A

Modification that occur on a protein, catalysed by enzymes, after its translation by ribosomes is complete.

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23
Q

What is the transcriptome

A

The collection of RNA molecules produced by a genome is known as the transcriptone.

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24
Q

What are the 2 main forces of post-translational modifications?

A

Addition of chemical groups
Covalent modification

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25
What is the endoplasmic reticulum involved in?
- Involved in the synthesis and export of proteins and lipids - involved in the synthesis of membrane components (phospholipids and proteins ) - carbohydrate metabolism
26
What is the major modification taking place in the Golgi?
The addition of carbohydrate groups to proteins, carried out by enzymes
27
RER main function?
Synthesise proteins
28
SER main purpose
Synthesise lipids
29
Vesicles are used to...
Transfer proteins from the ER to the Golgi apparatus by cycles of budding and fusion
30
Addition of a carbohydrate group is also known as
Glycosylation
31
Where do lysosomes originate
By budding Off from the Golgi apparatus
32
Are the digestive enzymes contained in the lyosemes made
In the ER (but further processed in the Golgi apparatus
33
Vesicles containing proteins made in the ER (and hochbied in the Golgi apparatus) can be ...... From the cell
Exported
34
Describe exocytosis
After vesicles containing proteins made in the ER (and modified in the Golgi apparatus) are exported The vesicles which bud off from the Golgi then fuse with the cell membrane releasing proteins in a process called exocytosis
35
Alter exocytosis, what do vesicles do
Move along the microtubules to other membranes in the cell then fuse with them
36
Vesicles Move along the microtubules to other membranes in the cell then fuse with them What happens next
New vesicles can then bud off and more to another intracellular membrane giving rise to vesicle traffic moving along microtubutes
37
What is the function of the secretory pathway
Moves proteins from inside the cell, where they're synthesised to outside the cell using vesicles
38
What are 2 examples of secreted proteins
Peptide hormones Digestive enzymes
39
Describe the secretary pathway (in short)
Secreted proteins are translated in ribosomes on the RER and enter its lumen The proteins more through the Golgi apparatus where they'reprocessed then packaged into secretory vesicles These vesicles more to and fuse with the plasma membrane, releasing the proteins out of the cell
40
What is proteolytic cleavage?
Proteolytic cleavage is basically the process of breaking the peptide bonds between amino acids in proteins.
41
How are many secreted proteins synthesised
As inactive precursors
42
What do inactive precursors require to produce active proteins
Proteolytic cleavage
43
In the case of enzymes, what are inactive precursors
Proenzymes (or zymogens)
44
How can peptide hormones be activated
By proteolytic cleavage
45
What does proteolytic cleavage prevent
Digestive enzymes becoming active in an inappropriate location and causing damage to the cell
46
Proteins definition
Proteins are polymers of amino acid monomers
47
What does the R group of an amino acid determine
The r group attached to the central Carbon determines the characteristics of that amino acid.
48
How do r groups of amino acids vary
Size, charge, hydrogen bonding capacity and chemical reactivity.
49
Amino acids may be:
- Acidic: negatively charged - Basic: positively charged - polar - hydrophobic
50
The wide range of functions carried out by proteins results from...
The diversity of their R groups
51
Key features of acidic amino acids
- Acidic, negatively charged amino acids are hydrophilic and the key component of their R group is a carboxylic acid ( COOH ) group - when in solution, the COOH group will lose a hydrogen ion to form COO-, so is negatively charged.
52
Key features of basic amino acids
- Basic, positively charged amino acids are hydrophilic and the key component of their R group is an amine group ( NH↓2 ) - when in solution, the NH↓2 group will gain a hydrogen ion to form NH↑3+ so is positively charged
53
Six amino acids have... They are able to form... They are...
Side chains that are polar Hydrogen bonds Hydrophilic
54
Amino acids link by.... To form...
peptide bonds Polypeptides
55
The primary sequence is...
The order in which the amino acids are synthesised into the polypeptide
56
The primary structure determines..
All the higher levels of the paypeptides' structure (due to interaction of r-groups)
57
The amino acids along the length of the polypeptide chain interact with one another Some amino ands form hydrogen bonds which result in secondary protein structure:
- Alpha helices - Beta sheets - beta turns
58
Key features of a-helix
- One type of secondary structure - it is a spiral with the R groups sticking outwards - it is stabilised by hydrogen bonds
59
Key features of B-pleated sheet
-Formed when the polypeptide chain is arranged in rows - rows can run parallel or anti-parallel and are stabilised by hydrogen bonds - the R groups can sit above and below the sheet.
60
Key features of turns
- Turns are type of secondary structure; they reverse the direction of the polypeptide chain -This is when the polypeptide chain changes its overall direction without forming a helix or a street - they are stabilised by hydrogen bonds.
61
Tertiary structure refers to...
The overall final folded 3D shape of the polypepticle
62
What are bonds involved in folding in tertiary structure
-Ionic bonds - disulphide bridges (covalent bonds) - LDFs - hydrogen bonding - hydrophobic interactions
63
Describe hydrophobic interactions
Hydrophobic R groups are repelled by water and so usually end up on the inside of the polypeptide where they cluster away from water
64
Describe hydrophilic interactions
Hydrophilic amino acids will predominate at the surface of a soluble protein. This hydrophobic effect is one of the main driving forces oh protein folding
65
The cytoplasm is an... Medium so cytoplasmic proteins, such as enzymes, have to be...
Aqueous Soluble
66
The cytoplasm is an aqueous Medium so cytoplasmic proteins, such as enzymes, have to be soluble. What is in place to allow this?
The surface of the protein has a greater proportion of hydrophilic R groups Hydrophobic R groups cluster at the centre of the folded polypeptide chain to form a globular structure with a hydrophobic core
67
What is a disulfide bridge?
A covalent bond between two sulfur containing R groups of cysteines (sulphydry((SH)) in different parts of the polypeptide

Adv. Higher Bio (2 decks)

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