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Biology > U1: KA2 - Proteins > Flashcards

U1: KA2 - Proteins Flashcards

(60 cards)

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1
Q

What is genomics?

A

Study of the genome

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2
Q

What is the genome?

A

Total genetic material in a cell

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3
Q

What is the proteome?

A

Entire set of proteins expressed by a genome.

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4
Q

Why is the proteome larger than the number of genes?

A

More than one protein can be produced from a single cell due to alternative RNA splicing

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5
Q

What are non-coding RNA genes transcribed to produce?

A

tRNa, rRNA, RNA molecules that control the expression of other genes

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6
Q

What factors affect the set of proteins expressed?

A

Metabolic activity, cellular stress, response to signaling molecules, diseased versus healthy cells

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7
Q

What kind of membranes do eukaryotic cells have?

A

Plasma membrane

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8
Q

What increases the total area of the membrane on a eukaryote?

A

Internal membranes

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9
Q

Which structures have a membrane in the cell in a eukaryote?

A

Endoplasmic Reticulum
Golgi apparatus
Lysosomes
Vesicles

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10
Q

What does the ER do?

A

Forms a network of membrane tubules with the nuclear membrane

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11
Q

What is the difference between RER and SER?

A

RER has ribosomes on its cytosolic face.
SER lacks ribosomes

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12
Q

The golgi apparatus is a series of?

A

Flattened membrane discs

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13
Q

What is a lysosome?

A

Membrane bound organelle consisting of a variety of hydrolases.

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14
Q

What is a hydrolase?

A

Enzyme that digest proteins, lipids, nucleic acids and carbohydrates.

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15
Q

What is a vesicle?

A

Transports materials between membrane compartments.

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16
Q

Where are lipids and proteins synthesised?

A

Endoplasmic reticulum

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17
Q

How are lipids synthesised?

A

In SER and then inserted into its membrane.

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18
Q

Where does protein synthesis begin?

A

cytosolic ribosomes

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19
Q

How are cytosolic proteins made?

A

Completed in the cytosolic ribosome and remain in the cytosol.

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20
Q

How are transmembrane proteins made?

A

They 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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21
Q

What is a signal sequence?

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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22
Q

How are proteins transported after they are made?

A

By vesicles that bud off from ER and fuse with the golgi apparatus.

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23
Q

How do molecules move through the golgi apparatus?

A

In vesicles that bud off from one disc and fuse to the next one in a stack.

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24
Q

As proteins move through the golgi apparatus they undergo post-translational modification what is this?

A

When polypeptide chains have carbohydrates or phosphates added to them or are cleaved to make them an active protein.

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25
Enzymes catalyse the addition of various sugars in multiple steps to from what?
Carbohydrates
26
Vesicles that leave the golgi apparatus take proteins where?
The plasma membrane and lysosomes.
27
Vesicles move along microtubules to other membranes and fuse with them within the cell what are microtubules?
Structures that make up the cells cytoskeleton and offer support and a means of transport.
28
What are secreted substances?
Made inside the cell and released outside. E.g - Peptide hormones and digestive enzymes.
29
Where are secreted substances packaged?
Secretory vesicles
30
Secreted proteins often synthesised as inactive precursors and require what to produce active proteins?
Proteolytic cleavage
31
What is proteolytic cleavage?
Post-transitional modification where the polypeptide is cut.
32
Proteins are ploymers of what?
Amino acid monomers
33
What are amino acids linked by?
Peptide bonds to form polypeptides
34
What is a peptide bond
strong covalent bond between carbon atom of one amnio acid and nitroghen of another. water is removed
35
What are the 4 types of amino acids?
Polar Hydrophobic Acidic Basic
36
Describe acidic amino acids.
Ends with negatively charged Hydrophillic Carboxylic acid side chain
37
Descibe Basic R group amino acids.
Ends with positively charged group hydrophillic amino acid side chain
38
Describe polar R group amino acids.
Slightly charged hydrophillic amino acid side chain
39
Describe hydrophobic r group amino acids.
Non-polar no charges hydrophobic hydrocarbon chain
40
What is a primary sequence protein?
N-terminus at one end and a C-terminus at the other end./ order in which amino acids are synthesised
41
What is a secondary protein?
Hydrogen bonding along the backbone of the protein strand results in regions of the secondary structure.
42
What is the difference between alpha helix and beta sheet?
Alpha helix is formed by twisting the peptide chain and stabilising with hydrogen bonding where as beta sheets are formed by parts of the chain running alongside each other.
43
What are Turns?
A type of secondary structure that reverse the direction of the polypeptide chain and the chain folds back on itself
44
The tertiary structure is the final folded shape, its stabilised by many different interactions such as?
Hydrophobic interactions Ionic bonds ldfs hydrogen bonds disulphide bridges
45
What proteins does quaternary structure exist in?
Proteins with two or more connected polypeptide subunits which are linked by bonds between the R groups of the polypeptide chains
46
What is quaternary structure?
The spatial arrangement of the subunits
47
What is a prosthetic group?
Non-protein unit tight;y bound to a protein and necessary for its funtion.
48
What happens to a protein with an increase of temperature?
Disrupts interactions that hold protein in shape so protein unfolds and eventually becomes denatured.
49
What happens to a protein with a change to pH?
Normal ionic interactions between charged groups are lost so conformation of the protein changes becoming denatured.
50
Describe ligand binding.
R groups not involved in protein folding allow ligand binding. Binding sites have complementary shapes to ligand as it binds the conformation changes causing a functional change.
51
What is an allosteric enzyme?
Activity regulated by altering conformation. Consist of multiple sununits. Allosteric interactions occur between spatially distinct sites.
52
What is a modulator?
Regulates activity of enzyme when binds to allosteric site.
52
What are the 2 types of modulators and what do they do?
Positive - increase enzyme activity Negative - decrease enzyme affinity
52
What is cooperativity?
Changes binding at one subunit alter the affinity of remaining subunits
53
The binding of a substrate to one active site of an allosteric enzyme does what?
Increases the affinity of the other active sites. this is of biological importance because activity of allosteric enzymes can vary greatly with a small change in substrate concentration.
54
What can phosphorylation of proteins cause?
reversible conformational changes in proteins.
55
What are protein kinases?
Enzymes that catalyse the transfer of a phosphate group to other proteins.
56
What happens to the terminal phosphate of ATP?
transferred to specific R groups
56
What are protein phosphatases?
Transfer phosphate group from proteins onto ADP to regenerate ATP/ catalyse removal of phoshpate from a protein.
57
What does phosphorylation bring about in a protein?
Conformational changes some proteins activated while others inhibited Adding a phos[hate group adds negative charges.

Biology (13 decks)

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