Cells And Proteins Flashcards

(35 cards)

1
Q

Why is having a cytoskeleton important to a cell?

A

Retains cell shape, keeps structure of cell and things in the correct place.

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2
Q

What is the cytosol and what cellular functions take place there?

A

Metabolism, contains cytoskeleton so allows things to move through the cell

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3
Q

Why do cells need lysosomes and peroxisomes?

A

Lysosomes- mainly degrade proteins
Peroxisomes- remove H2O2 and other toxic substances, as well as lipids

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4
Q

Why does a mitochondrion need a double membrane to produce energy for the cell?

A

To set up a Proton gradient, for the ETC. Inner membrane increases SA for ETC, in cellular respiration

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5
Q

Why are the functions of the Golgi apparatus required in a cell?

A

Needed to package proteins and add components to proteins, finishing protein synthesis. Makes lysosomes

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6
Q

What are the functions of the endoplasmic reticulum and what is the difference in function between “rough” and smooth endoplasmic reticulum?

A

Smooth has no ribos; rough does.
Smooth- processes lipids

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7
Q

What cellular functions does the nucleus perform ?

A

Stores DNA in form of chromatin. Most of the DNA in a eukaryotic cell is stored inside of it.

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8
Q

What do microtubules do?

A

Provide a structure for things to prove through or from

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9
Q

What is the primary structure of a protein?

A

Aa sequence

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10
Q

What’s the secondary structure of a protein?

A

Initial folding of pp chain

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11
Q

What’s the tertiary structure of a protein?

A

The overall shape

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12
Q

What are chaperones?

A

Proteins that help other proteins fold

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13
Q

How are peptide bonds between amino acids formed?

A

Carboxylic acid group of 1 aa reacts w amine group of another

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14
Q

Types of R group

A

Charged, non-polar aliphatic, polar uncharged (hydrophobic), aromatic

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15
Q

What determines amino acid properties

A

The R group

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16
Q

What determines protein structure?

A

R groups, environment, chaperones

17
Q

What type of bond stabilises alpha helixes (and beta pleated sheets) within the secondary protein structure?

A

H bonds. R groups face outwards

18
Q

How is the tertiary structure of a protein determined?

A

By the lowest energy route. Ie not -ve and -ve, or hydrophobic and hydrophilic next to each other

19
Q

What’s the quaternary structure of a protein?

A

A complex of 1 or more pp chain

20
Q

Types of tertiary protein structures

A

Beta pleated sheet, fibrous, globular, helix

21
Q

How do we determine protein structure (shape)?

A

X ray cystallography, NMR

22
Q

Why may proteins be globular?

A

For secretion

23
Q

Why may proteins be elongated?

24
Q

What do multi-polypeptide complexes contain?

A

Homomers or Heteromers. Eg haemoglobun

25
Describe how proteins aren’t rigid structures
Conformation is flexible and dynamic Post translational modification (phosphorylation) Function due to changes in conformation- eg enzyme and substrate
26
Protein functions (4)
Binding- ligands, receptors Catalysis Switching- cell signalling pathways Structural- cytoskeleton
27
What’s the regulatory protein for the cell cycle’s CdK?
Cyclin
28
What’s CdK?
Cyclin dependent kinase. The catalytic protein in regulating the cell cycle.
29
Where does P53 tumour suppressor protein bind?
To DNA, to control transcription
30
Why do we need to know about proteins?
To target them with drugs. Eg blocking active site
31
Where are most proteins synthesised?
On ribosomes on the rER
32
What directs proteins to the correct site in the cell as part of localisation?
Sorting signals
33
What transports proteins from 1 compartment to another?
Transport vesicles
34
What do specialised cells have for carrying the secretions?
Secretory vesicles . They store hormones, enzymes,. They require an extracellular signal for exocytosis
35
What are the 3 aa that phosphate covalently bonds to on the side chains?
Tyrosine, serine, Theronine