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Molecules to Medicine > Cells And Proteins > Flashcards

Cells And Proteins Flashcards

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Organic Chemistry 101 flashcards
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?

A

For strength

24
Q

What do multi-polypeptide complexes contain?

A

Homomers or Heteromers. Eg haemoglobun

25
Q

Describe how proteins aren’t rigid structures

A

Conformation is flexible and dynamic
Post translational modification (phosphorylation)
Function due to changes in conformation- eg enzyme and substrate

26
Q

Protein functions (4)

A

Binding- ligands, receptors
Catalysis
Switching- cell signalling pathways
Structural- cytoskeleton

27
Q

What’s the regulatory protein for the cell cycle’s CdK?

A

Cyclin

28
Q

What’s CdK?

A

Cyclin dependent kinase. The catalytic protein in regulating the cell cycle.

29
Q

Where does P53 tumour suppressor protein bind?

A

To DNA, to control transcription

30
Q

Why do we need to know about proteins?

A

To target them with drugs. Eg blocking active site

31
Q

Where are most proteins synthesised?

A

On ribosomes on the rER

32
Q

What directs proteins to the correct site in the cell as part of localisation?

A

Sorting signals

33
Q

What transports proteins from 1 compartment to another?

A

Transport vesicles

34
Q

What do specialised cells have for carrying the secretions?

A

Secretory vesicles . They store hormones, enzymes,. They require an extracellular signal for exocytosis

35
Q

What are the 3 aa that phosphate covalently bonds to on the side chains?

A

Tyrosine, serine, Theronine

Molecules to Medicine (1 decks)

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