Session 5 (Protein Structure And Function + Mitosis) Flashcards

1
Q

What happens is there are more than 2 centrosomes/ centrioles?

A

You get multi polar spindles

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2
Q

What are targeted often in cancer treatments?

A

Mitotic spindles (no cell division=cell death)

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3
Q

Give an example of a drug that interferes with microtubules?

A

Taxanes (taxol)

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4
Q

What are the two types of chromosome instabilities?

A

Structural and numerical

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5
Q

What is the molecular glue that holds sister chromatids together?

A

Cohesin (makes centromere)

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6
Q

What is pK?

A

The pH at which 50% of an amino acid is deprotonated and 50% is in protonated form

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7
Q

What is the isoelectric point? (pI)

A

The pH at which a molecule has no net charge

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8
Q

What happens if:
A) pHpK
C) pI<7
D) pI>7

A

A) amino acid will be protonated
B) amino acid will be deprotonated
C) protein is acidic
D) protein is basic

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9
Q

State the main difference between 2nd and 3rd protein structures?

A

Secondary- local spacial arrangement of backbone only

Tertiary- spacial arrangement of amino acids that are far apart in structure

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10
Q

What are conjugated proteins?

A

Proteins with chemical components covalently bonded ie haem, zinc etc

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11
Q

Describe the different types of protein (2)

A

Fibrous-support, shape, protection,
Long sheets and strands, repeating 2nd structure
Globular- catalysis and regulation
Compact, several structures within

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12
Q

What are electro static interactions?

A

Interactions involving charge

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13
Q

What bonding do you get at the different protein structure levels?

A

1- covalent
2- hydrogen
3+4- covalent, ionic, hydrogen, hydrophobic, disulphide

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14
Q

What shape are peptide bonds?

A

Planar

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15
Q

Why can the bond between 2 amino acids not rotate?

A

Because the bond is partially double bond (you get resonance)

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16
Q

What conformation do peptide bonds exhibit?

A

Trans-conformation

Cis is repelled

17
Q

How are protein structures reached?

A

Trial and error, localised folding,and with stable conformation, is maintained

18
Q

What d you call a protein with an abnormal structure?

A

Amyloid

19
Q

What do you need to consider when classifying an amino acid? (3)

A

Charges
Acidity
Interactions (bonding)

20
Q

What charge do acidic side chains have?

A

Negative

21
Q

What are aliphatic molecules?

A

A hydrocarbon chain

22
Q

What does an increased ka mean for acids?

A

It means they’re stronger so dissociate more