Lesson 5: Protein Folding Flashcards

1
Q

What does the primary structure of a protein determine ?

A

It determines how a protein will fold

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2
Q

Why is the primary structure formed ?

A

Due to the peptide bonding

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3
Q

What are the 2 examples of chaperones ?

A

hsp70 and hsp60

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4
Q

What do the 2 chaperons we learned stop ?

A

The aggregation of proteins

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5
Q

What causes Alzeheimer’s ?

A

Accumalation of B-amyloid

solube aplha rich state –> insoluble B-rich state

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6
Q

Which structures can renature ?

A

Secondary, Tertiary, Quaternary,

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7
Q

What structure is the protein first biologically active ?

A

Tertiary

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8
Q

What determines the tertiary strcutre of proteins ?

A

the interactions between the functional groups of side chains

disulfide bond, h-bond, hydrophobic interactions, salt-bridge

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9
Q

What are domains ?

A

Parts of the protein that serve a specific function

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10
Q

What determines the Quaternary structure ?

A

The covalent and non covalent interactions between subunit surfaces

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11
Q

T/F: Hemoglobin is a dimeric protein.

A

False, Tetrameric

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12
Q

What happens to the solubility and viscosity of a denatured protein ?

A

Solubility decreases and viscosity increases

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13
Q

What does the quaternary structure define ?

A

The number&type of polypeptide & their spatial arrangment

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14
Q

What determines the secondary structure ?

A

The H-bond interactions

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15
Q

How many amino acid residues are found per turn of helix ?

A

3.6

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16
Q

Where do Gly & Pro residues occur ?

A

In the B-turns on the surface of globular proteins.