Proteins Flashcards

(32 cards)

1
Q

How is the R group positioned in an α helix protein structure?

A

Facing the outside where it can interact with the environment

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2
Q

What are the four levels of protein structure?

A

Primary, secondary, tertiary, and quaternary

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3
Q

What is primary protein structure?

A

Sequence of amino acids in a polypeptide chain

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4
Q

What determines a protein’s sequence of amino acids?

A

DNA

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5
Q

How can a change in DNA affect the protein?

A

It could change the protein structure or function by altering the amino acid sequence

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6
Q

What is a common disease caused by a primary protein mutation?

A

Sickle cell anemia

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7
Q

What causes sickle cell anemia?

A

An amino acid mutation in hemoglobin (glutamic acid –> valine)

The 6th amino acid on the beta chain

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8
Q

What is sickle cell anemia?

A

Hemoglobin molecules assemble as long fibers which causes red blood cells to have a crescent shape

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9
Q

What is secondary protein structure?

A

Proteins with local folds within their structure

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10
Q

Describe the bonding that creates a secondary protein structure.

A

Hydrogen bonding between the backbones

R groups aren’t involved!

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11
Q

What are the most common types of secondary protein structures?

A

α helix and the β pleated sheet

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12
Q

Describe the α helix protein structure.

A

Secondary structure that looks spiraled

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13
Q

Describe the β pleated sheet protein structure.

A

Secondary structure that looks folded

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14
Q

What bonds are involved in the α helix and the β pleated sheet protein structures?

A

Hydrogen bonds connect the carbonyl group to another amino acid’s amino group

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15
Q

What is the bonding pattern in an α helix protein structure?

A

The hydrogen bond between two amino acids that are 3 apart

ex. carbonyl on amino 1 binds to the amino on amino 5

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16
Q

How many amino acids are in each turn of an α helix protein?

A

3.6 amino acids

17
Q

How is the R group positioned in a β pleated sheet protein structure?

A

They extend above and below the lane

18
Q

What are the two types of β pleated sheet formations?

A

Parallel or antiparallel

19
Q

What is a parallel β pleated sheet?

A

The N and C terminals of each strand match up (point the same direction)

20
Q

What is an anti parallel β pleated sheet?

A

The N and C terminals of each strand don’t match up (point different directions)

21
Q

What amino acid is an example of a ‘helix breaker’?

A

Proline

Not compatible in an α helix

22
Q

What amino acids are commonly found in β pleated sheets?

A

Amino acids with large aromatic rings

ex. tryptophan, tyrosine, and phenylalanine

23
Q

What is a tertiary protein structure?

A

Three-dimensional folding pattern of a protein

24
Q

Where are the interactions that cause tertiary protein structure?

A

Between the side chains (R) of amino acids

25
What type of interactions are involved in the tertiary protein structure?
Non-covalent bonding (and disulfide bonds)
26
Explain hydrophobic interactions in tertiary proteins.
The non polar groups cluster together inside the proteins and the hydrophilic R groups are on the outside to interact with surrounding water molecules
27
What are disulfide bonds?
Bonds between two sulfur molecules
28
What are the strongest bonds contributions to the tertiary protein structure?
Disulfide bonds
29
What is quaternary protein structure?
Protein consisting of more polypeptide chains
30
What are two examples of molecules with quaternary protein structure?
Hemoglobin and DNA polymerase
31
What type of interactions are involved in the quaternary protein structure?
Hydrogen bonding and LDS
32
What does it mean for a protein to be denatured?
When a protein loses its structure but not sequence