Protein Structure Flashcards

1
Q

Structure of a protein

A

NH2, C00H and R group

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2
Q

How many amino acids are there

A

20

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3
Q

R group types

A

Non-polar aliphatic (hydrophobic)
Aromatic (hydrophobic and carbon ring)
Polar (uncharged and hydrophilic)
+ and - charged (hydrophilic at ph7)

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4
Q

What is the primary structure

A

Sequence of amino acids linked by peptide bonds

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5
Q

The primary structure is rigid and planar as

A

The bond has a partial double bond character

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6
Q

Amino acids are folded into shape by

A

Electrostatic attractions, Hydrogen bonds, Vanderwall’s attractions and disulphide bonds

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7
Q

What is a secondary structure

A

Beta pleated sheet, alpha helix, beta turns

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8
Q

The beta sheet is either

A

Antiparallel- one up and one down from C to N and and vice versa
Parallel – hydrogen bonds form between chains

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9
Q

Alpha helix has internal

A

Hydrogen bonds

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10
Q

Beta turn Connect 

A

Secondary structures and make a kink in chain of beta sheets or alpha helix

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11
Q

Tertiary structure is

A

3-D structure of folded protein

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12
Q

The quaternary structure is

A

Several chains put together e.g. haemoglobin

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13
Q

What is entropy

A

The measure of disorder

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14
Q

The primary structure determines

A

The tertiary structure

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15
Q

Proteins from generating a structure with the lowest

A

Free energy (entropy)

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16
Q

What interactions are important in protein folding

A

Hydrophobic

17
Q

What drives folding and maintains the overall structure

A

Hydrophobic core

18
Q

What happens when a protein is unfolded

A

Hydrophobic collapse to form molten globule, internal core rearrangement to form native event

19
Q

Proteins are folded into multiple

A

Domains

20
Q

Domains have a specific function e.g.

A

DNA binding, spanning plasma membranes

21
Q

What does chaperones do in protein domains

A

Guide proteins to fold correctly

22
Q

What happens in protein denaturation

A

Solvents that break noncovalent interactions cause the protein to unfold
Some proteins recover and refold

23
Q

Protein mutations  are

A

A change in amino acid sequence which alters its tertiary structure and causes inherited disorders eg sickle cell anaemia

24
Q

What is a signal sequence

A

A group of an amino acid which determines where the proteins will go (ReR, golgi etc)
If there is no sequence then they will go to the cytosome