Proteins (B) Flashcards

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1
Q

What is the primary structure?

A

This refers to the sequence of amino acids in the polypeptide chain

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2
Q

What does the sequence of amino acids determine?

A

The specific shape of the protein

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3
Q

What type of chains are in the primary structure?

A

Long, straight chains

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4
Q

What exactly is bonded in the primary structure?

A

The H from the amine groups and the C=O from the carboxyl groups

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4
Q

What is the secondary structure?

A

Representing the folding or coiling of the polypeptide chain as a result of the hydrogen bonding between amine groups and carboxyl groups

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5
Q

Why do proteins have such a wide variety of roles?

A

This is because tertiary structures are specific and unique

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5
Q

What is the tertiary structure?

A

Further folding and coiling of the secondary structure, creating a unique 3D shape due to hydrogen bonds, ionic bonds and disulfide bonds.

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6
Q

What types of secondary structures exist?

A

Alpha helix and Beta pleated sheet

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7
Q

What does the tertiary structure of an enzyme determine?

A

The shape of its active site and its specific function

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8
Q

List the strengths of the bonds in a tertiary structure, weakest to strongest

A

Hydrogen bonds
Ionic bonds
Disulfide bonds

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9
Q

What is the quaternary structure?

A

When proteins consist of more than one polypeptide chain

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10
Q

What are these polypeptide chains held together by?

A

Ionic bonds, hydrogen bonds and disulfide bonds

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11
Q

What are the two types of proteins?

A

Globular
Fibrous

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12
Q

What are the features of globular proteins?

A

Are soluble in water
They include enzymes, antibodies and hormones
Consist of a highly folded and coiled polypeptide chain to produce a compact, complex tertiary structure

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13
Q

What are the features of fibrous proteins?

A

Are insoluble in water
Is a secondary structure made up of long polypeptide chains which can form sheets or fibres
The fibres give strength while the sheets give flexibility
Their structural roles in the body are due to their strength and flexibility

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14
Q

How is denaturation of a protein caused?

A

The breaking of hydrogen and ionic bonds
High temperatures above the optimum temperature
Extreme changes in pH
Heavy metals

15
Q

What is the denaturation of a protein?

A

An alteration in the tertiary structure of a protein
The loss of the 3D shape of the protein causes the protein to be no longer functional

16
Q

What is important to note about disulfide bonds strength?

A

They are not broken at the temperature which breaks hydrogen and ionic bonds. In some proteins the disulfide bonds can remain intact at temperatures as high as 70’C

17
Q

What is the test for proteins?

A

Add Biuret reagent
A purple or lilac colour indicates protein is present
If the solution remains blue, no protein is present