Protein Structure And Types Flashcards

1
Q

The sequence of amino acids in a polypeptide chain is called the […] structure of a protein

A

Primary

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2
Q

In a polypeptide there is always one end with a free amino group called the […] and one with a free carboxyl group called the […]

A

N-terminus, C-terminus

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3
Q

When does a proteins secondary structure form

A

When a chain of amino acids coils to form an alpha helix or folds into a beta pleated sheet

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4
Q

What bonding between the amine and carboxyl groups is needed for the proteins secondary structure to form

A

Hydrogen bonding

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5
Q

What happens for the protein to form it’s tertiary structure

A

The secondary structures fold up to form a precise 3D structure

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6
Q

What R group interactions are in the tertiary structure as

A

Hydrophobic and hydrophilic interactions (weak interactions between polar and non-polar R-groups, no actual bonds)

-Hydrogen bonds (weakest of the bonds formed)

-Ionic bonds (form between oppositely charged R-groups)

-Disulphide bonds/bridges (covalent bonds and the strongest, only form if the R-group contains sulfur atoms)

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7
Q

What can split the hydrogen bonds in the tertiary structure

A

High temperatures / altered pH

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8
Q

How do quaternary structure proteins form

A

Because of the interactions of the tertiary structures of the different subunits

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9
Q

What are multiple polypeptide chains called

A

Subunits

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10
Q

Haemoglobin is an example of a […] protein with a […] structure

A

globular, quaternary

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11
Q

Summary of each type of structure found in proteins

A
  • The primary structure of a protein is the sequence of amino acids, joined by peptide bonds

• The secondary protein structure occurs when the sequence of amino acids are linked by hydrogen bonds in an alpha helix or beta pleated sheets

• The tertiary structure describes the folding of a polypeptide chain that result from the molecular interactions among the R groups of the different amino acids (H, disulphide, ionic bonds)

• The arrangement of two or more polypeptide chains in a protein make up its quaternary structure

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12
Q

Properties of globular properties

A
  • compact
  • water soluble
  • roughly spherical in shape
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13
Q

How come globular proteins are water soluble

A

In their tertiary structure they fold so their hydrophobic R-groups are kept away from the aqueous environment, and the hydrophilic R-groups are on the outside in the aqueous environment

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14
Q

What are conjugated proteins

A

globular proteins that contain a non-protein component called a prosthetic group

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15
Q

Lipids combined with proteins =

A

Lipoproteins

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16
Q

Carbohydrates combined with proteins =

A

Glycoproteins

17
Q

Metal ions and vitamins can also form […] groups

A

Prosthetic

18
Q

Fibrous proteins characteristics

A
  • tend to make strong long molecules which don’t fold into complex three dimensional shapes like globular proteins
19
Q

Why do fibrous proteins have organised structures (due to…)

A

• Fibrous proteins being formed from long insoluble molecules
•This is due to the presence of a high proportion of amino acids with hydrophobic R-groups in their structure
•The amino acids sequence in the primary structure is usually quite repetitive, therefore it’s organised

20
Q

Function of globular proteins

A
  • acting as enzymes
  • messengers
  • transport molecules
    -acting as hormones
21
Q

Function of conjugated proteins

A

Provide structure and support for cells

22
Q

Whats a prosthetic group

A

A non-amino acid unit e.g sugar or a nucleic acid

23
Q

Haemoglobin is made from […] polypeptides, […] alpha and 2 […] subunits

A

4, 2, beta

24
Q

Each haemoglobin subunit contains a […] group

A

Prosthetic haem

25
What enables haemoglobin to transport oxygen around the body
The iron (II) ions present in the haem group are each able to combine reversibly with an oxygen molecule
26
Fibrous proteins characteristics
- long, insoluble molecules - organised structures - not 3D shapes
27
Why are fibrous proteins insoluble
Due to the presence of a high proportion of amino acids with hydrophobic R groups in their primary structures
28
Examples of fibrous proteins
Keratin, elastin, collagen
29
Function of fibrous proteins
Provides structural strength due to presence of many hydrogen bonds which results in great tensile strength