Protein Structure And Types Flashcards

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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
Q

What enables haemoglobin to transport oxygen around the body

A

The iron (II) ions present in the haem group are each able to combine reversibly with an oxygen molecule

26
Q

Fibrous proteins characteristics

A
  • long, insoluble molecules
  • organised structures
  • not 3D shapes
27
Q

Why are fibrous proteins insoluble

A

Due to the presence of a high proportion of amino acids with hydrophobic R groups in their primary structures

28
Q

Examples of fibrous proteins

A

Keratin, elastin, collagen

29
Q

Function of fibrous proteins

A

Provides structural strength due to presence of many hydrogen bonds which results in great tensile strength