Protein Structure and Function - Lecture 4 Flashcards

1
Q

What is a Primary Structure of Proteins?

A

A Sequence of amino acid residues

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2
Q

What is a Secondary Structure of Protein?

A

Localised conformation shape of the polypeptide backbone

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3
Q

What is the tertiary structure of protein?

A

The three dimensional structure of the entire polypeptide, including all its side
chains.

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4
Q

What is the Quaternary Structure of Proteins?

A

Spatial arrange of polypeptides chains in a protein with multiple chains.

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5
Q

What type of structures are amino acids?

A

Planar Structures

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6
Q

What bond helps form the secondary structure of proteins?

A

Hydrogen Bonds

Polypeptide Backbone

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7
Q

What are the examples of secondary structure?

A

Alpha Helix

Beta Sheet

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8
Q

How would you describe the type of twists in an alpha helix?

A

Right Handed Twists

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9
Q

What is Proline’s effect on an Alpha Helix?

A

Proline residues break alpha helices - Proline puts in a left handed 90 turn

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10
Q

What are the two types of Beta Sheets?

A

Parallel

Aniparallel

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11
Q

Describe the structure of a Beta Sheet?

A

Polypeptide backbone almost completely extended.

Beta Pleated sheets have a zigzag structure

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12
Q

What is Collagen?

A

Component of Bone or Connective Tissue

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13
Q

What is the repeating sequence of Collagen?

A

Amino Acid
Proline
Glycine

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14
Q

Describe the Strucutre of Collagen?

A

Beta Pleated sheets have a zigzag structure
Can have flat sheets or pleated sheets
There are only inter-chain H bonds, no intra chain.
There are inter and intra-molecular covalent bonds.

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15
Q

What are the two groups of Tertiary Protein?

A

Fibrous Protein

Globular Protein

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16
Q

What are the features of a Fibrous Protein?

A

Insoluble in water and dilute salt solutions

Polypeptide chains organised approximately parallel along a single axis.

Mechanically strong

Structural roles.

17
Q

What are the features of a Globular Protein?

A

Soluble in water and salt solutions

Spherical shapes.

Polar side chains are on the outside and interact with the aqueous environment

Non polar components are buried inside

Substantial Secondary Structures articulate

18
Q

What are the forces that stabilies a tertiary protein?

A

Covalent disulphide bonds

Electrostatic interactions = salt bridges

Hydrophobic interactions

Complex formation with metal ions

19
Q

What are the features of a Disulphide bond?

A

Readily reversible

Detects oxygen free radicals, can cause ion channels to open and to
close

20
Q

What may occur to a protein if an amino acid is omitted?

A

Leads to significant functional changes

21
Q

What helps the folding process of a protein?

A

A Chaperone protein

22
Q

What causes Creutzfeldt -Jacob Disease?

A

Disease Prion Protein (PrPsc)

23
Q

What is the normal form of Prion Protein?

A

Normal form of Prion protein termed PrPc

24
Q

What is disruption of a protein called?

A

Denaturation

25
Q

How many Oxygen can Haemoglobin carry?

A

4

Each Haem group can carry one

26
Q

What is the redox centre of Haemoglobin?

A

Iron atom