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Science For Med A ellen > Proteins > Flashcards

Proteins Flashcards

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Biology 101 flashcards
1
Q

Describe the primary structure of a protein.

A

The exact sequence of amino acid residues within the polypeptide chain.

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2
Q

Describe the secondary structure of a protein.

A

The spatial arrangement of amino acid residues which are close together in a linear sequence.
Results in alpha helix or Beta pleated sheet

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3
Q

Describe the tertiary structure of a protein.

A

The spatial arrangement of amino acid residues which are far apart in a linear sequence.
Held together by Hydrogen bonds, Disulphide Bridges, Van Der Waal forces, Ionic Interactions and Hydrophobic Interactions.

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4
Q

Describe the quaternary structure of a protein.

A

The spatial arrangement of individual polypeptide chains within a multi subunit protein.

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5
Q

What isomer of amino acids do proteins consist of?

A

L isomer

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6
Q

What type of bond links two amino acid residues in a polypeptide chain?

A

Peptide bond

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7
Q

What is the R group of Glycine?

A

H

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8
Q

What is the R group of Alanine?

A

CH3

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9
Q

What is the R group of Valine?

A

C(CH3)2H

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10
Q

What is the R group of Tyrosine?

A

CH2PHENOL

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11
Q

What is the R group of Lysine?

A

(CH2)4NH2

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12
Q

What degrees of the structure of a protein does denaturation effect?

A

Secondary and Tertiary.

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13
Q

What are the four main effects of denaturation of a protein?

A
  • Reduced solubility
  • Increased digestibility
  • Altered water binding ability
  • Loss of biological function
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14
Q

What is the mechanism of action of peptidases?

A

Cleavage of peptide bonds

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15
Q

What is the mechanism of action of exopeptidases?

A

Cleavage of one amino acid at a time

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16
Q

What is the mechanism of action of endopeptidases?

A

Cleavage of internal bonds

17
Q

What is the mechanism of action of carboxypeptidases?

A

Cleavage at the -COOH terminal

18
Q

What is the mechanism of action of aminopeptidases?

A

Cleavage at the -NH2 terminal

19
Q

What are glycoproteins?

A

Structures composed of proteins and carbohydrates

20
Q

Where does glycosylation occur?

A

At the ER and Golgi Apparatus

21
Q

What are the functions of glycosylation?

A
  • Proteins stabilisation
  • Protein Orientation
  • Affects solubility
  • Creates compounds which can be used for signalling and cell to cell recognition.
22
Q

What are lipoproteins?

A

Structures containing proteins and lipids covalently or non-covalently bonded together,

23
Q

What is the function of lipoproteins?

A

The transport of water insoluble fats and cholesterol in the blood.

24
Q

What are metalloproteins

A

Protein molecules with a bound metal ion

25
Q

What is the role of haemoglobin?

A

Transport oxygen in the blood

26
Q

What type of protein is haemoglobin?

A

Quaternary metalloprotein

27
Q

What is meant by ‘cooperative binding’ of oxygen to haemoglobin?

A

Once one oxygen has bound to one haem group in the haemoglobin molecule, a conformational change occurs, making it easier for a second oxygen molecule to bind to a second haem group. This process repeats for the third and fourth haem group/ oxygen binding process.

28
Q

What is a peptide bond?

A

Covalent bond formed between the amino group on one amino acid and the carboxyl group on another. Involves the elimination of a H20 molecule.

29
Q

At what part of the cell should a peptide bond form?

A

At the ribosome

30
Q

What structure of a protein will not be affected by denaturation?

A

Primary structure

31
Q

What is the difference between fibrous and globular proteins?

A

Fibrous proteins are non- water soluble and have their function in support and structure.
Globular proteins are water soluble and have their function in metabolic reactions (enzymes)

Science For Med A ellen (20 decks)

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