Proteins Flashcards

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1
Q

What is a protein?

A

A protein is a macromolecule consisting of monomers called amino acids. They arranged in particular structures and arrangements to allow specific functionality.

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2
Q

Describe the broad structure of an amino acid.

A

Amino group (NH2), side chain/residue, carboxyl group (COOH)

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3
Q

How many amino acids are there?

A

20

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4
Q

What gives amino acids their specificity?

A

The residue side chain.

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5
Q

Are amino acids chiral?

A

Yes- they have a carbon attached to four non-carbon other groups giving an asymmetric approach.

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6
Q

What are the 7 types of amino acid?

A
Aliphatic 
Aromatic 
Sulfur
Basic 
Acidic 
Polar 
Miscellaneous
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7
Q

What does the R-group of aliphatic amino acids contain?

A

Hydrocarbons

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8
Q

What does the R-group of aromatic amino acids contain?

A

Benzene ring

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9
Q

What does the R-group of sulphur amino acids contain?

A

Sulfur

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10
Q

What does the R-group of basic amino acids contain?

A

NH group

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11
Q

What does the R-group of acidic amino acids contain?

A

COOH group

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12
Q

What does the R-group of polar amino acids contain?

A

Electronegativity

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13
Q

What does the R-group of miscellaneous amino acids contain?

A

Does not fit with any other.

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14
Q

What is the primary structure?

A

The initial sequence of amino acids in the polypeptide chain.

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15
Q

What is the secondary structure?

A

The initial chain of AA folds to form structures called alpha-helices and beta-pleated sheets, held by hydrogen bonding.

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16
Q

How is secondary structure stabilised?

A

Hydrogen bonding.

17
Q

How is tertiary structure established?

A

Tertiary structure results through the reactions of functional groups in the residue chains of amino acids, These include ionic bonds, further hydrogen bonds, hydrophobic interactions, VDW forces, hydrophilic reactions and disulfide bridges.

18
Q

How does tertiary structure occur?

A

Quarternary structure occurs when there are multiple chains interacting with each other.

19
Q

What is denaturation?

A

Denaturation occurs when the bonds in the protein are broken and the functionality is lost.

20
Q

Why are the bonds in the primary structure usually not broken in denaturation?

A

Strong peptide bonds.

21
Q

What is protein conjugation?

A

Reversible combination of proteins and factors.

22
Q

What are glycoproteins?

A

Proteins that are covalently attached to a carbohydrate factor.

23
Q

How are glycoproteins formed?

A

The carbohydrate attaches through a post-translational modification called glycosylation whereby a sugar molecule binds via an amino acid to the protein.

24
Q

What are lipoproteins?

A

Proteins that are covalently or non-covalently attached to fats.

25
Q

What are metalloproteins?

A

Proteins that are ionically attached to metals. One third of body proteins require a metal cofactor for function.

26
Q

What is co-operativity?

A

Co-operativity occurs when the shape of one protein sub-unit is altered by the substrate or some other molecule so as to alter the affinity of a neighbouring subunit and change its shape. (Eg. haemoglobin).

27
Q

What are globular proteins?

A

Storage / enzymes / hormones / transporters / structural

28
Q

What is the pathology of globular proteins?

A

Myeloma

29
Q

What are fibrous proteins?

A

Muscle fibres / connective tissue

30
Q

What is the pathology of fibrous proteins?

A

Scurvy.

31
Q

What are membranous proteins?

A

Membrane transporters / membrane enzymes / cell adhesion molecules

32
Q

What is the pathology of membranous proteins?

A

Familial hypercholesterolaemia