proteins 1 Flashcards

1
Q

What do proteins do?

A

provide structure (bone, skin, tendon)
Transport molecules (LDL-cholesterol, haemoglobin-oxygen)
Defence (antibodies)
Biological catalysts (enzymes, eg lysosomes)
Regulation of genes (lac repressor)

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2
Q

Hypercholesterolemia

A

mutation histadine residue in LDL receptor

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3
Q

What do the functions of protein really come down to?

A

Specific binding which depends on conformation

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4
Q

What changes the activity of a protein?

A

A change in conformation

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5
Q

What are proteins?

A

Linear polymers: amino acids joined by peptide bonds

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6
Q

What defines the structure and function of a protein?

A

The R group of it’s amino acids

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7
Q

Classification of hydrophilic amino acids

A

Basic
Acidic
Polar with uncharged R groups

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8
Q

Basic amino acids (hydrophillic)

A

Lysine
Arginine
Histidine

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9
Q

Acidic amino acids (hydrophillic)

A

Aspartate and Glutamate

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10
Q

Polar amino acids with uncharged R groups (hydrophillic)

A

Serine, Threonine, Asparagine, Glutamine

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11
Q

Hydrophobic amino acids

A

Alanine, Valine, Isoleucine, Leucine, Methionine, phenylalaline, Tyrosine, Tryptophan

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12
Q

Special amino acids

A

Cysteine (covanent S-S)
Glycine (smallest)
Proline (ring R, kink)

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13
Q

what do we mean by acid

A

a molecule that tends to release a hydrogen ion

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14
Q

what do we mean by base

A

ion that readily binds to H

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15
Q

How is the pH of a reaction calculated?

A

Henderson hasselbach equation

pH=pKa + log [A-]/[HA]

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16
Q

What is the pKa of an acid?

A

The pH at which half the molecules are disassociated.

17
Q

Why is pH relevant?

A
Affect disassociation(mainly over 2 units of pH centred on pKa) 
Changes charge of overall aminoacid.
Means local environment affect pKa.
18
Q

Give an example where a reduction in pH affects proteins

A

histadine residues -on LDL acting as carriers (cholesterol)- change conformation with change in pH, release cholesterol in endosomes

19
Q

Peptide bond

A

condensation reaction, carbon from carboxylate shares electron with N from amino

20
Q

Why is there a limit to the number of 3D conformations possible for a peptide?

A

peptide bond does not permit rotation, bulky R groups positioned on either side of backbone

21
Q

What is secondary structure of a protein? (Stabilised by H bonds)

A

periodic repeats, initial folding patter.

a helix, b sheet, bend/loop

22
Q

What groups are capable of hydrogen bonding?

A

H and oxygen, nitrogen or fluorine