Lecture 1 Flashcards

(26 cards)

1
Q

Define 3 major classes of globular protein.

A

α-domain structures made up entirely of α-helices.
β-domain helices made up entirely of β-strands.
αβ-domain structures made up pf mixed α-helices and β-strands. Generally more complex in structure.

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2
Q

As an isolated α-helix is barely stable in solution, how are they typically arranged?

A

Pairwise in proteins, with hydrophobic residues pointing towards the core.

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3
Q

What is the major protein present in blood plasma, and in what concentration?

A

Serum albumin (40g/L).

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4
Q

What is the total concentration of protein in blood?

A

70g/L.

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5
Q

2 functions of serum albumin?

A
Transporter of smaller (typically hydrophobic) molecules.
Major contributor (80%) of osmotic swelling pressure of blood plasma.
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6
Q

To which electrode does albumin migrate to?

A

Positive electrode.

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7
Q

To which electrode does albumin migrate to?

A

Positive electrode.

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8
Q

What is the pI (Isoelectric point)?

A

The pH at which a particular molecule carries no net overall charge.

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9
Q

What is the Mr and pI of HSA (Human Serum Albumin)?

A

66,500 Da, 5.67.

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10
Q

How would you define HSA’s structure?

A

Almost entirely α-helical.

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11
Q

How many polypeptide chains,
amino acids,
and intra-chain disulphide bonds are there in HSA?

A

1,
585,
17.

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12
Q

What is the purpose of disulphide bonds in HSA?

A

To form large (L) and small (S) double loops.

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13
Q

How may HSA have evolved?

A

L (large loop) gene duplicated twice, forming LLL. The middle gene mutates, creating LSL. The sequence then duplicates twice, forming LSL LSL LSL.

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14
Q

What amino acid does the amino acid sequence of albumin contain a very high percentage of (and how many)?

A

Cysteine. (35/585).

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15
Q

Of note, what does the primary structure of cysteine contain?

A

One free sulphydryl.

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16
Q

Of note, what does the primary structure of Cys-34 contain?

A

One free sulphydryl.

17
Q

What percentage of free sulphydryl Cys-34 is oxidised?

18
Q

Some preparations of serum albumin can contain up to ??% albumin dimers.
Also, what must happen to form an albumin dimer?

A

20%.

Cys-34s must disulphide bond to each other.

19
Q

Albumin’s many binding sites can carry which 3 types of molecule?

A

Long-chain fatty acids,
Small heterocyclic/aromatic carboxylic acids,
Metals.

20
Q

What 4 ions can Cys-34 bind to?

A

Cd, Au, Hg, Ag.

21
Q

His-3 on the N terminal of HSa can bind which ions?

A

Cu(II), Ni(II).

22
Q

How is Cu(II) typically transported in the blood?

A

Complex with Albumin and free His.

23
Q

What 4 drugs can be transported via Albumin?

A

Aspirin, AZT, Penicillin, Warfarin.

24
Q

What may happen to small molecules not transported in the blood via protein?

A

Excretion via the kidney into the urine.

25
Thanks to it's ready availability, what is albumin used for in biochemistry?
Mr marker, and as a blocking reagent in immuno-biochemistry.
26
Thanks to it's ready availability, what is albumin used for in biochemical fields?
Mr marker, and as a blocking reagent in immuno-biochemistry.