Protein Biochemistry And Enzymology Flashcards

(36 cards)

1
Q

What is the natural function of B-galactosidase?

A

To hydrolyse lactose

It also hydrolyses other galactosidases such as nitrophenylgalactose.

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2
Q

What is the enzyme-substrate complex equation?

A

Enzyme + substrate = Enzyme-substrate complex = Enzyme + product

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3
Q

What happens to the fraction of enzyme molecules bound to substrate as substrate concentration increases?

A

It increases

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4
Q

What does saturation of an enzyme indicate?

A

Most enzyme molecules have substrate bound

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5
Q

What does the Michaelis-Menten equation describe?

A

V = (Vmax)(substrate concentration / (Km + substrate concentration))

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6
Q

What does Km represent in enzyme kinetics?

A

Michaelis constant (units of concentration)

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7
Q

What does Kcat describe?

A

How fast the enzyme works (turnover rate)

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8
Q

What is the specificity constant formula?

A

Kcat / Km

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9
Q

What does a high specificity constant indicate about an enzyme?

A

High catalytic efficiency

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10
Q

What does a Lineweaver-Burk plot represent?

A

A double reciprocal plot used to determine enzyme kinetics

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11
Q

What is the effect of competitive inhibition on Vmax?

A

Vmax stays the same

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12
Q

What is the main characteristic of irreversible inhibition?

A

Inhibitors react covalently with essential groups in the enzyme

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13
Q

What condition is associated with the blockage of acetylcholine receptors?

A

Myasthenia gravis

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14
Q

What is the role of Edrophonium?

A

Competitive inhibitor of acetylcholinesterase used for diagnosis of Myasthenia gravis

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15
Q

What are the components of proteins?

A

Amino acids

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16
Q

What bonds join amino acids in proteins?

A

Peptide bonds

17
Q

What is the secondary structure of proteins characterized by?

A

Alpha helix and beta sheets

18
Q

Which amino acid is a helix breaker?

19
Q

What is the hydrophobic effect?

A

Most important determinant of tertiary structure

20
Q

What is the significance of disulfide bonds in proteins?

A

Covalent bonds between two cysteine side-chains

21
Q

What does the Henderson-Hasselbalch equation relate to?

A

pH, pKa, and the ratio of base to acid

22
Q

What does isoelectric focusing rely on?

A

The isoelectric point (pI) where a molecule has no net charge

23
Q

What is the purpose of SDS-PAGE?

A

To separate proteins based on their size

24
Q

What type of chromatography uses a charged matrix?

A

Ion exchange chromatography

25
What is affinity chromatography based on?
Selective affinity of proteins for specific structures
26
What is the quaternary structure of a protein?
Assembly of more than one polypeptide chain
27
What is the role of collagen in the human body?
It comprises ¼ of protein in the human body
28
What is the primary structure of proteins?
Sequence of amino acids
29
What does a protein's tertiary structure involve?
Packing of secondary structures and side chain interactions
30
What is the main factor that affects protein folding?
Hydrophobic effect
31
What is the molecular architecture of the beads used in size exclusion chromatography?
Cross-linked polydextran
32
What does the term 'domain' refer to in protein structure?
Globular unit formed from part of a polypeptide
33
What is a dipetide?
2 amino acids
34
Fill in the blank: The formula for the rate of formation of P in an enzyme catalysed reaction is V = Kcat (______).
ES
35
True or False: The apparent value of Km decreases in competitive inhibition.
False
36
What is the role of the side chain in amino acids?
Determines the properties of the amino acid