2.3 Protein Structure, Ligand Binding and Conformational Change ii Ligand Binding Changes the Conformation of a Protein Flashcards

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1
Q

What is a ligand?

A

A substance that can bind to a protein

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2
Q

Which molecule allows binding to ligands?

A

R groups that are not involved in protein folding

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3
Q

What about a ligand’s binding site is described as complimentary?

A

Shape and chemistry

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4
Q

What changes about a protein once a ligand binds to a ligand- binding site?

A

Conformation

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5
Q

What does a change in the shape of a protein result in?

A

This change in conformation causes a functional change in the protein

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6
Q

Where do allosteric interactions occur?

A

Between spatially distinct sites

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7
Q

The binding of a substrate molecule to one active site of an allosteric enzyme does what to the affinity of the other active sites

A

Increases the affinity of the other active sites for binding of subsequent substrate molecules.

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8
Q

How can the activity of allosteric enzymes vary?

A

Small changes in substrate concentration causes a great variation in activity.

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9
Q

What kind of structure do most allosteric proteins have?

A

Quaternary structure (consist of multiple subunits)

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10
Q

What do allosteric proteins show when binding?

A

co-operativity, in which changes in binding at one subunit alter the affinity of the remaining subunits

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11
Q

What is the second type of site found on an allosteric enzyme called

A

Allosteric site

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12
Q

What is the purpose of a modulator?

A

Modulators regulate the activity of the enzyme

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13
Q

Where do modulators bind to?

A

The allosteric site

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14
Q

What happens once a modulator has bound to the enzyme?

A

Following binding of a modulator, the conformation of the enzyme changes and this alters the affinity of the active site for the substrate

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15
Q

Effect of a positive modulator

A

Positive modulators increase the enzyme’s affinity for the substrate

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16
Q

Effect of a negative modulator

A

Negative modulators reduce the enzyme’s affinity.

17
Q

What does the binding and release of oxygen in haemoglobin show?

A

Co-operativity

18
Q

How does a change in the binding of oxygen at one subunit affect the remaining subunits?

A

Alters the affinity of the remaining subunits for oxygen.

19
Q

A decrease in pH or an increase in temperature does what to the affinity of haemoglobin for oxygen?

A

Lowers the affinity of haemoglobin for oxygen, so the binding of oxygen is reduced.

20
Q

Reduced pH and increased temperature in actively respiring tissue causes what?

A

Reduction in the binding of oxygen to haemoglobin promoting increased oxygen delivery to tissue.