1.23 b) Ligand Binding Changes the Conformation of a Protein Flashcards

1
Q

What is a ligand?

A

A substance which can bind to a protein

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2
Q

Under what circumstances does the conformation of a protein change?

A

if a ligand binds to a protein’s binding site (eg a substrate binds to an enzyme’s active site)

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3
Q

Conformational changes in proteins causes ___ changes.

A

functional

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4
Q

R groups not involved in protein folding can allow ___ to ligands.

A

binding

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5
Q

Binding sites have a complementary ___ and ___ to the ligand.

A

shape, chemistry

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6
Q

Induced fit is a ___ change in the shape of the ___ site, which increases the ___ interacting with the substrate.

A

temporary, active, area

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7
Q

This chemical environment lowers the ___ ___ for the reaction.

A

activation energy

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8
Q

Name the two sites that allosteric enzymes have.

A

active site and allosteric site

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9
Q

Allosteric enzymes can change ___ upon binding a ___.

A

conformation, modulator

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10
Q

In allosteric enzymes, modulators bind at secondary locations known as ___ ___.

A

allosteric sites

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11
Q

Once the modulator has bound, the conformation of the enzyme changes which alters the ___ of the ___ ___.

A

shape, active site

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12
Q

Modulators that increase the enzyme’s affinity for the substrate are called…

A

positive modulators

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13
Q

Modulators that decrease the enzyme’s affinity for the substrate are called…

A

negative modulators

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14
Q

Modulators bind to the ___ ___ and change the shape of the ___ ___.

A

allosteric site, active site

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15
Q

What is cooperativity?

A

when a ligand binding to one subunit of a multi-subunit protein changes the affinity of the other subunits for that ligand

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16
Q

In what type of proteins does cooperativity occur?

A

ones with quarternary structure

17
Q

What is an example of a molecule that exhibits cooperativity?

A

haemoglobin

18
Q

Haemoglobin has quarternary structure and so is made of 4 ___ ___.
Each one has a ___ group, capable of binding to a molecule of ___.

A

polypeptide chains.
haem, oxygen

19
Q

When one of haemoglobin’s subunits binds an oxygen molecule the remaining subunits bind with ___ ___.

A

increasing ease

20
Q

The reverse is also true, when the first of oxy-haemoglobin’s subunits releases its oxygen molecule, the remaining subunits release theirs with ___ ___.

A

increasing ease

21
Q

What are the two main factors that affect haemoglobin’s affinity to oxygen?

A

pH and temperature

22
Q

Describe how haemoglobin’s affinity to oxygen changes under the following conditions:
1. As temperature increases
2. As pH increases

A
  1. affinity decreases.
  2. affinity increases
23
Q

Describe the conditions in actively respiring tissue with respect to temperature and pH and; suggest a benefit to these conditions.

A

Actively respiring tissue has a high temperature and low pH;
this lowers haemoglobin’s affinity to oxygen, which promotes oxygen delivery to respiring cells (which require oxygen)

24
Q

Phosphates can cause ___ conformational changes in proteins.

A

reversible

25
Q

The addition of phosphate groups is a common form of __-__ ___.

A

post-translational modification

26
Q

What is the name of the enzyme that catalyses the addition of phosphate groups to other proteins?

A

protein kinase

27
Q

The phosphate group that is transferred by the enzyme ___ ___, comes from ___ (it is the ___ phosphate).

A

protein kinase, ATP, terminal/third

28
Q

What is the name of the enzyme that catalyses the reverse reaction (dephosphorylation)?

A

protein phosphatase

29
Q

Phosphorylation affects a proteins activity by causing ___ ___.

A

conformational changes

30
Q

Proteins can be ___ or ___ by phosphorylation. This is how many cellular proteins are ___.

A

activated, inhibited.
regulated

31
Q

Phosphate groups have a ___ charge (just like phosphorus ions haha cute)

A

negative

32
Q

Since phosphate groups have a negative charge, phosphorylation can disrupt the ___ interactions in the un____ protein, or create new ones.

A

ionic, unphosphorylated

33
Q

Name a protein who’s function is dependent on phosphorylation.

A

The sodium potassium pump (its phosphorylated by ATP to transport 3 sodiums out and dephosphorylated by ADP to transport 2 potassiums in)

There are other proteins as well probably