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AH Biology > Unit 1.2c(ii) > Flashcards

Unit 1.2c(ii) Flashcards

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1
Q

What is a ligand?

A

A substance that binds to a protein

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2
Q

What do R groups stabilise?

A

Folding of tertiary structures in proteins

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3
Q

What facilitates molecule binding?

A

R-groups on the proteins outer surface

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4
Q

What causes ligand binding sites on the protein surface?

A

Proteins folding

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5
Q

What on binding sites is complementary to ligands?

A

Their shape and chemistry

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6
Q

What matching elements bind the protein and ligand together?

A

Charged, polar and non-polar R-groups

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7
Q

What is the enzyme specific shape called?

A

The active site

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8
Q

What is ligand binding essential for?

A

Cell signalling that activates receptors or channels

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9
Q

Why is DNA considered a ligand?

A

Because it binds to proteins involved in replication, transcription and translation regulation in operons

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10
Q

How do DNA-protein interactions help fit DNA into the nucleus?

A

They help package long DNA into chromosomes

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11
Q

In eukaryotes how does DNA Lind to histone protein?

A

DNAs negatively charged backbone binds to the positively charged histone

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12
Q

What is formed when DNA wraps around a histone?

A

It forms a nucleosome

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13
Q

What happens when double stranded DNA binds to transcription factors?

A

Transcription is inhibited or initiated

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14
Q

What do transcription factors do?

A

Control gene expression

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15
Q

What happens if an activator protein binds to a specific DNA sequence?

A

Transcription of downstream genes is stimulated

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16
Q

What is the enhancer?

A

The part of DNA that that recruits transcription factors and RNA polymerase to the promoter region of the transcribed gene

17
Q

Why do conformational changes occur?

A

The interaction between the ligand and protein binding site pull the polypeptide towards the ligand

18
Q

What is a proteins change in shape called?

A

Conformational change

19
Q

What does a change in protein shape cause?

A

A change in the proteins function

20
Q

What regulates the proteins activity?

A

Conformational change

21
Q

What is an allosteric enzyme/protein?

A

An enzyme/protein that has multiple sub-units (quaternary structure) with multiple binding sites

22
Q

What happens when a ligand binds to an allosteric subunit?

A

The affinity of the rest increases

23
Q

What causes allosteric enzymes activity to vary?

A

Small changes in substrate concentration

24
Q

What are ligands that bind to allosteric enzymes called?

A

Modulators

25
Q

When the subunits affinity increases how would they be described?

A

As showing cooperativity

26
Q

Do conformational changes affect enzymes activity?

A

Yes as the active sites affinity changes

27
Q

What is affinity?

A

The attractive force that binds atoms in molecules

28
Q

What is cooperativity?

A

When the binding of 1 sub-unit increases the affinity for the remaining sub-units

29
Q

What is the Haemoglobin subunit called?

A

Haem

30
Q

What does Haem bind to?

A

Oxygen

31
Q

What happens to the other 3 harms once one oxygen binds?

A

The next one will be easier and so on (affinity increases)

32
Q

What the name given to the oxygen-Haem compound?

A

Oxy-Haemoglobin

33
Q

What happens to the other subunits if oxy-Haemoglobin releases one of the oxygens?

A

The next will find it easier to release its oxygen and so on

34
Q

How does low pH affect Haemoglobins affinity for oxygen?

A

It decreases the affinity

35
Q

How does high temp affect Haemoglobins affinity for oxygen?

A

It decreases the affinity

36
Q

Why does exercise cause more oxygen to be delivered to the tissue?

A

Exercise increases body temp, CO2 is produced and blood becomes acidified. This means less oxygen binds to the Haemoglobin so more goes to the tissue.

37
Q

When would Haemoglobin hold lots of oxygen?

A

When it’s in a rich oxygen environment

38
Q

When would Haemoglobin hold little oxygen?

A

In low oxygen environments

AH Biology (51 decks)

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