1.2b protein structure Flashcards

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1
Q

What determines protein structure?

A

amino acid sequence

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2
Q

What are proteins polymers of?

A

amino acid monomers

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3
Q

What are amino acids monomers of?

A

protein polymers

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4
Q

What are amino acids linked by and what do they form?

A
  • linked by peptide bonds

- to form polypeptides

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5
Q

What are the 4 groups that amino acids are classified in according to their R groups?

A
  • basic
  • acidic
  • polar
  • hydrophobic
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6
Q

What classifies and amino acid as basic?

A

R group results in:

  • positively charged
  • hydrophilic
  • key component of R group is an amine group(NH)
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7
Q

What classifies and amino acid as acidic?

A

R group results in:

  • negatively charged
  • hydrophilic
  • key component of R group is a carboxylic acid group (COOH)
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8
Q

What classifies an amino acid as Polar?

A

R group results in:

  • slightly charged
  • forms hydrogen bonds
  • hydrophilic
  • key component of R group is hydrophilic group (carbonyl C=O, hydroxyl OH, amine NH)
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9
Q

what classifies an amino acid as hydrophobic?

A

R group results in:

  • no charge, non-polar
  • don’t form hydrogen bonds
  • so don’t mix readily with water
  • Key component of R group is hydrocarbon group CH
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10
Q

How does the structure of different amino acids vary?

A

they have the same basic structure differing only in R group

  • R groups vary in:
    • size
    • shape
    • charge
    • hydrogen bonding capacity
    • chemical reactivity
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11
Q

What is responsible for the wide range of functions carried out by proteins?

A

the diversity of the R groups

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12
Q

What is primary structure?

A

the sequence in which the amino acids are synthesised into the polypeptide

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13
Q

What causes secondary structure?

A

hydrogen bonding along the backbone of the protein strand results in regions of secondary structure

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14
Q

Give examples of secondary structure

A
  • alpha helices
  • parallel or anti-parallel beta-pleated sheets
  • turns
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15
Q

Describe tertiary structure

A

the polypeptide folds into a tertiary structure

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16
Q

What stabilises tertiary structure?

A

interactions between R groups:

  • hydrophobic interactions
  • ionic bonds
  • London dispersion forces
  • hydrogen bonds
  • disulfide bridges
17
Q

What are disulfide bridges?

A

covalent bonds between R groups containing sulfur

18
Q

What is quaternary structure?

A

Quaternary structure describes the spatial arrangement of subunits

19
Q

When does quaternary structure happen?

A

Quaternary structure exists in proteins with two or more connected polypeptide subunits

20
Q

What is a prosthetic group?

A

a non-protein unit tightly bound to a protein and necessary for its function

21
Q

What is the ability of hemoglobin to bind oxygen dependent on?

A

the non-protein haem group

22
Q

What is the effect of increasing temperature on interactions of the R groups?

A
  • disrupts the interactions that hold the protein in shape
  • the protein begins to unfold
  • and eventually becomes denatured
23
Q

What is the effect of pH on interactions between R groups?

A
  • the charges on acidic and basic R groups are affected by pH.
  • as pH increases or decreases from the optimum
  • the normal ionic interactions between charged groups are lost
  • which gradually changes the conformation of the protein until it becomes denatured