lecture 4 - proteins Flashcards

1
Q

Which polypeptide helix is more common? right-handed or left handed?

A

Right - handed

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2
Q

Why do polypeptide helices have a dipole moment?

A

C terminus = negative

N terminus = positive

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3
Q

Why don’t peptide bonds liked to be lined up with a 0 degree angle?

A

Don’t want a steric clash

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4
Q

What is the minimum number of polypeptide chains needed for a Beta pleated sheet?

A

2

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5
Q

Which Beta sheet is stronger? Anti - parallel or parallel?

A

Anti- Parallel

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6
Q

Do Beta sheets have a dipole moment ?

A

NO - due to the alternating planes which cancel each other out.

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7
Q

What are two very rare polypeptide chains?

A

Beta helices and Allpha - pleated sheets

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8
Q

What is a Beta turn?

A

Antiparallel sheets connected via a Beta turn

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9
Q

Primary structure

A

Amino acid sequence

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10
Q

Secondary structure

A

Regular, arrangement of the polypeptide chain

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11
Q

Tertiary structure

A

Complete fading of a single chain

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12
Q

Quaternary structure

A

association of multiple chains

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13
Q

How is the conformation stabilised?

A

Non - covalent interactions;

  • Hydrogen bond
  • Ionic interactions
  • Hydrophobic interaction
  • Van der Waals interaction
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14
Q

What are the roles of disulphide bonds (form of covalent bonds)

A
  • covalent bonds between cysteine side chains
  • ## no all proteins have cys residues
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15
Q

What environment can disulphide bonds form in?

A

Can only happen In an oxidising environment

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16
Q

What do disulphide bridges do in hair?

A

Cause a curl

17
Q

What reducing agent is used to straighten hair/

A

ammonium thioglycolate

18
Q

What oxidising agent is used to permanently curly hair?

A

Hydrogen peroxide

19
Q

Do covalent bonds break under heat?

A

NO

20
Q

The synthesis of insulin

A
  • Synthesised as inactive precursor prepreinsulin
  • pre - sequence removed
  • proinsulin folds and and disulphides form - forms inactive precursor
  • Activation involves removal of pro sequence
21
Q

What are the experimental methods for study of proteins?

A
  • purification
  • determine amino acid sequence
  • determine conformation
22
Q

how to determine conformation

A
  • X-ray crystallography / NMR

- Homology model if there is a closely related protein of a known structure

23
Q

Column chromatography

A
  • separations of soluble proteins based on differences in molecular characteristics
24
Q

Gel filtration

A

separation depends on molecular charge

25
Q

ion exchange

A

separation depends on molecular charge

26
Q

Affinity chromatography

A

separation depends on specific binding interaction