Lecture 8: Protein Structure Flashcards

1
Q

what do non-polar proteins bind to

A

lipids, eg in the membrane

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2
Q

what forms the shape of an alpha helix

A

hydrogen bonds forming between carbonyl groups and amine group 4 amino acids down the chain

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3
Q

how many amino acids are there per turn of an alpha helix

A

3.6

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4
Q

what is a beta pleated sheet made up of

A

laterally packed beta strands

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5
Q

what forms the shape of a beta pleated sheet

A
  • hydrogen bonds between carbonyl groups and amine group of a neighbouring chain
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6
Q

what helps hold alpha chains and beta pleated sheets together

A
  • turns, 3-5 amino acids long which form a sharp bend redirecting the polypeptide backbone
  • loops, longer than a turn, tend to be hydrophobic and found on surface of protein
  • random coils
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7
Q

what is the barrel configuration

A
  • tertiary structure

- first and last strand form Hydrogen bonds, forming a barrel shape

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8
Q

what is the coiled coil configuration

A
  • tertiary structure
  • 2 or 3 alpha helices coil round each other
  • hydrophobic amino acids line up together where the helices meet
  • eg. keratin and collagen
  • gives great structural strength
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9
Q

what is post translational modification

A
  • covalent processing events

- addition of a modifying group

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10
Q

what can post translational modification change

A
  • activity state
  • localisation
  • turnover
  • interactions with other proteins
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11
Q

where are disulfide bridges found

A
  • between SH and CH bonds, between two cysteines

- typically present in excreted proteins, as in the cytoplasm it’s a reducing environment which would reduce this bond

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12
Q

what can we use to predict the shape of a protein from its amino acid sequence

A

X-ray crystallography

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13
Q

what permanently dentaures proteins and what reversibly denatures them

A
  • acid/base is reversible

- temperature is irreversible

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14
Q

what do molecular chaperones do

A

bind to a partially folded polypeptide and assist them in folding

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15
Q

what are the classes of chaperones

A
  • heat shock proteins: more expressed at higher temperatures
  • chaperonins: prevent protein aggregation, prevent non-productive intermediates and can shield proteins from its aqueous environment
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16
Q

what are protein domains

A
  • discrete 3D structures linked by a short link chain
  • part of the protein
  • function independently to one another
17
Q

what can a domain’s function be predicted by

A

its sequence motif

18
Q

what causes Alzheimer’s disease

A

amyloid beta misfolding

19
Q

what causes cystic fibrosis

A
  • deletion of phenylamine at position 508

- the protein gets stuck in the ER and can’t make it up to the cell surface

20
Q

what is Creutzpelat-Jakob disease caused by

A
  • prion protein misfolds, gets sticky and aggregates

- forms very stable beta pleated sheets and amyloid fibrils, causing slow progressive neuronal cell death