Lecture 6 - protein structure and folding Flashcards

1
Q

what is the building of a tertiary protein structure

A

secondary structure, supersecondary structure and protein domains

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2
Q

what is a supersecondary structure

A

several adjacent elements of a secondary structure that is smaller than a protein domain

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3
Q

examples of supersecondary structures

A

helix - turn - helix , beta hairpin, greek key, strand - helix - strand

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4
Q

what do supersecondary structures combine to form

A

domains

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5
Q

what are domains

A

independentley folded regions that often possess a specific function

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6
Q

what is a hydrophobic core of a protein domain important for

A

very important for protein stability

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7
Q

where are the hydrophilic parts arranged in protein domains

A

on the surface in contact or near the solvent

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8
Q

how many domains do small proteins usually have

A

usually one

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9
Q

how many domains do larger proteins have

A

may have multiple domains

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10
Q

what are three examples of how proteins can be grouped into families based on tertiary structure

A
  • a domain family
  • a/B family
  • anitparallel B family
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11
Q

properties of an a domain family

A

mostly helical with a hydrophobic core

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12
Q

properties of an a/B domain family

A

mix of a and b structure
- a/b barrel
- a/b horseshoe fold

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13
Q

properties of an antiparallel B family

A

mostly antiparallel b structure
- often for transporting things like vitamin A

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14
Q

what did Anfinsen’s experiment show

A

all the information needed for a protein to fold for its function is in the linear amino acid sequence

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15
Q

what is the likely sequence of events in folding a newly synthesised protein

A
  • formation of short secondary segments (alpha helices and beta strands)
  • subdomains form (supersecondary structure)
  • subdomains come together to form loose domains
  • final domain structure emerges, small conformational adjustments to give overall tertiary structure
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16
Q

what helps with stabilisation of a protein

A
  • non covalent interactions = individually weak in proteins but collectively make significant contribution
  • some proteins have additional covalent bonds (e.g disulfide bonds)
  • hydrophobic core
17
Q

what are chaperones

A

they can bind to hydrophobic regions to make sure they fold properly

18
Q

what is an example of a disease due to a misfolded protein

A

prions disease