Modular structure of proteins Flashcards

1
Q

What is a motif in a protein? [2 marks]

A

The minimum arrangement of independently forming secondary structures combining recognisable folds across many proteins
OR
A combination of two or more secondary structures to form a recognisable folded arrangements.

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2
Q

What do motifs usually associate with? [1 mark]

A

Domains with functional properties.

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3
Q

What are examples of well known domains? [3 marks]

A
  • Immunoglobin: two anti-parallel beta sheets.
  • ATPase: found in many different enzymes.
  • Transmembrane: formed form multiple hydrophobic alpha helices connected by intervening hydrophilic loops.
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4
Q

What is the function and structure of the EF hand and where is it found? [3 marks]

A
  • Binds to Ca2+.
  • Resembles a helix turn helix but combines with a metal ion like calcium.
  • Found in calmodulin & troponin-C.
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5
Q

What is the function and structure of the Greek key? [2 marks]

A
  • It isn’t associated with a specific function.

- Consists of antiparallel beta strands.

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6
Q

What is the structure of a beta barrel? [2 mark]

A
  • Bea strands wrapped around.

- Forms a circular tunnel.

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7
Q

What is the structure of a beta-alpha-beta? [1 mark]

A

Parallel strand of a beta sheet interlinked with alpha helix.

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8
Q

Where do helices on DNA binding motifs go? [1 mark]

A

Into the major groove of DNA.

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9
Q

Where is the helix loop helix found? [2 marks]

A
  • Max & Mad

- Ca2+ binding

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10
Q

Where is the helix turn helix found? [3 marks]

A
  • Cro
  • Tryptophan
  • Ca2+ binding
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11
Q

Where is the leucine zipper found? [1 mark]

A

GCN4 (involved in translation in yeast)

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12
Q

Where is the zinc finger found? [1 mark]

A

Hormone receptors.

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13
Q

Structure of membrane bound receptors [3 marks]

A
  • Intracellular region: responsible for downstream signalling and functionality of the protein.
  • Transmembrane region: embedded in lipid bilayer, formed from bundles of helices (alpha helices are around 20 a.a. long)
  • Extracellular region: main structure of protein.
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14
Q

What is domain shuffling? [1 mark]

A

When modular units of structure are conserved but shuffled between genes.

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15
Q

Structure of helix loop helix [4 marks]

A
  • Binds only in dimeric form.
  • Exist as hetero and homodimers.
  • Central part is from overlapping helices to allow dimerisation.
  • Terminal part of lower opposing helices contains basic amino acids that interact with major grooves of DNA.
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16
Q

Structure of helix turn helix [2 marks]

A
  • Two short helices oriented at right angles to each other, connected by a turn.
  • CRO is a homodimer.
17
Q

Structure of the leucine zipper [3 marks]

A
  • Formed from 2 contiguous alpha helices.
  • Dimeric protein.
  • Dimers zip together to form a coiled coil (held by hydrophobic interactions).
18
Q

Structure of the zinc finger [3 marks]

A
  • Alpha helix and beta sheet
  • Held together by non-covalent interactions with zinc.
    Alpha helix interacts with major groove of DNA.