lecture 18 - protein structure: beta sheets Flashcards

1
Q

explain beta-sheet structure

A
  • repetitive phi/psi angles
  • zig-zag comfirmations of backbone
  • not formed by a contiguous region of amino acid sequence
  • minimum of 2 beta strands come together to form a beta sheet
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2
Q

what is a beta sheet stabilized by?

A

H-bonds between strands (can be parallel or anti-parallel)

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3
Q

explain anti-parallel H-bonds between beta sheets

A
  • R groups on adjacent strands are oriented in the same direction (e.g. all R groups are above the plane)
  • H-bonds are perpendicular to strands and in the plane of the sheet
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4
Q

explain parallel H-bonds between beta sheets

A

-some R groups are above the plane, some R groups are below the plane

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5
Q

explain the relationship between parallel H bonds and an amphipathic B-sheet

A
  • can create an amphipathic B-sheet by having hydrophobic R groups on face and hydrophilic groups on another face
  • implies mechanism for folding B-sheets to bury hydrophobic face
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6
Q

beta sheets often have a twist (not strictly planar), what does this mean? what does this require?

A
  • have a mix of anti-parallel and parallel H-bonds

- need more than 2 strands

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7
Q

explain how secondary structures link together

A
  • flexible regions (have primary structure) allow the secondary structure to fold into 3D fold
  • have alternate folding pattern: parallel beta sheet with alpha helix on top, etc.
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8
Q

define motif

A

collection of secondary structural elements

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