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1. Alpha Helix
  • rod like
  • CO & NH of the mainchain are hydrogen bonded together, allowing the mainchain to be buried
  • n+4 H bonding scheme
  • all alpha carbons are H bonded and in line with each other
  • R groups are on the outside & backbone on the inside
  • always right handed (clockwise)
  • can be a single chain (usually less than 45 Angstroms)
  • Residues that are 1 & 2 residues apart are on opposite sides, while residues that are 3 & 4 residues apart are on the same side; this allows small steric hindrance
  • 1.5 Angstroms rise (from one alpha carbon to the second)
  • 100 degree rotation
  • 3.6 residues per turn
  • Ramachandran diagrams (1) Right handed: can only occur between -60, -60; little hindrance (2) Left handed: +60, +60; large hindrance
2. Beta Sheet
  • sheet like
  • Beta sheets are formed by linking 2 or more Beta strands by H bonds
  • side chain of adjacent residues point in opposite directions
  • only trans peptide bonds give R groups on opposite sides
  • cannot exist as a single Beta strand; must be 2 or more
  • in proteins, 4-5 strands make up a beta sheet; it is possible to be made of more than 10
  • 3.5 Angstroms rise between residues
  • 7 Angstroms between R groups
  • Arrow in pictures always points to the CO group
  • can be antiparallel, parallel, or mixed
  • anti: 1:1; alpha carbons are completely lined up across from each other; CO & NH of adjacent strands are H bonded together; chains are in opposite directions
  • parallel: strands are in the same direction; NH group of the first chain is bonded to the CO of the 2nd chain through H bond, then move two residues to the right and the CO of the first chain is H bonded to the NH of the 2nd chain.
  • Ramachandran diagrams: exists between -60 to -120, 100-190
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12y ago
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9y ago

Alpha helix and beta pleated sheets both are held together with H bonds between carbonyl O and amino N. Alpha helix specifies with residues bind. Beta pleated sheets can happen between any 2 residues.

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13y ago

Stabilized by hydrogen bonds, hydrogen bonding between amides groups

Polypeptide secondary structures.

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11y ago

Beta sheets consist of beta strandsconnected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet.

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12y ago

Secondary structure

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Q: What is the difference between beta strand and beta sheet?
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