Examples of β-pleated sheet in the following topics:
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- In β-pleated sheets, stretches of amino acids are held in an almost fully-extended conformation that "pleats" or zig-zags due to the non-linear nature of single C-C and C-N covalent bonds. β-pleated sheets never occur alone.
- They have to held in place by other β-pleated sheets.
- The stretches of amino acids in β-pleated sheets are held in their pleated sheet structure because hydrogen bonds form between the oxygen atom in a polypeptide backbone carbonyl group of one β-pleated sheet and the hydrogen atom in a polypeptide backbone amino group of another β-pleated sheet.
- The β-pleated sheets which hold each other together align parallel or antiparallel to each other.
- The R groups of the amino acids in a β-pleated sheet point out perpendicular to the hydrogen bonds holding the β-pleated sheets together, and are not involved in maintaining the β-pleated sheet structure.
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- Steric interactions also cause a slight bending or contraction of the peptide chains, and this results in a puckered distortion (the pleated sheet).
- Using the dihedral angle terminology, an antiparallel β-sheet has Φ = -139º and a Ψ = 135º.
- Some proteins have layered stacks of β-sheets, which impart structural integrity and may open to form a cavity (a beta barrel).
- An example is human retinol binding protein, which has a cavity formed by eight β-sheet strands.
- When beta-sheets are observed as secondary structural components of globular proteins, they are twisted by about 5 to 25º per residue; consequently, the planes of the sheets are not parallel.
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- Secondary structures such as the α-helix and β-sheet take on a dominant role in the architecture and aggregation of keratins.
- In the case of β-sheets, Gly allows sterically-unhindered hydrogen bonding between the amino and carboxyl groups of peptide bonds on adjacent protein chains, facilitating their close alignment and strong binding.
- The secondary structure is roughly 30% β-sheets, 20% α-helices and 50% unordered.
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- Mutations in the gene for the prion protein can cause a misfolding of the dominantly alpha helical regions into beta pleated sheets.
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- All chains have a characteristic immunoglobulin fold in which two beta sheets create a "sandwich" shape, held together by interactions between conserved cysteines and other charged amino acids.
- More specifically, variable loops of β-strands, three each on the light (VL) and heavy (VH) chains are responsible for binding to the antigen .
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- In appearance, properties, and structure, black phosphorus resembles graphite -- it is black and flaky, a conductor of electricity, and has puckered sheets of linked atoms.
- Solid white phosphorus exists in two forms; at low temperatures, the β form is stable, and at high temperatures, the α form is predominant.
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- Beta particles (β) have a higher penetration power than alpha particles (they are able to pass through thicker materials such as paper).
- Alpha particles can be completely stopped by a sheet of paper.
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- This problem will work best if you have a sheet of graph paper.In a spacetime diagram one draws a particular coordinate (in our case $x$) along the horizontal direction and the time coordinate vertically.People also generally draw the path of a light ray at 45$^\circ$.This sets the relative units of the two axes.
- If my pal observes the photon to have an energy of 100 MeV while I say its energy is less than 500 keV, what is the minimal value of γ for my pal (take β ≈ 1 to make life easier)?
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- Hemoglobin is a globular protein composed of four polypeptide subunits (two alpha chains, in blue, and two beta pleated sheets, in red).
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- Some of these integral proteins are collections of beta-pleated sheets that form a channel through the phospholipid bilayer.