Baker - 3 - Protein Structure
- United Kingdom
- University of Sheffield
- Biochemistry 211
- Baker - 3 - Protein Structure
Last Modified: 2017-01-14
- All side chains point away (outside) and down from the helix.
- It is right-handed coil (walking down circular staircase and turn right - left is the banister).
- The helix carries a macro charge - charged on both ends (amino = +ve, carboxyl = -ve)
- Sheets can be flat, however, due to steric clashes between the backbone and side chains, can become twisted.
- They also do not need to be next to each other in the sequence - bits from the whole sequence can join together to make one beta sheet.
- beta-alpha-beta unit
- beta hairpin (3 antiparallel beta sheets connected together).
- alpha-alpha motif (two opposite direction helices packed together).
- helix-turn-helix motif (two helices close together).
- How residues are arranged in the active site.
- How the substrates bind to the enzyme.
- Hydride transfer and formation of iminoglutarate (intermediate)
- Attack by bound water to form carbinolamine (intermediate).
- Collapse of carbinolamine to give α-ketoglutarate and ammonia.
- Asp165 acts as a base as domains become closer to remove a proton from amino group of glutamate.
- Lys125 acts as a base, removing proton from the enzyme bound water molcule.
- The activated water attacks the alpha C of glutamate to form carbinolamine.
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