protein stability

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Across
  1. 1. is an undesirable association of partially unfolded proteins that may trigger immune responses.
  2. 7. covalent bond is formed between two cysteine residues that play a key role in stabilizing tertiary and quaternary structures.
  3. 8. bond between carbonyl oxygen and amide hydrogen stabilise α-helices and β-sheets.
  4. 10. interaction is the dominant stabilizing force in protein tertiary structure resulting from burial of non-polar residues away from water.
Down
  1. 2. is chemical degradation initiated by free radicals.
  2. 3. Disulfide exchange is formation of incorrect covalent S–S bonds between ..... residues
  3. 4. is the cleavage of peptide or amide bonds caused by nucleophilic attack of water.
  4. 5. is the conversion of an amino acid into a different stereochemical form due to rearrangement around a chiral α-carbon.
  5. 6. is a degradation pathway involving hydrolysis of amide side chains of Asn or Gln leading to changes in protein charge.
  6. 9. is the only amino acid lacking a chiral α-carbon and therefore incapable of stereochemical isomerisation.