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In some proteins, strong covalent bridges are formed between two cysteines at different sites in the chain.
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A disulphide bond between two cysteines (residues 25 and 80) covalently links these sheets [5].
Some have one or two cysteines at position 6-9 (numbering according to HLA-A2 ) while some have an additional cysteine at position 48.
The M13 phage displays a randomized amino acid heptamer between two cysteine residues on the pIII minor coat protein.
This trait requires two mutations, for example a disulphide bridge between two cysteine residues.
Thiol-reactive cross-linkers work by forming covalent bonds between two cysteine residues.
A disulphide bridge between two cysteine residues located in the first extracellular segment stabilizes the beta-sheet structure [ 53].
The six cysteines at position of 9, 11, 15, 23, 40 and 49 form three disulfide bridges between C9 and C23, C11 and C40, C15 and C49 showing abcabc pattern.
All members of the OT, AVP and VT peptide family share high sequence similarity, namely an N-terminal six-residue ring, formed by a disulfide bond between the two cysteine residues at positions 1 and 6, and a flexible C-terminal three-residue tail with a highly conserved Pro and a glycine amide at position 9 (CXXXXCPXG).
The number of aa residues between the two cysteines of the ZF1 C2H2 motif was 15.
OXT has a disulfide bond between the two cysteines, and reduction of the disulfide bond inactivates OXT [ 5].
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