As an alternative to looking at the conservation of cysteine residues amongst homologs of a protein of interest, is anyone aware of a server that can predict whether disulphide bond formation within a protein is likely to be required for correct folding/oligomerisation? That way one could add a reducing agent to the buffer to reduce the chances of unwanted aggregates forming. Essentially it might be useful to reduce the need for an optimisation step i.e. detection of aggregation after a gel filtration run.
It is a difficult question, and I doubt there is a reliable tool for that. You could enter a known protein sequence into various tools (disulfind, etc') and see if they can confirm the formation of a disulfide bond. If a crystalized version of the protein (or a homolog of it) show disulfide bonds, then the answer may be yes. The following page may be of some use:
https://www.researchgate.net/post/Are_there_any_user-friendly_tools_to_predict_disulfide_bonds_from_a_protein_sequence
Alternatively, you could look up evidence of dimerization in the literature - native gels before and after reduction, size estimation via gel filtration columns, and so on.
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