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From experiment we've identified a subset of known mammalian protein complexes as interesting (approximately 50 CORUM complexes). We'd like to do an enrichment-style analysis to know more about them. One question I have is whether these complexes are particularly stable, since stable complexes should be biased towards detection. However, I don't have a chemistry or molecular biology background, so I don't know how to approach finding the stability of a protein complex.

Given a list of proteins in a complex, are there any conventional, in silico ways to estimate the stability of that protein complex? If not, have people published numbers for the stability of well-known complexes?

Edit: I'm okay being vague about the definition of "stability" since I'll be satisfied with an answer that uses any definition of it.

Edit: This question is answered on biostars.

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  • $\begingroup$ Is this a homework question? If so, you should add the homework tag. Also, in general I would avoid using the word stability, because it is a vague concept. If you are talking about free energy you are talking about the structure of lowest free energy. Binding of ligands may involve quite different thermodynamic properties like binding energies. It's not my field. But my point is you should define precisely what it is you want to measure. $\endgroup$ – David Feb 22 '17 at 19:37
  • $\begingroup$ @David Thanks. I edited the question to be more precise, although I'm not sure how to define "stability" in this case. Really I'm asking if there are conventional ways to estimate the theoretical tendency for protein complexes to "stick together", whatever that means exactly. $\endgroup$ – R Greg Stacey Feb 23 '17 at 1:31

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