In think most of the salt bridges I recall in structures are either in the core of the protein or in interfaces (crystallin or complex interfaces with little or no polar solvent around). Just like charge interactions, the lower dielectric constant of the environment makes them stronger.
Carlos Em 20/10/2012, às 04:49, Ed Pozharski escreveu: > On 10/19/2012 10:37 PM, Acoot Brett wrote: >> Will you please explain to me why the protein salt bridge can still exist in >> the high salt concentration as used in the crystallization condition? > > You are saying it as if there is some fundamental law of nature that says > that salt bridges cannot be maintained at high salt concentration. I know of > no such law. The observation simply means that (mostly for entropic reasons) > the free energy of the salt bridge is still lower. If you present your case > as to why the salt bridges must be disrupted, we can poke holes in it :) > > Cheers, > > Ed > > -- > Oh, suddenly throwing a giraffe into a volcano to make water is crazy? > Julian, King of Lemurs
