The Role of Side-Chain Hydrogen Bonds

I am grateful to my colleagues Jon Cooper, Yvonne Edwards, Mark Johnson, John Overington, Andrej Sali, Lynn Sibanda and Chris Topham for many stimulating discussions. 

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From the theory presented in this chapter it can be seen that studies of the pH dependence of denaturation, and also of urea denaturation, can provide valuable information for assessing the role of side-chain hydrogen bonding and the nature of the groups involved in the stabilization of the native protein. 

In conclusion, the fibrinogen-fibrin conversion provides an excellent example of a set of reactions which illustrate the role of side-chain hydrogen bonding in limited proteolysis and in protein association. Further work on step 3 may indicate to what extent the ideas of Chapter IV may be applicable. Finally, the key role which side-chain hydrogen bonding can play, not only in denaturation, but also in the modification of pK s, in limited proteolysis, and in protein association, should be noted. 

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