Protein-protein interactions play a major role in determining the thermodynamic properties of protein solutions as well as the phase behavior, with attractive interactions driving phase separation.  The anisotropy of shape and functionality of proteins complicates the prediction of protein interactions, and we examine here the possibility of predicting the conflicting trends seen in the interactions and phase behavior of lysozyme and chymosin B; the former shows salting-out behavior over a wide range of pH values while the latter salts in at low salt near the pI.  Our emphasis is on identifying the orientational configurations that contribute most strongly to the overall interactions � due to high-complementarity interactions characteristic of molecular recognition events � and on calculating the effect of salt on such interactions.  The roles of these high-complementarity configurations relative to other interactions and the ability to predict the general trend in solution behavior (salting-out or salting-in) will be discussed.

Anisotropic contributions to protein-protein interactions in salting-out and salting-in

243rd National Meeting (2012)

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