The application and development of network principles to protein modeling have led to significant advancement in understanding the underlying determinants of protein folds. In this work, we will use a modified version of the network principle 'degrees of separation' we term 'levels of separation' (LOS) to provide insight into the evolution of protein folds. In specific, we propose that long-range tertiary interactions between the transition and native state form in LOS. Rationalizing the formation of long-range interactions in this way provides a means for understanding the mechanism by which the formation of the native tertiary structure can be obtained from the transition-state. We present a theoretical model that visualizes how a protein may fold through a sequence of modifications of the transition state to the native state facilitated by LOS. Our approach is interdisciplinary and unites the fields of network theory, mathematics and biochemistry. A number of proteins are being studied. The model protein system used in our current study is chymotrypsin inhibitor 2; a small mixed a/�-protein consisting of sixty-four residues.References:L.H. Greene and T.M. Grant (2012) Protein folding by 'levels of separation': A hypothesis, FEBS Letters 586  , 962-966.

Protein folding using a network approach

246th National Meeting (2013)

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