Abstract
One of the current challenges in protein engineering is to accurately predict distal mutations which lead towards desired functional changes. A large and continuously developed body of research suggests protein function evolves through subtle changes as a result of sequence variations which impact dynamics on a local scale, rather than global dynamics which are generally associated with changes in the 3-D fold of a protein. In order to understand and subsequently predict the functional outcome of mutations, we must first understand how changes in conformational dynamics and internal protein networking give rise to changes in biochemical quantities.
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