Latent evolutionary potentials under the neutral mutational drift of an enzyme

By Gil Amitai, R. Gupta, Dan S. Tawfik. 2007

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A structural model of latent evolutionary potentials underlying neutral networks in proteins (2007, result): “Furthermore, this view reconciles the ideas of adaptive and neutral mutations, thus providing a conceptual framework to rationalize pertinent experimental results reported in the companion article (Amitai et al., 2007) and elsewhere (Aharoni et al.”
Improved Modeling of Side-Chain–Base Interactions and Plasticity in Protein–DNA Interface Design (2012, background): “29,31,32 This neutral drift facilitates enzyme adaptations by reducing the number of mutations necessary to acquire new functions in the face of evolutionary pressure and is particularly important for the endonuclease family of proteins.”
Enzyme promiscuity: a mechanistic and evolutionary perspective. (2010, background): “This pattern is consistent with promiscuous activities not being under selection and also with the observation that promiscuous activities show large increases and decreases in response to one or a few mutations that are neutral with respect to the primary function (110, 111).”
Exploring protein fitness landscapes by directed evolution (2009, unknown): “Because many of the mutations made by recombination are neutral or nearly neutral, recombination is an efficient way to generate the neutral drifts (the accumulation of neutral mutations) that have been shown to lead to increases in promiscuous function”