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In proteins, functional divergence involves mutations that modify structure and dynamics. Here we provide experimental evidence for an evolutionary mechanism driven solely by long-range dynamic motions without significant backbone adjustments,

In proteins, functional divergence involves mutations that modify structure and dynamics. Here we provide experimental evidence for an evolutionary mechanism driven solely by long-range dynamic motions without significant backbone adjustments, catalytic group rearrangements, or changes in subunit assembly. Crystallographic structures were determined for several reconstructed ancestral proteins belonging to a GFP class frequently employed in superresolution microscopy. Their chain flexibility was analyzed using molecular dynamics and perturbation response scanning.

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    Date Created
    • 2015-01-06
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    Identifier
    • Digital object identifier: 10.1016/j.str.2014.11.011
    • Identifier Type
      International standard serial number
      Identifier Value
      0969-2126
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    Kim, Hanseong, Zou, Taisong, Modi, Chintan, Doerner, Katerina, Grunkemeyer, Timothy J., Chen, Liqing, Fromme, Raimund, Matz, Mikhail V., Ozkan, S. Banu, & Wachter, Rebekka M. (2015). A Hinge Migration Mechanism Unlocks the Evolution of Green-to-Red Photoconversion in GFP-like Proteins. STRUCTURE, 23(1), 34-43. http://dx.doi.org/10.1016/j.str.2014.11.011

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