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Showing 1–7 of 7 results
Advanced filters: Author: Burckhard Seelig Clear advanced filters
  • The emergence of a primordial RNA world would have required the formation of RNA polymers of sufficient length to possess catalytic activities, which are difficult to obtain by spontaneous polymerization. An analysis of an autocatalytic assembly pathway that can self-construct a functioning ribozyme from smaller oligonucleotide building blocks describes a potential route for RNA extension.

    • Burckhard Seelig
    News & Views
    Nature Chemical Biology
    Volume: 4, P: 654-655
  • Family 1 glycosidases (GH1) are present in the three domains of life and share classical TIM-barrel fold. Structural and biochemical analyses of a resurrected ancestral GH1 enzyme reveal heme binding, not known in its modern descendants. Heme rigidifies the TIM-barrel and allosterically enhances catalysis.

    • Gloria Gamiz-Arco
    • Luis I. Gutierrez-Rus
    • Jose M. Sanchez-Ruiz
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-16
  • It has been challenging to rationalize the emergence of complex biochemical systems because many parts with different functions needed to come together. This Perspective proposes a molecular bricolage—an evolutionary tinkering involving parts that initially evolved for unrelated functions—to provide an intellectual framework to study the origin of protein translation.

    • Burckhard Seelig
    • Irene A. Chen
    Reviews
    Nature Chemistry
    Volume: 17, P: 11-19
  • Structural characterization of an artificial zinc-dependent enzyme created by in vitro evolution yields a new, flexible fold that challenges straightforward definitions of active site residues and raises questions about protein evolution.

    • Fa-An Chao
    • Aleardo Morelli
    • Burckhard Seelig
    Research
    Nature Chemical Biology
    Volume: 9, P: 81-83
  • New enzymatic activities can be evolved de novo (that is, without the need for prior mechanistic information) by using mRNA-display. Functional proteins were selected for from an in vitro translated protein library of high complexity and it was possible to isolate novel RNA ligases that exhibited rate enhancements of more than two million-fold.

    • Burckhard Seelig
    • Jack W. Szostak
    Research
    Nature
    Volume: 448, P: 828-831