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Showing 1–8 of 8 results
Advanced filters: Author: Srivatsan Raman Clear advanced filters
  • Epistasis plays an important role in the evolution of novel protein functions because it determines the mutational path a protein takes. Here, the authors combine functional, structural and biophysical analyses to characterize epistasis in a computationally redesigned ligand-inducible allosteric transcription factor and found that epistasis creates distinct biophysical and biological functional landscapes.

    • Kyle K. Nishikawa
    • Nicholas Hoppe
    • Srivatsan Raman
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14
  • The use of allosteric transcription factors (aTFs) as biosensors has been constrained by their limited natural ligand repertoire. Here, the authors report a method to screen large libraries of aTF variants to develop biosensors with altered specificities to non-native ligands.

    • Kyle K. Nishikawa
    • Jackie Chen
    • Srivatsan Raman
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-18
  • A new computational approach that can be used to refine the three dimensional structural models of proteins is described. When used to refine models generated from nuclear magnetic resonance data, the method can improve the accuracy of the structures in terms of the backbone conformations and the placement of core side chains. In addition, the approach can be used to generate significantly better solutions to the X-ray crystallographic phase problem in molecular replacement trials.

    • Bin Qian
    • Srivatsan Raman
    • David Baker
    Research
    Nature
    Volume: 450, P: 259-264
  • A computational design strategy guided by biophysical principles enables engineering of split protein systems to tune their degree of interfacial destabilization, and thus reconstitution propensity, while preserving stability and catalytic activity.

    • Taylor B. Dolberg
    • Anthony T. Meger
    • Joshua N. Leonard
    Research
    Nature Chemical Biology
    Volume: 17, P: 531-539