Data from: Random heteropolymers preserve protein function in foreign environments

  • Brian Panganiban (Contributor)
  • Baofu Qiao (Contributor)
  • Tao Jiang (Contributor)
  • Christopher DelRe (Contributor)
  • Mona M. Obadia (Contributor)
  • Trung Dac Nguyen (Contributor)
  • Anton A.A. Smith (Contributor)
  • Aaron Hall (Contributor)
  • Izaac Sit (Contributor)
  • Marquise G. Crosby (Contributor)
  • Patrick B. Dennis (Contributor)
  • Eric Drockenmuller (Contributor)
  • M Olvera de la Cruz (Contributor)
  • Ting Xu (Contributor)
  • Izaac Sit (Contributor)
  • Monica Olvera De La Cruz (Contributor)
  • Ting Xu (Contributor)



The successful incorporation of active proteins into synthetic polymers could lead to a new class of materials with functions found only in living systems. However, proteins rarely function under the conditions suitable for polymer processing. On the basis of an analysis of trends in protein sequences and characteristic chemical patterns on protein surfaces, we designed four-monomer random heteropolymers to mimic intrinsically disordered proteins for protein solubilization and stabilization in non-native environments. The heteropolymers, with optimized composition and statistical monomer distribution, enable cell-free synthesis of membrane proteins with proper protein folding for transport and enzyme-containing plastics for toxin bioremediation. Controlling the statistical monomer distribution in a heteropolymer, rather than the specific monomer sequence, affords a new strategy to interface with biological systems for protein-based biomaterials.
Date made availableFeb 13 2019

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