Supercharging proteins can impart unusual resilience

Michael S. Lawrence, Kevin J. Phillips, David R. Liu

Research output: Contribution to journalArticle

308 Scopus citations

Abstract

The creation and application of proteins with desirable properties would benefit significantly from strategies to reduce the problem of protein aggregation. Here we demonstrate "supercharging" the surface of three disparate proteins to alter their net charge by as much as 55 charge units, without destroying protein folding or function. These supercharged variants acquire unusual resistance to aggregation and, unlike their natural counterparts, can refold and function even after boiling. Our findings demonstrate an approach to increasing protein robustness, suggest surprisingly broad, untapped plasticity at protein surfaces, and may help explain the modest net-charge distribution of natural proteins.

Original languageEnglish (US)
Pages (from-to)10110-10112
Number of pages3
JournalJournal of the American Chemical Society
Volume129
Issue number33
DOIs
StatePublished - Aug 22 2007

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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