How do miniproteins fold?

Derek N. Woolfson*, Emily G. Baker, Gail J. Bartlett

*Corresponding author for this work

Research output: Contribution to journalShort survey (Academic Journal)peer-review

2 Citations (Scopus)
245 Downloads (Pure)


How does the amino acid sequence of a protein chain determine and maintain its three-dimensional folded state? Answering this question—a key aspect of the protein-folding problem (1)—would help to explain how multiple noncovalent interactions conspire to assemble and stabilize complicated biomolecular structures; to predict protein structure and function from sequence for proteins that cannot be characterized experimentally; and to design new protein structures that do not exist in nature (2). On page 168 of this issue, Rocklin et al. use parallel protein design on a massive scale to create thousands of miniprotein variants and to determine what sequences specify and stabilize these structures (3). The work opens up considerable possibilities for protein folding and design.
Original languageEnglish
Pages (from-to)133-134
Number of pages2
Issue number6347
Publication statusPublished - 14 Jul 2017

Structured keywords

  • Bristol BioDesign Institute

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