PerspectiveBiochemistry

How do miniproteins fold?

See allHide authors and affiliations

Science  14 Jul 2017:
Vol. 357, Issue 6347, pp. 133-134
DOI: 10.1126/science.aan6864

You are currently viewing the summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

Summary

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.