Asymmetric protein design from conserved supersecondary structures

We report the successful design of a dRP lyase domain fold, which agrees with the experimental NMR structure at atomic accuracy (backbone RMSD of 0.94 Å). Our results show that the residual folding information within conserved fragments, combined with efficient interface-directed sampling, can effectively yield globular proteins with novel sequences and biophysical properties.Graphical abstract

Source: Journal of Structural Biology - October 26, 2018 Category: Biology Source Type: research