We used numerous bioinformatic predictors of secondary structure and protein disorder to compare four polypeptide libraries: (A) random sequences in which the ratios of individual amino acids...

In short, we wanted to understand the physico-chemical principles that underpin protein structure, folding, assembly, and stability. In other words, we sought to decipher the underlying sequence-to-structure relationships for these properties.

The far-UV circular dichroism spectra (190~260 nm) is commonly used for analyzing the secondary structure of proteins such as α-helix, β-folding, and random curling. The BSA stock solution (60 μmol/L, without sodium ion) at different pH was diluted to 0.6 μmol/L with corresponding pH buffer solution.

We used numerous bioinformatic predictors of secondary structure and protein disorder to compare four polypeptide libraries: (A) random sequences in which the ratios of individual amino acids reflect those found in natural proteins, (B) fragments of natural proteins from the TOP8000 database of non-redundant structurally characterized proteins ...

We find that the structural predictions for de novo and random proteins differ significantly from conserved proteins. Interestingly, a positive correlation between disorder and confidence scores (pLDDT) is observed for de novo and random proteins, in contrast to the negative correlation observed for conserved proteins.