The fundamental roles that peptides and proteins play in today's biology makes it almost
indisputable that peptides were key players in the origin of life. Insofar as it is appropriate to …

Primordial sequence signatures in modern proteins imply ancestral origins tracing back to
simple peptides. Although short peptides seldom adopt unique folds, metal ions might have …

Highlights•Sub-domain segments may carry hints to the evolution of protein
domains.•Similar sub-domain segments shared among globally dissimilar domains are …

The vast majority of theoretically possible polypeptide chains do not fold, let alone confer
function. Hence, protein evolution from preexisting building blocks has clear potential …

De novo emergence demands a transition from disordered polypeptides into structured
proteins with well-defined functions. However, can polypeptides confer functions of …

The evolution of proteins from simpler, self-assembled peptides provides a powerful
blueprint for the design of complex synthetic materials. Previously, peptide–metal …

The emergence of novel proteins, beyond these that can be readily made by duplication and
recombination of preexisting domains, is elusive. De novo emergence from random …

The design of completely synthetic proteins from first principles—de novo protein design—is
challenging. This is because, despite recent advances in computational protein–structure …

Coiled coils are a widespread and well understood protein fold. Their short and simple
repeats underpin considerable structural and functional diversity. The vast majority of coiled …

The extant complex proteins must have evolved from ancient short and simple ancestors.
The double-ψ β-barrel (DPBB) is one of the oldest protein folds and conserved in various …