2010/10/01 by Wilfried Haerty, G. Brian Golding · 1 citation
Biochemistry, Genetics and Molecular Biology · #RNA and protein synthesis mechanisms #Protein Structure and Dynamics #Machine Learning in Bioinformatics
paper · doi:10.1139/g10-063
openalex publication_date 2010/10/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/15
For decades proteins were thought to interact in a "lock and key" system, which led to the definition of a paradigm linking stable three-dimensional structure to biological function. As a consequence, any non-structured peptide was considered to be nonfunctional and to evolve neutrally. Surprisingly, the most commonly shared peptides between eukaryotic proteomes are low-complexity sequences that in most conditions do not present a stable three-dimensional structure. However, because these sequences evolve rapidly and because the size variation of a few of them can have deleterious effects, low-complexity sequences have been suggested to be the target of selection. Here we review evidence that supports the idea that these simple sequences should not be considered just "junk" peptides and that selection drives the evolution of many of them.