In this fascinating episode, we welcome Dr. Ulijn, a pioneering researcher in the field of peptide sequence buildup and molecular adaptation. He delves into his groundbreaking study that illuminates the behavior of living systems and their distinctive ability to distribute stress among a vast number of covalent and noncovalent interactions in mixtures of molecules.

Dr. Ulijn takes us on a journey into the world of biomolecular complexity, starting from the basics. He discusses how the selection of a chemical interaction space of mixtures of 5 or 15 dipeptides, through reversible enzymatic sequence exchange, can produce 25 or 225 dynamically interacting tetrapeptides. This setup allows his team to study complex systems that are usually challenging to investigate due to their inherent complexity.

Dr. Ulijn describes the complex process through which the abundance of tetrapeptide sequences can be analyzed, leading to patterns that are surprisingly interpretable. These patterns reveal that a system with this level of complexity is capable of responding stochastically, self-organizing, and driving sequence selective oligomerization in response to changes in external conditions.

Moreover, he explains how the system exhibits robustness, demonstrating its ability to distribute the impact of a change of conditions across a multitude of interactions. The episode culminates in a fascinating discussion of the implications of this research on our understanding of living systems.

If you're interested in peptide sequences, molecular complexity, and the adaptive capabilities of living systems, this conversation with Dr. Ulijn will captivate you.

Keywords: Peptide Sequence Buildup, Enzymatic Exchange, Dipeptides, Tetrapeptides, Biomolecular Complexity, Molecular Adaptation, Robustness, Stochastic Processes.

https://doi.org/10.1016/j.chempr.2022.03.016 Enzymatic exchange of mixes of dipeptides leads to the buildup of tetrapeptides that can be tracked. Self-organization drives selective peptide sequence buildup