Enzymes catalyze multistep reactions by stabilizing successive transition states within well organized, yet dynamic active sites. However, computational enzyme design typically targets a single transi...

Enzymes catalyze multistep reactions by stabilizing successive transition states within well organized, yet dynamic active sites. However, computational enzyme design typically targets a single transi...

In honour of the 40th anniversary of Protein Engineering, Design and Selection (PEDS), Protein Engineering: Status Report brings together contributions fro

Abstract. With this status report, we aim to provide a timely snapshot of the protein engineering field as a broad and rapidly advancing discipline that in

Abstract. Structural dynamics play a crucial role in protein function, and tuning these dynamics through mutagenesis has emerged as a promising strategy fo

The TIM barrel is nature’s most versatile enzyme fold, yet de novo variants lack functional active sites. Minimal de novo TIM barrels have now been converted into enzymes by designing structural lids ...

The TIM barrel is nature’s most versatile enzyme fold, yet de novo variants lack functional active sites. Minimal de novo TIM barrels have now been converted into enzymes by designing structural lids ...

Join 6th Protein Engineering Canada (PEC) Conference, June 22-24, 2026. Learn more on Fourwaves.

YouTube video by The DiffUSE Project

Both experts in the field, one with an academic view and one from industry, they discuss what can be done today with protein design, new innovations coming in the next year or two, and how they think ...

The ability to create efficient artificial enzymes for any chemical reaction is of great interest. Here, we describe a computational design method for increasing the catalytic efficiency of de novo en...

Distal mutations, though far from the active site, enhance Kemp eliminase catalysis by tuning conformational dynamics that facilitate substrate binding and product release, thereby promoting the full catalytic cycle.

Amino acid residues distant from an enzyme’s active site are known to influence catalysis, but their mechanistic contributions to the catalytic cycle remain poorly understood. Here, we investigate the...

We report the development and initial experimental validation of a computational design procedure aimed at generating enzyme-like protein catalys...

Despite substantial effort, the de novo design of a stable TIM-barrel protein fold has remained elusive. A Rosetta-based computational strategy identifies a unique 184-residue sequence that adopts a T...

The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model pepti...

The TIM barrel is the most prevalent fold in natural enzymes, supporting efficient catalysis of diverse chemical reactions. While de novo TIM barrels have been successfully designed, their minimalisti...

<div style="text-align: justify;">The&nbsp; research&nbsp; group&nbsp; „Organic&nbsp; Chemistry&nbsp; and&nb...

Computational design of molecular recognition remains challenging despite advances in deep learning. The design of proteins that bind to small molecules has been particularly difficult because it requ...

The role of amino-acid residues distant from an enzyme's active site in facilitating the complete catalytic cycle—including substrate binding, chemical transformation, and product release—remains poor...