This research investigates how antiviral drug resistance develops by examining structural changes in viral proteins. Using protein crystallography, it identified why SARS-CoV-2 mutations prevent Paxlovid binding and discovered two compounds capable of inhibiting resistant viruses. The findings could guide development of more effective antivirals against future drug-resistant viral infections.

This research introduces the first simple mathematical model capable of capturing the cooperative folding of alpha helices, a fundamental protein structure. By revealing how these proteins fold, stabilize, and misfold, the model offers new insights into diseases such as Alzheimer's and Parkinson's while providing a fast, flexible platform for protein research.

Using a Twilight analogy, this research explains antibiotic-resistant bacteria as “vampires” protected by membranes. By crystallizing membrane proteins and analyzing them with X-ray techniques, the study reveals their structure and function. This enables precise drug design to block these proteins, potentially overcoming antibiotic resistance and targeting harmful bacteria more effectively.

This research designs simplified, custom-built proteins to understand how natural proteins work and to create new biocatalysts. By choosing a desired function and designing the amino-acid sequence and structure from scratch, the project aims to develop clean, efficient protein-based alternatives to environmentally harmful industrial chemistry.

The researcher rebuilds how cells sort materials to understand Alzheimer’s and Parkinson’s diseases. Using proteins and lipids like Lego pieces, they study how a key protein, retromer, malfunctions and disrupts cell transport. With cryogenic electron tomography, they aim to model this process and guide new treatments that restore healthy cellular function.