#proteins

The Scientific Research Notes of S. Sunkavally. Years: 1986 - 1990.

The Scientific Research Notes of S. Sunkavally. Years: 1986 - 1990.

A study by researchers at Duke University School of Medicine identifies a new way that G protein–coupled receptors (GPCRs)—targets of roughly one-third of FDA-approved drugs—control signaling in cells. The paper is published in the journal Nature.

Imperfect polymer sequences still control protein function, revealing new design rules

What happens when a scientific problem seems too complex to solve precisely, yet understanding it could reshape how researchers design new materials and medicines? For decades, much of the polymer science community has relied on a "good enough" approach to a stubborn problem: binding a polymer to a protein in a precise way that reliably controls how the protein behaves. Polymers—long chains built from repeating small molecules called monomers—make up much of the material world, from plastic bags and clothing to advanced medicines. Designing those chains to interact with proteins, however, has pushed the limits of precision chemistry. In a study published in Angewandte Chemie, chemist Darwin Gomez, a member of Adrian Figg's lab, and fellow Virginia Tech researchers Ronnie Mondal and Swarnadeep Seth demonstrated that even when a polymer lacks a perfectly tailored sequence, the protein it binds to can still function as intended.

New recyclable protein textiles could cut microplastic pollution and lower clothing waste

The textile industry produces a substantial portion of the world's waste, with only about 12% of fiber materials ending up in recycling. Textiles also account for much of the microplastics in oceans. During every wash cycle, synthetic fibers shed microplastics that are flushed down the drain and eventually enter aquatic environments. Increasing textile recycling alone won't solve this problem because most petrochemical-based fibers are difficult to recycle and continue to release persistent microplastics throughout their life cycle. Engineers from Washington University in St. Louis may have a solution, thanks to dedicated synthetic biology work in the lab of Fuzhong Zhang, the Francis F. Ahmann Professor in the Department of Energy, Environmental & Chemical Engineering in the McKelvey School of Engineering and co-director of Synthetic Biology Manufacturing of Advanced Materials Research Center (SMARC).

Time-evolving polymer recreates nature's signature twist

Science has long taken inspiration from the natural world, and few natural designs are as iconic as the helical shape that makes life possible. The best-known example of such a molecule is DNA, a double helix that carries the genetic instructions for all living organisms. Similar helical shapes are also found in proteins. This shape is special in that it imparts a certain adaptability to biological molecules. For instance, by changing how tightly they twist or even the direction of their twist, biological systems can respond and adapt to their environment. This helps proteins adjust their shapes to fold correctly and perform essential tasks.