Articles tagged with Protein Stability
Whitehead Institute scientists have developed a novel method using the enzyme sortase A to site-specifically modify proteins, increasing their potency, thermal stability, and metabolism. This technique can be applied to improve therapeutically important proteins such as interferon alpha 2 and granulocyte colony-stimulating factor 3.
Researchers at Scripps Research Institute discover a way to stabilize proteins by attaching specific oligomeric arrays of sugars, potentially increasing the stability and reducing the cost of protein-based drugs. The new methodology has broad implications for the drug industry, particularly for glycoprotein-based drugs.
A new technique called Fast Relaxation Imaging enables real-time observation of protein folding and unfolding in living cells. The method reveals that proteins are more stable and their thermal denaturation is more gradual in a cellular environment compared to an in vitro setting.
Researchers at the University of Michigan have discovered a way to stabilize proteins by linking their stability to antibiotic resistance in bacteria. This method enables easy selection for stabilizing mutations, rendering proteins more resistant to unfolding and increasing their practical utility.
Researchers at Scripps Institution of Oceanography have discovered that marine fireworms use bioluminescence for both attracting mates and as a defense mechanism to distract predators. The study found that the light is stable in temperatures as low as -20 degrees Celsius and resilient in low oxygen levels.
Researchers at Rensselaer Polytechnic Institute have developed a targeted strategy to substantially increase the thermodynamic stability of nearly any protein while preserving its unique function. The design technique creates proteins that remain stable at temperatures 10 degrees Celsius higher than normal.
Researchers identified four small molecules that stabilize both normal and mutated PAH proteins, increasing their activity and amount in human cells. These findings suggest chaperones might provide a new approach to treating individuals with phenylketonuria.
Researchers at Arizona State University have evolved new proteins in a fraction of the time it took nature, providing new lessons on how to optimize proteins. The team used 'synthetic evolution' to improve protein stability and binding efficiency, discovering that subtle amino acid changes can significantly enhance function.
Researchers have constructed a protein out of amino acids not found in natural proteins, discovering they can form a complex, stable structure resembling a natural protein. This finding could help scientists design effective drugs that won't be degraded by enzymes or targeted by the immune system.
Researchers from UW-Madison reveal that protein stability under severe confinement is a delicate balance between energy and entropy. This finding has significant implications for numerous applications, including laundry detergent engineering where enzymes must withstand high temperatures.
Researchers at Duke University have shown that hydrogen bonds are crucial for protein folding and are highly conserved across different proteins. Their study found that deleting hydrogen bonds from proteins led to destabilization of the structure, supporting the importance of these bonds in protein folding.
Researchers discovered an alternate folding mechanism that protects some proteases from breakdown by other proteases, making them highly resistant to degradation. This novel strategy, involving a pro-region catalyst, allows for exceptional stability and rigidity in the folded state.
Researchers from UNC School of Medicine and Pharmacy have developed a new method to calculate protein stability, which could improve drug design and engineering. The approach uses computational manipulations to predict the effects of amino acid mutations on protein stability.
By altering the order of structural elements during folding, researchers successfully redesigned the protein G's pathway to mimic that of another protein. The re-engineered protein exhibited increased stability and a significantly faster folding rate than its natural counterpart.