All articles tagged with #protein folding
AlphaFold, developed by DeepMind, has revolutionized biology by accurately predicting protein structures, earning a Nobel Prize and expanding into DNA, RNA, and drug interactions, with ongoing advancements aimed at understanding cellular systems and improving medicine.
Scientists at King's College London have created the world's hottest microengine, operating at temperatures hotter than the sun's core, which could revolutionize our understanding of thermodynamics and aid in developing treatments for diseases by improving knowledge of protein folding.
Caltech researchers have discovered that nearly 20% of mitochondrial proteins are imported during their synthesis, guided by folding patterns and structural signals, overturning the traditional model that proteins are imported only after translation is complete.
AI is significantly advancing scientific research by enabling breakthroughs in protein structure prediction, brain mapping, materials science, climate forecasting, and fundamental physics, while also paving the way for autonomous laboratories and AI-driven hypothesis generation, despite some challenges in interpretability and understanding.
Researchers used a 36-qubit trapped-ion quantum computer with a specialized algorithm to solve complex protein folding problems involving up to 12 amino acids, marking a significant milestone in quantum biology and optimization, and demonstrating the platform's potential for tackling computationally hard problems beyond classical capabilities.
Demis Hassabis and James Manyika discuss the transformative potential of AI in advancing scientific discovery, highlighting DeepMind's achievements like AlphaFold, which solved the protein folding problem and accelerated research across various fields. They emphasize the importance of responsible AI development, collaboration with diverse stakeholders, and the potential for AI to unlock new scientific insights and address global challenges.
A new study led by researchers from the University of Helsinki and the Georgia Institute of Technology has discovered a mechanism driving the evolution of multicellular life, highlighting the role of altered protein folding. Through experimental evolution with laboratory yeast, the study found that changes in protein folding, particularly the expression of the chaperone protein Hsp90, played a crucial role in the evolution of novel multicellular traits, such as the development of robust bodies in snowflake yeast. This research emphasizes the significance of non-genetic mechanisms in driving rapid evolutionary change and provides insights into the complex nature of evolutionary adaptations.
Scientists have discovered a new, intermediate state in the process of protein folding, showing that folding can occur in two stages, one fast and the next much slower. This newly observed dry molten globule state, occurring over a period of 3–10 milliseconds, was found to be a crucial step in the protein folding process. The discovery provides insight into the structural evolution of proteins and may have implications for understanding diseases related to protein misfolding.
Researchers from the University of Massachusetts Amherst have uncovered the carbohydrate-based code that governs the folding of certain proteins, offering potential therapeutic avenues for diseases caused by protein misfolding. Using innovative techniques such as glycoproteomics, the team investigated the role of carbohydrates attached to proteins called serpins in ensuring correct folding. Understanding this glyco-code could lead to targeted drug therapies for diseases like emphysema, cystic fibrosis, and Alzheimer's. The discovery of the carbohydrate-based chaperone system in the endoplasmic reticulum (ER) sheds light on how chaperones identify correctly folded proteins. The enzyme UGGT tags misfolded proteins with specific sugars, allowing chaperones to recognize and correct folding errors. This research opens doors for understanding and treating diseases resulting from misfolded proteins.
Researchers from the University of Tokyo have developed a novel physical theory, called WSME-L, that can accurately predict how proteins fold into specific structures. This model overcomes limitations of previous models and can provide insights into protein folding pathways and transient states. Improved knowledge of protein folding has significant implications for medical research and industrial processes.
Scientists have discovered a connection between number theory and evolutionary genetics, revealing that mathematical relationships underpin the mechanisms governing the evolution of life on molecular scales. The study found that mutational robustness, which generates genetic diversity, can be maximized in naturally-occurring proteins and RNA structures. The maximum robustness follows a self-repeating fractal pattern called a Blancmange curve and is proportional to a basic concept of number theory called the sum-of-digits fraction. This research highlights the role of mathematics in understanding the structure and patterns of the natural world.
A new high-throughput technique has been developed that can analyze the folding stabilities of nearly one million protein sequences at a time. This method, which is fast, accurate, and scalable, provides valuable data for understanding protein folding and improving machine learning models. By measuring stability for 1.8 million sequences, researchers obtained 776,000 high-quality folding stabilities. The large dataset is already proving useful for developing machine learning models to predict protein folding stability and understanding the impact of genetic variants on protein stability.
A new method has been developed to measure protein folding stabilities on a large scale, providing insights into evolutionary trends and potential applications in machine learning. Protein alterations that affect stability have significant implications for evolution, health, disease, and biotechnology.