The 2024 Nobel Prize in Chemistry was awarded to David Baker, Demis Hassabis, and John M. Jumper for the development of protein structure prediction and design. At the ALS, Baker leveraged high-throughput small-angle x-ray scattering (SAXS) and protein crystallography capabilities to design novel proteins and pave a new pathway for science, technology, and the environment. Read more »
Caught in the Actinium
In this work, researchers demonstrated a macromolecular scaffold that combines an 8-coordinate synthetic ligand and a mammalian protein to characterize the solution and solid-state behavior of the longest-lived actinium isotope. The information could help design better cancer treatments. Read more »
Computer-Aided Protein Design for New Biomaterials
Using a computer-based approach, researchers designed porous protein crystals that were revealed to be stable, tunable, and atomically accurate using x-ray scattering and diffraction at the ALS. The work provides a powerful new platform for biological materials engineering and opens up wide applications in biotechnology and medicine. Read more »
Gemini Beamline 2.0.1 Banks Its First Protein Structure
A protein structure obtained from ALS Beamline 2.0.1 (“Gemini”) has recently been published in the literature and deposited into the Protein Data Bank (PDB)—two significant firsts for this beamline. The structure helped provide new insights into the molecular mechanisms involved in triggering certain inflammatory diseases. Read more »
Uncompetitive, adduct-forming SARM1 inhibitors are neuroprotective in preclinical models of nerve injury and disease
Researchers describe potent small-molecule inhibitors that are neuroprotective in preclinical models of nerve injury and disease. The cover depicts the destruction of an axon by the enzyme SARM1, shown disproportionately large to convey its catastrophic role in driving degeneration once it is activated upon injury. Read more »
Protein Assemblies Show Surprising Variability
Protein-structure studies performed in part at the ALS helped researchers discover that the protein assemblies in a key carbon-cycling enzyme can rearrange with surprising ease. The findings raise the prospect of genetically tuning the protein in agricultural plant species to produce more productive and resource-efficient crops. Read more »
Chemical acylation of an acquired serine suppresses oncogenic signaling of K-Ras(G12S)
Small-molecule targeting of particular KRAS mutations offer promise for cancer therapy. The cover depicts a small-molecule ligand (red) inhibiting the oncogenic mutant protein K-Ras(G12S) (cyan) by forming a covalent ester adduct at the mutant serine. Read more »
An Expanded Set of DNA Building Blocks for 3D Lattices
Researchers studied 36 DNA-based molecular junctions and discovered factors that yield superior self-assembled 3D lattice structures. The work expands the set of building blocks for lattices that can scaffold molecules into regular arrays, from proteins for structure studies to nanoparticles for nano-antennas and single-particle sensors. Read more »
Protein Structures Aren’t Set in Stone
A group of researchers studying the world’s most abundant protein, an enzyme involved in photosynthesis called rubisco, showed how evolution can lead to a surprising diversity of molecular assemblies that all accomplish the same task. The findings reveal the possibility that many of the proteins we thought we knew actually exist in other, unknown shapes. Read more »
Deep-Learning AI Program Accurately Predicts Key Rotavirus Protein Fold
Rotaviruses are the major causative agents of gastroenteritis worldwide. Attempts to design vaccines are complicated by the rotaviruses’ enormous genetic and immunological diversity. At the ALS, researchers validated the novel structure of a key rotavirus protein, predicted using AlphaFold2, a deep-learning artificial-intelligence program. Read more »
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