KAUST Discovery Associate Professor Stefan Arold has established KAUST's first structural biology lab specializing in determining the atomic 3D structure of proteins and other biological macromolecules. The lab setup involved challenges such as assembling instruments and continuing research, but the Bioscience Core Lab at KAUST and support from colleagues aided in the process. Arold's research focuses on understanding protein function through an integrated 'hybrid' approach to analyze 3D structure and function of proteins. Why it matters: This new lab enhances KAUST's capabilities in molecular biophysics and structural biology, enabling advanced research into the functions of proteins and their implications for health and disease.
KAUST researchers have determined the atomic 3D structure of a key protein involved in plant stress signaling using X-ray crystallography at the SOLEIL synchrotron in France. Postdoctoral fellow Umar Farook Shahul Hameed optimized a tiny crystal of the plant enzyme for over six months. The team used the EIGER 9M detector to capture the weak diffraction pattern from the crystal. Why it matters: Understanding the interactions between proteins that communicate plant stress could lead to engineering more stress-tolerant crops, enhancing food security.
Daisuke Kihara from Purdue University presented a seminar at MBZUAI on using deep learning for biomolecular structure modeling. His lab is developing 3D structure modeling methods, especially for cryo-electron microscopy (cryo-EM) data. They are also working on RNA structure prediction and peptide docking using deep neural networks inspired by AlphaFold2. Why it matters: Applying advanced deep learning techniques to biomolecular structure prediction can accelerate drug discovery and our understanding of molecular functions.
KAUST researchers developed a statistical approach to improve the identification of cancer-related protein mutations by reducing false positives. The method uses Bayesian statistics to analyze protein domain data from tumor samples, accounting for potential errors due to limited data. The team tested their method on prostate cancer data, successfully identifying a known cancer-linked mutation in the DNA binding protein cd00083. Why it matters: This enhances the reliability of cancer research at the molecular level, potentially accelerating the discovery of new therapeutic targets.
KAUST researchers used cryogenic electron microscopy (cryo-EM) to study the 3D structure of protein complexes involved in DNA replication and repair. They investigated the interaction between the Y-family TLS polymerase Pol K and mono-ubiquitylated PCNA. The study revealed that DNA binding is required for Pol K to form a rigid, active complex with PCNA. Why it matters: Understanding these structural interactions may provide insights into cancer development and drug resistance mechanisms.
Natasa Przulj at the Barcelona Supercomputing Center is developing an AI framework that fuses multi-omic data to improve precision medicine. The framework uses graph-regularized non-negative matrix tri-factorization (NMTF) and network science algorithms for patient stratification, biomarker prediction, and drug repurposing. It is applied to diseases like cancer, Covid-19, and Parkinson's. Why it matters: This research can enable more personalized and effective treatments by leveraging complex biological data to understand disease mechanisms and tailor therapies.
KAUST researchers have identified a protein complex of HuR and YB1 that stabilizes messenger RNA during muscle-fiber formation. The complex protects RNA as it carries muscle-forming code through the cell. Further research aims to elucidate the individual roles of each protein in the stabilization process. Why it matters: Understanding this RNA-stabilizing complex could lead to new therapies for muscle recovery and the prevention of muscle-related pathologies.
A KAUST team discovered a simple method to fabricate microspheres using block copolymer self-assembly. The resulting particles have pH-responsive gates and a highly porous structure, granting them ultrahigh protein sorption capacity. The team leveraged their expertise in block copolymers and self-assembly to achieve this. Why it matters: This new method and the resulting particles have potential applications in biotechnology, medicine, and catalysis, advancing materials science in the region.