Publications by authors named "Abbas Idris"
Allosteric modulation of protein function, wherein the binding of an effector to a protein triggers conformational changes at distant functional sites, plays a central part in the control of metabolism and cell signalling. There has been considerable interest in designing allosteric systems, both to gain insight into the mechanisms underlying such 'action at a distance' modulation and to create synthetic proteins whose functions can be regulated by effectors. However, emulating the subtle conformational changes distributed across many residues, characteristic of natural allosteric proteins, is a significant challenge.
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- Protein clustering is vital for cell functions and related to diseases, but traditional methods struggle to detect small protein oligomers effectively.
- The CluMPS (clusters magnified by phase separation) reporter enhances the visibility of these small clusters, allowing for sensitive detection and quantification of protein aggregates that are otherwise hard to see.
- The study demonstrates CluMPS's capability to identify both pathological and normal protein clusters in cells, supporting its use for advanced research in understanding protein assembly in their natural environment.
Article Synopsis
- Proteins can change shapes in response to environmental signals, similar to how transistors manage information flow in computers.
- Designing proteins with two stable shapes is complex, as it involves creating a specific energy landscape with two low-energy states.
- The study presents "hinge" proteins that switch between two accurately designed states—one when a ligand is absent and one when it is present—validated through advanced imaging and spectroscopy techniques.