Research Spotlight: Which proteins respond to magnetic fields? 🔬
At the Quantum Biology Institute (QBI), our research spans four connected areas: quantum, proteins, omics, and metabolism. Today, we're taking a closer look at our work on proteins.
Our goal here is to identify proteins that respond to magnetic fields and understand the molecular features that might explain this sensitivity.
One starting point is MagLOV2, an engineered protein whose fluorescence (the light it emits when illuminated) changes in response to magnetic fields. Building on this work, we're investigating whether similar responses occur in proteins found naturally across different organisms.
So, where are we today?
Our team has screened 34 naturally occurring LOV-domain sequences from bacteria and archaea. LOV (Light-Oxygen-Voltage) domains are light-sensitive regions of proteins, and our screening has identified several with measurable magnetic-field-dependent fluorescence, known as magnetofluorescence.
These include proteins from diverse groups of organisms, from cyanobacteria to archaea, suggesting that this property may be more widespread than previously understood.
We're also investigating flavoproteins naturally found in E. coli, where early experiments have identified a promising magnetofluorescence signal associated with thioredoxin reductase (trxB). At the same time, we're working to distinguish these responses from background fluorescence and better understand how illumination conditions influence what we measure.
Alongside these findings, we've experimentally supported some predictions from our kinetic model, which helps us understand how magnetofluorescence changes under different illumination conditions.
The next steps are to repeat and expand our screening, characterize the proteins showing promising responses, and investigate what they have in common.
Ultimately, we want to move beyond identifying magnetosensitive proteins toward understanding, and potentially predicting, the molecular features responsible for their responses.
At the Quantum Biology Institute (QBI), our research spans four connected areas: quantum, proteins, omics, and metabolism. Today, we're taking a closer look at our work on proteins.
Our goal here is to identify proteins that respond to magnetic fields and understand the molecular features that might explain this sensitivity.
One starting point is MagLOV2, an engineered protein whose fluorescence (the light it emits when illuminated) changes in response to magnetic fields. Building on this work, we're investigating whether similar responses occur in proteins found naturally across different organisms.
So, where are we today?
Our team has screened 34 naturally occurring LOV-domain sequences from bacteria and archaea. LOV (Light-Oxygen-Voltage) domains are light-sensitive regions of proteins, and our screening has identified several with measurable magnetic-field-dependent fluorescence, known as magnetofluorescence.
These include proteins from diverse groups of organisms, from cyanobacteria to archaea, suggesting that this property may be more widespread than previously understood.
We're also investigating flavoproteins naturally found in E. coli, where early experiments have identified a promising magnetofluorescence signal associated with thioredoxin reductase (trxB). At the same time, we're working to distinguish these responses from background fluorescence and better understand how illumination conditions influence what we measure.
Alongside these findings, we've experimentally supported some predictions from our kinetic model, which helps us understand how magnetofluorescence changes under different illumination conditions.
The next steps are to repeat and expand our screening, characterize the proteins showing promising responses, and investigate what they have in common.
Ultimately, we want to move beyond identifying magnetosensitive proteins toward understanding, and potentially predicting, the molecular features responsible for their responses.
