Get to know the leadership of QRB and QRBD! #Biophysics #OpenAccess #Science

9/9.Life is more than the sum of its parts. But can we ever engineer that “more”?.Synthetic biology is either about to reveal the essence of life… or expose its ultimate mystery. What do YOU think?.Will we build a living cell — or chase shadows forever?.

Join millions who have switched to Grok.

8/9.The field is at a crossroads. Do we pour billions into a “Synthetic Cell Project” (like the Human Genome Project), or let it evolve through smaller labs tinkering in parallel?.Big science vs bottom-up chaos — the debate is heating up.

7/9.Tracking these processes in real time requires molecular beacons, aptamers, and clever microscopy tricks. Yet every probe interferes with the system it measures. How do you study life without disturbing it? Quantum physics déjà vu.

6/9.But here’s the controversy:.Most synthetic biology still uses fluorescent proteins as reporters. They glow beautifully… but they do nothing for cell function. Are we building “real life” or just flashy toys for imaging?.

5/9.Encapsulation is the next frontier. Researchers trap these systems in giant unilamellar vesicles (GUVs) — cell-like bubbles where RNA and proteins can be born. This isn’t just mimicry. It’s proto-life in action.

4/9.PURE system, on the other hand, is “biological LEGO.”.Every piece is defined and purified. Great for control. Terrible for efficiency: 100× less protein than lysate!.How can something so engineered be worse than nature’s chaos?.

3/9.Cell lysate feels like “hacking biology with duct tape.”.It couples transcription & translation naturally, but proteases and nucleases lurk inside, ready to sabotage. High yields, but little control.

2/9.Two rival approaches dominate:.Cell lysate: messy but powerful, a black-box soup of bacterial guts. PURE system: minimal, elegant, but frustratingly weak in protein yields. Which one will power synthetic life?.

Synthetic biology’s holy grail: building a living cell from scratch. But before we get there, we must master the two processes that define life: transcription and translation. Can we reconstitute them outside the cell?.Read a recent QRBD paper about it!.

7/7.Zheng Ser argues: XL-MS is not a side dish—it’s the missing puzzle piece of structural biology. Are you using it?.Should we all be doing more?.Join the debate. 🧪 Read: 🧠 Thoughts?👇.#MassSpectrometry #Biophysics #Proteomics.

6/7.Every structure tells a story. But cross-linking mass spec fills in the plot holes. From epitope mapping to drug design, it’s unlocking the structural dark matter of the proteome. Think you know your complex? XL-MS might say otherwise. #StructuralGaps #DrugDiscovery.

5/7.XL-MS works in cells. That’s right—in cellulo structural biology is real. By capturing native cross-links inside tissues and cells, we glimpse true protein architecture and interactions as they exist. Integrative biology finally gets. integrative. #InCellulo.

4/7.“But AI solved structure prediction!”.Not so fast. XL-MS exposes flaws in AlphaFold’s static predictions—especially for multi-protein complexes. It not only validates models but can improve them by providing real-world distance constraints. #AlphaFold #AIbiology.

3/7.You know that static structure you’re looking at?.Yeah—it’s a lie. Proteins are dynamic machines. XL-MS catches them in action across functional states: apo vs bound, ATP vs ADP, open vs closed. It’s a snapshot of conformational choreography. #DynamicProteins.

2/7.Cross-linking Mass Spectrometry (XL-MS) isn’t just a sidekick to #cryoEM or X-ray—it’s a structural technique in its own right. It captures flexible regions others can’t even see, like loops and disordered domains, using residue-residue distance restraints. #XLMS.

1/7.Even the best protein structures leave critical biology in the dark!.We’re missing flexible regions, conformational states, and in-cellulo realities. But one approach is filling in these gaps. literally 🧩.👇.#StructuralBiology #Proteomics #MassSpec

RT @Biophysics_CUP: @biorxiv_biophys @BiophysicalSoc @BiophysicsFL @PiereBiophysics @BlackInBiophys @UCSFBiophysics @UCD_BPH @TheoBiophysic….

@biorxiv_biophys @BiophysicalSoc @BiophysicsFL @PiereBiophysics @BlackInBiophys @UCSFBiophysics @UCD_BPH @TheoBiophysics @bps_students What bold, innovative, leading-edge areas in #biophysics is QRB Discovery promoting? Find out by listening to the brief interview snippet attached and taking a look at the Special Issues being promoted by QRBD's leadership and our Guest Editors:

7/7.Should more structural biology efforts focus on non-canonical roles of virulence factors like LPMOs?.What experiments would you design to test their role in different calcium concentrations or environmental transitions?.👇 Chime in!.#PathogenBiology #LPMO #ProteinStructure.

6/7.This work challenges us to think beyond the “one-environment, one-function” model of virulence factors. 🧠 What if many “pathogenic” proteins are moonlighting survival tools for harsh or shifting conditions?.We need to test more environmental hypotheses in infection models.