Tessera
Folgen

Niopek Lab

@niopeklab.bsky.social

Lab account for AG Niopek at the University of Heidelberg IPMB Protein Engineering | Allostery | CRISPR | Optogenetics | ML Account is managed by PhD Students https://Niopeklab.de/

28 Posts171 Follower22 Folgt
Nicholas Southern@neuroscinikolai.bsky.social · last mo.

New preprint! We used protein domain insertion to tighten the editing window of the TadA8e adenine base editor. Bulky domain insertions concentrated editing around position A5, maintained robust on-target activity, and reduced Cas-independent off-target editing. 🧬 doi.org/10.64898/202...

Domain Insertion Improves the Precision of a CRISPR Adenine Base Editor

Adenine base editors (ABEs) enable efficient A:T to G:C conversion, but their broad activity windows frequently cause unintended bystander edits. We hypothesized that insertion of a bulky, inert prote...

biorxiv.org

Nicholas Southern@neuroscinikolai.bsky.social · 4mo ago

1/28 How do you optimize a dynamic protein property that emerges from multiple states? Our finally published paper in @NatureComms takes on one of the hardest problems in protein engineering with phage assisted evolution: evolving allosteric switches🧵

Jan Mathony@jmathony.bsky.social · 6mo ago

🎉🎉 Our paper on temperature-dependent protein control using AsLOV2 variants is now published at @natchembio.nature.com: www.nature.com/articles/s41... including some new insights from extend variant characterizations.

Modular engineering of thermoresponsive allosteric proteins - Nature Chemical Biology

Thermogenetics enables spatiotemporal control of protein activity using temperature. Now, engineering of a compact, insertable thermoresponsive protein module diversifies the classes of proteins amena...

nature.com

Jan Mathony@jmathony.bsky.social · last yr.

New paper alert! We introduce the modular allosteric thermo-control of protein activity. Employing the AsLOV2 domain and mutants thereof as thermoreceptors, we engineered diverse hybrid proteins, whose activity can be controlled by small temperature changes (37-40/41 °C). doi.org/10.1101/2025...

Niopek Lab@niopeklab.bsky.social · last yr.

Inspired by how nature evolves trigger responsiveness through alternating pressures, we are excited to present POGO-PANCE and RAMPhaGE: Phage-assisted evolution platforms for engineering allosteric protein switches under dynamic selection. Preprint: doi.org/10.1101/2025...

Phage-Assisted Evolution of Allosteric Protein Switches

Allostery, the transmission of locally induced conformational changes to distant functional sites, is a key mechanism for protein regulation. Artificial allosteric effectors enable remote manipulation...

doi.org

Dominik Niopek@dominikniopek.bsky.social · last yr.

Check out the new pre-print from our lab on phage-assisted evolution of light-switchable, allosteric proteins. Congrats to first author @neuroscinikolai.bsky.social, co-corresponding author @jmathony.bsky.social and everyone from the @niopeklab.bsky.social involved! www.biorxiv.org/content/10.1...

Phage-Assisted Evolution of Allosteric Protein Switches

Allostery, the transmission of locally induced conformational changes to distant functional sites, is a key mechanism for protein regulation. Artificial allosteric effectors enable remote manipulation...

biorxiv.org

Niopek Lab@niopeklab.bsky.social · 2y ago

We are thrilled to share ProDomino a model for the prediction of domain insertion sites in proteins. Our approach enables the simple and rapid engineering of highly potent switchable proteins, as we exemplify by creating novel inducible variants of Cas9 and Cas12a. www.biorxiv.org/content/10.1...

Rational engineering of allosteric protein switches by in silico prediction of domain insertion sites

Domain insertion engineering is a powerful approach to juxtapose otherwise separate biological functions, resulting in proteins with new-to-nature activities. A prominent example are switchable protei...

biorxiv.org

Niopek Lab@niopeklab.bsky.social · 2y ago

New pre-print from our group reporting engineered, broad-spectrum anti-CRISPR proteins based on AcrIIA5, a type II inhibitor, and AcrVA1, a type V inhibitor, for opto- and chemogenetic control of CRISPR-Cas9 and -Cas12a: www.biorxiv.org/content/10.1... (1/3)

A Versatile Anti-CRISPR Platform for Opto- and Chemogenetic Control of CRISPR-Cas9 and Cas12 across a Wide Range of Orthologs

CRISPR-Cas technologies have revolutionized life sciences by enabling programmable genome editing across diverse organisms. Achieving dynamic and precise control over CRISPR-Cas activity with exogenou...

biorxiv.org

Jan Mathony@jmathony.bsky.social · 2y ago

Our paper on DMS of anti-CRISPR proteins is out in it's final form Nucleic Acids Research! Many congrats to first authors Tobias and Michael! It was lots of fun to see the story develop. academic.oup.com/nar/advance-...

A deep mutational scanning platform to characterize the fitness landscape of anti-CRISPR proteins

Abstract. Deep mutational scanning is a powerful method for exploring the mutational fitness landscape of proteins. Its adaptation to anti-CRISPR proteins,

academic.oup.com