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/
Protein Engineering | Allostery | CRISPR | Optogenetics | ML
Account is managed by PhD Students
https://Niopeklab.de/
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 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
June 13, 2025 at 1:29 PM
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 platforms for engineering allosteric protein switches under dynamic selection.
Preprint: doi.org/10.1101/2025...
Reposted by Niopek Lab
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...
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...
www.biorxiv.org
June 13, 2025 at 10:13 AM
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...
www.biorxiv.org/content/10.1...
Excited to announce our optogenetic transcriptional deactivation toolbox is now out in its final form at Nucleic Acids research: academic.oup.com/nar/advance-....
A modular toolbox for the optogenetic deactivation of transcription
Abstract. Light-controlled transcriptional activation is a commonly used optogenetic strategy that allows researchers to regulate gene expression with high
academic.oup.com
December 16, 2024 at 12:54 PM
Excited to announce our optogenetic transcriptional deactivation toolbox is now out in its final form at Nucleic Acids research: academic.oup.com/nar/advance-....
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...
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...
www.biorxiv.org
December 5, 2024 at 9:59 AM
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...
www.biorxiv.org/content/10.1...
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)
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...
www.biorxiv.org
November 26, 2024 at 11:34 AM
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)
www.biorxiv.org/content/10.1...
(1/3)
Now out in Nucleic Acids Research: A deep mutational scanning platform to characterize the fitness landscape of anti-CRISPR proteins: doi.org/10.1093/nar/...
(1/4)
(1/4)
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,
doi.org
November 26, 2024 at 11:30 AM
Now out in Nucleic Acids Research: A deep mutational scanning platform to characterize the fitness landscape of anti-CRISPR proteins: doi.org/10.1093/nar/...
(1/4)
(1/4)
Reposted by Niopek Lab
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-...
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
November 22, 2024 at 6:19 PM
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-...
Many congrats to first authors Tobias and Michael! It was lots of fun to see the story develop.
academic.oup.com/nar/advance-...