Rappsilber Laboratory – Innovation in protein mass spectrometry

Their structure and interactions define cellular processes and are therefore critical
to our understanding how cells work and how diseases can be cured.

Proteins are the active ingredient of life

Our mission is to develop approaches to study protein structure
and interactions in cells and make them universally accessible.

Learn more

Our mission is to develop approaches to study protein structure
and interactions in cells and make them universally accessible.

Learn more

Our mission is to develop approaches to study protein structure
and interactions in cells and make them universally accessible.

Learn more

Our mission is to develop approaches to study protein structure
and interactions in cells and make them universally accessible.

Learn more

LATEST PUBLICATIONS

In-cell architecture of an actively transcribing-translating expressome

Science, 2020

by Andrea Graziadei, on 31 July 2020, in Crosslinking, Crosslinking (in situ), Publication, Structural Biology (application), Structural Biology (method)

Proteomics Using Protease Alternatives to Trypsin Benefits from Sequential Digestion with Trypsin

Therese Dau, Giulia Bartolomucci, Juri Rappsilber Analytical Chemistry, 2020 https://doi.org/10.1021/acs.analchem.0c00478 Trypsin is the most used enzyme in proteomics. Nevertheless, proteases with complementary cleavage specificity have been applied in special circumstances. In this work, we analyzed the characteristics of five protease alternatives to trypsin for protein identification and sequence coverage when applied to S. pombe whole cell lysates.

by rapplab-admin, on 06 July 2020, in Method development, Publication

Ultraviolet Photodissociation of Tryptic Peptide Backbones at 213 nm

Lars Kolbowski, Adam Belsom, Juri Rappsilber Journal of the American Society for Mass Spectrometry, 2020 https://doi.org/10.1021/jasms.0c00106 We analyzed the backbone fragmentation behavior of tryptic peptides of a four protein mixture and of E. coli lysate subjected to Ultraviolet Photodissociation (UVPD) at 213 nm on a commercially available UVPD-equipped tribrid mass spectrometer. We obtained 15,178 unique

by rapplab-admin, on 30 April 2020, in Method development, MS development, Publication

The structure of human thyroglobulin

Nature, 2020

by Ludwig Sinn, on 05 February 2020, in Collaboration highlights, Crosslinking, Publication, Structural Biology (application)

Co-regulation map of the human proteome enables identification of protein functions

Nature Biotechnology, 2019

by Georg Kustatscher, on 04 November 2019, in Machine learning, Publication, Software

LAB NEWS

Rappsilber laboratoryFollow

Rappsilber laboratory @RappsilberLab·

31 Jul

Our paper in collaboration with the Mahamid lab @embl is out in Science 🥳 We describe the architecture of transcription-translation coupling in a prokaryote entirely from in-cell data. [1/8] https://science.sciencemag.org/content/369/6503/554

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EMBL@embl·

31 Jul

EMBL scientists in the Mahamid group & colleagues @TUBerlin have created a new approach to observe molecular machines at work inside cells.

By combining three methods, they produced the
highest-resolution images ever obtained of Mycoplasma pneumoniae.

https://www.embl.org/news/science/visualising-the-cells-molecular-machinery-in-action/

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Francis O'Reilly @FJ_OReilly·

14 Jul

Fantastic collaboration with Haering, Lowe, @Beck_Laboratory and Aragon labs. @EMBL,
@MRC_LMB. The first of a few upcoming papers where we use high-density photo-crosslinking to aid interpretation of cryo-EM maps. (with @LrSinn)
https://www.nature.com/articles/s41594-020-0457-x

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MRC Laboratory of Molecular Biology @MRC_LMB·

14 Jul

First complete atomic model of condensin: Jan Lowe’s group lays the foundation for an improved understanding of chromosome assembly
https://www2.mrc-lmb.cam.ac.uk/first-complete-atomic-model-of-condensin-lays-foundation-for-understanding-chromosome-compaction/
#LMBresearch

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Rappsilber laboratory @RappsilberLab·

8 Jul

We are happy to share that with you 🥳Studying the impact of sequential digest with trypsin on the use of alternative proteases https://pubs.acs.org/doi/full/10.1021/acs.analchem.0c00478

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Funding

We gratefully acknowledge support by our funders especially the Wellcome Trust for their willingness to fund us when our vision was daring but the prospects of ever reaching our goals still far remote. We are also deeply indebted to Edinburgh for providing a very supportive research environment and many great colleagues for being the way they are. This allowed us to ultimately overcome the key challenges of our approach. We also thank the many gifted students of Biotechnology at the TU Berlin for their curiosity and interest in technology development and the TU Berlin for providing a space to tune and scale our approach.