Author

M. F. Peter

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:protein folding & dynamics· 3 Organism:bacteria (other)· 2 Assay:protein structure· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Assay:fluorescence / live-cell microscopy· 1

Frequent Co-Authors

G. H. Thomas· 4 shared G. Hagelueken· 4 shared N. Schneberger· 3 shared C. Gebhardt· 2 shared J. Glaenzer· 2 shared M. Geyer· 2 shared T. Cordes· 2 shared A. Durand· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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4 shared papersBiochemistry

G. H. Thomas

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Author profile →

5 papers

Recent·Most cited

Conformational coupling of the sialic acid TRAP transporter HiSiaQM with its substrate binding protein HiSiaP

M. F. Peter, J. A. Ruland, Y. Kim, P. Hendricks, J. P. Siebrasse, G. H. Thomas, U. Kubitscheck, G. Hagelueken

The paper demonstrates conformational coupling between the TRAP transporter HiSiaQM and its substrate binding protein HiSiaP using disulfide engineering and single-molecule TIRF microscopy.

bioRxiv · Mar 4, 2023Biochemistry

SAVED by a toxin: Structure and function of the CRISPR Lon protease.

C. Rouillon, N. Schneberger, H. Chi, M. F. Peter, M. Geyer, W. Boenigk, R. Seifert, M. F. White, G. Hagelueken

The paper reports the crystal structure of CRISPR-Lon, a protein that activates by binding cA4 and cleaves CRISPR-T to release a nuclease-like fragment.

bioRxiv · Dec 6, 2021Biochemistry

The structure of HiSiaQM defines the architecture of tripartite ATP-independent periplasmic (TRAP) transporters

M. F. Peter, P. Depping, N. Schneberger, E. Severi, K. Gatterdam, S. Tindall, A. Durand, V. Heinz, P. A. Koenig, M. Geyer, C. Ziegler, G. H. Thomas, G. Hagelueken

This paper presents the first cryo-EM structure of TRAP transporter membrane domains and identifies structural features that enable monomeric elevator architecture.

bioRxiv · Dec 3, 2021Biochemistry

Triggering closure of a sialic acid TRAP transporter substrate binding protein through binding of natural or artificial substrates

M. F. Peter, C. Gebhardt, J. Glaenzer, N. Schneberger, M. de Boer, G. H. Thomas, T. Cordes, G. Hagelueken

This study investigates the conformational changes in the sialic acid TRAP transporter SBP VcSiaP upon substrate binding, showing that substrate induces closure and provides structural insights for inhibitor development.

bioRxiv · Dec 2, 2020Biophysics

Cross-validation of distance measurements in proteins by PELDOR/DEER and single-molecule FRET

M. F. Peter, C. Gebhardt, R. Maechtel, J. Glaenzer, G. H. Thomas, T. Cordes, G. Hageluecken

This study compares PELDOR/DEER and smFRET for measuring distances in proteins, identifying discrepancies caused by cryoprotectants and label-protein interactions.

bioRxiv · Nov 23, 2020Biophysics