A2 - Resolving structural changes in 4D with PELDOR: CRISPR/Cas13a

Project-related Publications

[P1] T. Hett, T. Zbik, S. Mukherjee, H. Matsuoka, W. Bönigk, D. Klose, C. Rouillon, N. Brenner, S. Peuker, R. Klement, H.-J. Steinhoff, H. Grubmüller, R. Seifert, O. Schiemann*, U.B. Kaupp*
“Spatio-Temporal Resolution of Conformational Changes in Biomolecules by Combining
Pulsed Electron-Electron Double Resonance Spectroscopy with Microsecond Freeze-Hyperquenching”
J. Am. Chem. Soc. 2021, 143, 6981–6989. DOI: 10.1021/jacs.1c01081.

[P2] O. Schiemann*, C.A. Heubach, D. Abdullin, K. Ackermann, M. Azarkh, E.G. Bagryanskaya, M. Drescher, B. Endeward, J.H. Freed, L. Galazzo, D. Goldfarb, T. Hett, L.E. Hofer, L.F. Ibáñez, E.J. Hustedt, S. Kucher, I. Kuprov, J.E. Lovett, A. Meyer, S. Ruthstein, S. Saxena, S. Stoll, C.R. Timmel, M. Di Valentin, H.S. Mchaourab*, T.F. Prisner*, B.E. Bode*, E. Bordignon*, M. Bennati*, G. Jeschke*
“Benchmark test and guidelines for DEER/PELDOR experiments on nitroxide-labeled biomolecules”
J. Am. Chem. Soc. 2021, 143, 17875–17890. DOI: 10.1021/jacs.1c07371.

[P3] D. Nguyen, D. Abdullin, C.A. Heubach, T. Pfaffeneder, A. Nguyen, A. Heine, K. Reuter, F. Diederich, O. Schiemann*, G. Klebe*
“Unraveling a ligand-induced twist of a homodimeric enzyme by pulsed electron–electron double resonance”
Angew. Chem. Int. Ed. 2021, 60, 23419–23426. DOI: 10.1002/anie.202108179.

[P4] C. Wuebben, M.F. Vicino, M. Mueller, O. Schiemann*
“Do the P1 and P2 hairpins of the Guanidine-II Riboswitch interact?”
Nucleic Acids Res. 2020, 48, 10518–10526. DOI: 10.1093/nar/gkaa703.

[P5] N. Fleck, C.A. Heubach, T. Hett, F.R. Haege, P.P. Bawol, H. Baltruschat, O. Schiemann*
“SLIM: A short-linked, highly redox-stable trityl label for high sensitivity in cell EPR distance measurements”
Angew. Chem. Int. Ed. 2020, 59, 9767–9772. DOI: 10.1002/anie.202004452.

[P6] J.J. Jassoy, A. Berndhäuser, F. Duthie, S.P. Kühn, G. Hagelueken, O. Schiemann*
“Versatile Trityl Spin Labels for Nanometer Distance Measurements on Biomolecules in vitro and within cells“
Angew. Chem. Int. Ed. 2017, 56, 177–181. DOI: 10.1002/anie.201609085.

[P7] F. Rico*, A. Russek, L. González, H. Grubmüller*, S. Scheuring*
“Heterogeneous and rate dependent streptavidin-biotin unbinding revealed by high-speed force spectroscopy and molecular dynamics simulations”
Proc. Natl. Acad. Sci. U.S.A. 2019, 116, 6594–6601. DOI: 10.1073/pnas.1816909116.

[P8] J. Huang, S. Rauscher, G. Nawrocki, T. Ran, M. Feig, B.L. de Groot, H. Grubmüller, A.D. MacKerell*
“CHARMM36m: An improved force field for folded and intrinsically disordered proteins”
Nat. Methods 2017, 14, 71–73. DOI: 10.1038/nmeth.4067.

[P9] L.V. Bock, C. Blau, G.F. Schröder*, I.I. Davydov, N. Fischer, H. Stark, M.V. Rodnina, A.C. Vaiana*, H. Grubmüller*
“Energy barriers and driving forces in tRNA translocation through the ribosome”
Nat. Struct. Mol. Biol. 2013, 20, 1390–1396. DOI: 10.1038/nsmb.2690.

[P10] M. Igaev*, C. Kutzner, L.V. Bock, A.C. Vaiana*, H. Grubmüller*
“Automated cryo-EM structure refinement using correlation-driven molecular dynamics”
Life 2019, 8, e43542. DOI: 10.7554/eLife.43542.