Dr. Christine Beuck
Research
Nuclear Magnetic Resonance (NMR) spectroscopy
NMR spectroscopy is a versatile tool to study proteins and their molecular interactions. As part of the CRC 1093, I investigate both the interactions of proteins with their natural binding partners and synthetic ligands designed to target protein surfaces. NMR is a powerful method that can directly determine the protein residues involved in interactions with other biomolecules or synthetic ligands. I established the use of side chain specific NMR experiments for lysine and arginine residues to precisely monitor supramolecular ligand binding, which, in contrast to the standard amide 15N-HSQC experiment, allows to rank multiple binding sites within one protein. For larger proteins, fast-acquisition (BEST-TROSY; SOFAST) as well as Methyl-TROSY experiments are employed. Furthermore, NMR is used to determine the structures of proteins or isolated domains and probe their size, oligomerization status and dynamics or reaction kinetics.
Protein Structure Determination
I elucidate the structures of proteins with both solution NMR spectroscopy and X-Ray crystallography.
NMR structures:
- 2MXT: Acidic Domain of the human splicing factor SYNCRIP (24-107), BMRB # 25970.
- Acidic Domain of the human splicing factor SYNCRIP (24-140) (pdb 2NBB, NMR structure), BMRB # 25428.
X-Ray structures:
- 4DNN: Qua1 Homdimerization domain of the human splicing factor Quaking
- 3K6T: Qua1 homdimerization domain of the C. elegans translational regulator GLD1.
- 3KBL: Qua1 domain N169A mutant of the C. elegans translational regulator GLD1
Biochemical Characterization of Protein Complexes
To perform their task within the cell, proteins are interacting with a multitude of other biomolecules like other proteins, nu
Curriculum Vitae
Professional career
Since 2014 | Assistant Professor (Habilitandin) with Prof. Dr. P. Bayer, University of Duisburg-Essen, Germany |
2014 | Staff Scientist with Prof. Dr. J. R. Williamson, The Scripps Research Institute, La Jolla, USA |
2012 - 2014 | Senior Research Associate with Prof. Dr. J. R. Williamson, The Scripps Research Institute, La Jolla, USA |
2005 - 2012 | Research Associate (Postdoc) with Prof. Dr. J. R. Williamson, The Scripps Research Institute, La Jolla, USA |
2005 | Guest scientist with Prof. Dr. M. Shionoya, Tokyo University, Tokyo, Japan, as part of the GDCh/DFG Japan exchange program 2005 |
2003 | Exchange researcher with Dr. habil. S. Klimašauskas, Institute of Biotechnology, Vilnius, Lithuania |
Scientific education and degrees
2001 - 2005 | Ph.D. in Chemistry, with Prof. Dr. E. Weinhold, RWTH Aachen |
1996 - 2001 | Study of Chemistry (Dipl.) at the Technical University of Dortmund, Diploma thesis with Prof. Dr. E. Weinhold, Max Planck Institute for Molecular Physiology |
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Functional Linkers Support Targeting of Multivalent Tweezers to Taspase1In: Chemistry - A European Journal Vol. 30 (2024) Nr. 56, e202401542Online Full Text: dx.doi.org/ (Open Access)
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High resolution analysis of proteolytic substrate processingIn: The Journal of Biological Chemistry (JBC) Vol. 300 (2024) Nr. 11, 107812Online Full Text: dx.doi.org/ (Open Access)
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Increased Cytotoxicity of Bimetallic Ultrasmall Silver–Platinum Nanoparticles (2 nm) on Cells and Bacteria in Comparison to Silver Nanoparticles of the Same SizeIn: Materials Vol. 17 (2024) Nr. 15, 3702Online Full Text: dx.doi.org/ (Open Access)
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Possibilities and limitations of solution-state NMR spectroscopy to analyze the ligand shell of ultrasmall metal nanoparticlesIn: Nanoscale Advances Vol. 6 (2024) Nr. 13, pp. 3285 - 3298Online Full Text: dx.doi.org/ (Open Access)
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Rational correction of pathogenic conformational defects in HTRA1In: Nature Communications Vol. 15 (2024) Nr. 1, 5944Online Full Text: dx.doi.org/ (Open Access)
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The Molecular Footprint of Peptides on the Surface of Ultrasmall Gold Nanoparticles (2 nm) Is Governed by Steric DemandIn: Journal of Physical Chemistry B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical Chemistry Vol. 128 (2024) Nr. 17, pp. 4266 - 4281Online Full Text: dx.doi.org/
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Multivalent Molecular Tweezers Disrupt the Essential NDC80 Interaction with MicrotubulesIn: Journal of the American Chemical Society: JACS Vol. 145 (2023) Nr. 28, pp. 15251 - 15264Online Full Text: dx.doi.org/
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Potentiating Tweezer Affinity to a Protein Interface with Sequence-Defined Macromolecules on NanoparticlesIn: Biomacromolecules Vol. 24 (2023) Nr. 8, pp. 3666 - 3679Online Full Text: dx.doi.org/
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The UBX domain in UBXD1 organizes ubiquitin binding at the C-terminus of the VCP/p97 AAA-ATPaseIn: Nature Communications Vol. 14 (2023) Nr. 1, 3258Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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Ultrastructure and Surface Composition of Glutathione-Terminated Ultrasmall Silver, Gold, Platinum, and Alloyed Silver-Platinum Nanoparticles (2 nm)In: Inorganic Chemistry Vol. 62 (2023) Nr. 42, pp. 17470 - 17485Online Full Text: dx.doi.org/
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Dual activity inhibition of threonine aspartase 1 by a single bisphosphate ligandIn: RSC Advances Vol. 12 (2022) Nr. 53, pp. 34176 - 34184Online Full Text: dx.doi.org/ (Open Access)
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Recognition of a Flexible Protein Loop in Taspase 1 by Multivalent Supramolecular TweezersIn: Biomacromolecules Vol. 23 (2022) Nr. 11, pp. 4504 - 4518Online Full Text: dx.doi.org/
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Water-Based Synthesis of Ultrasmall Nanoparticles of Platinum Group Metal Oxides (1.8 nm)In: Inorganic Chemistry Vol. 61 (2022) Nr. 12, pp. 5133 - 5147Online Full Text: dx.doi.org/
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Metal-Ligand Interface and Internal Structure of Ultrasmall Silver Nanoparticles (2 nm)In: Journal of Physical Chemistry B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical Chemistry Vol. 125 (2021) Nr. 21, pp. 5645 - 5659Online Full Text: dx.doi.org/
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New tools to probe the protein surface : Ultrasmall gold nanoparticles carry amino acid bindersIn: Journal of Physical Chemistry B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical Chemistry Vol. 125 (2021) Nr. 1, pp. 115 - 127Online Full Text: dx.doi.org/ (Open Access)
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Peptide-Conjugated Ultrasmall Gold Nanoparticles (2 nm) for Selective Protein TargetingIn: ACS Applied Bio Materials Vol. 4 (2021) Nr. 1, pp. 945 - 965Online Full Text: dx.doi.org/ (Open Access)
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Specific inhibition of the Survivin–CRM1 interaction by peptide-modified molecular tweezersIn: Nature Communications Vol. 12 (2021) Nr. 1, pp. 1505Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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Targeting the Surface of the Protein 14-3-3 by Ultrasmall (1.5 nm) Gold Nanoparticles Carrying the Specific Peptide CRafIn: ChemBioChem Vol. 22 (2021) Nr. 8, pp. 1456 - 1463Online Full Text: dx.doi.org/ (Open Access)
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Functional Disruption of the Cancer-Relevant Interaction between Survivin and Histone H3 with a Guanidiniocarbonyl Pyrrole LigandIn: Angewandte Chemie International Edition Vol. 59 (2020) Nr. 14, pp. 5567 - 5571Online Full Text: dx.doi.org/ (Open Access)
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NMR Spectroscopy of supramolecular chemistry on protein surfacesIn: Beilstein Journal of Organic Chemistry Vol. 16 (2020) pp. 2505 - 2522Online Full Text: dx.doi.org/ (Open Access)
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Click chemistry on the surface of ultrasmall gold nanoparticles (2 nm) for covalent ligand attachment followed by nmr spectroscopyIn: Langmuir Vol. 35 (2019) Nr. 22, pp. 7191 - 7204Online Full Text: dx.doi.org/
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Multivalent Ligands with Tailor-Made Anion Binding Motif as Stabilizers of Protein–Protein InteractionsIn: ChemBioChem Vol. 20 (2019) Nr. 23, pp. 2921 - 2926Online Full Text: dx.doi.org/
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Solution NMR Spectroscopy with Isotope-Labeled Cysteine (¹³C and ¹⁵N) Reveals the Surface Structure of l -Cysteine-Coated Ultrasmall Gold Nanoparticles (1.8 nm)In: Langmuir Vol. 35 (2019) Nr. 3, pp. 767 - 778Online Full Text: dx.doi.org/
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Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPaseIn: Biomolecules Vol. 9 (2019) Nr. 12, 876Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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An NMR Method To Pinpoint Supramolecular Ligand Binding to Basic Residues on ProteinsIn: Angewandte Chemie International Edition Vol. 56 (2017) Nr. 46, pp. 14758 - 14762Online Full Text: dx.doi.org/
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Molecular tweezers target a protein-protein interface and thereby modulate complex formationIn: Chemical Communications: ChemComm Vol. 52 (2016) Nr. 98, pp. 14141 - 14144Online Full Text: dx.doi.org/ (Open Access)
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Structural Characterization of the Loop at the Alpha-Subunit C-Terminus of the Mixed Lineage Leukemia Protein Activating Protease Taspase1In: PLoS ONE Vol. 11 (2016) Nr. 3, pp. e0151431Online Full Text: dx.doi.org/ Online Full Text (Open Access)
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The acidic domain is a unique structural feature of the splicing factor SYNCRIPIn: Protein Science Vol. 25 (2016) Nr. 8, pp. 1545 - 1550Online Full Text: dx.doi.org/ (Open Access)
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Reversibly locked thionucleobase pairs in DNA to study base flipping enzymesIn: Beilstein Journal of Organic Chemistry Vol. 10 (2014) pp. 2293 - 2306Online Full Text: dx.doi.org/ (Open Access)