Dr. Christine Beuck
Forschung
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
Seit 2014 | Assistenzprofessorin(Habilitandin) bei Prof. Peter Bayer, Institut für Strukturelle und Medizinische Biochemie |
2012 - 2014 | Postdoktorandin und wissenschaftliche Mitarbeiterin, bei Prof. Dr. J. R. Williamson, The Scripps Research Institute, La Jolla, USA |
2005 | Gastwissenschaftlerin bei Prof. Dr. M. Shionoya, Tokyo University, Tokyo, Japan, im Rahmen des GDCh/DFG Japan Austauschprogramms 2005 |
2003 | Gastwissenschaftlerin bei Dr. habil. S. Klimašauskas, Institute of Biotechnology, Vilnius, Lithuania |
Wissenschaftliche Ausbildung
2001 - 2005 | Promotion in Chemie bei Prof. Dr. E. Weinhold, RWTH Aachen |
1996 - 2001 | Chemiestudium (Dipl.) an der Technischen Universität Dortmund, Diplomarbeit bei Prof. Dr. E. Weinhold, Max Planck Institut für Molekulare Physiologie
|
-
Functional Linkers Support Targeting of Multivalent Tweezers to Taspase1In: Chemistry - A European Journal Jg. 30 (2024) Nr. 56, e202401542Online Volltext: dx.doi.org/ (Open Access)
-
High resolution analysis of proteolytic substrate processingIn: The Journal of Biological Chemistry (JBC) Jg. 300 (2024) Nr. 11, 107812Online Volltext: dx.doi.org/ (Open Access)
-
Increased Cytotoxicity of Bimetallic Ultrasmall Silver–Platinum Nanoparticles (2 nm) on Cells and Bacteria in Comparison to Silver Nanoparticles of the Same SizeIn: Materials Jg. 17 (2024) Nr. 15, 3702Online Volltext: dx.doi.org/ (Open Access)
-
Possibilities and limitations of solution-state NMR spectroscopy to analyze the ligand shell of ultrasmall metal nanoparticlesIn: Nanoscale Advances Jg. 6 (2024) Nr. 13, S. 3285 - 3298Online Volltext: dx.doi.org/ (Open Access)
-
Rational correction of pathogenic conformational defects in HTRA1In: Nature Communications Jg. 15 (2024) Nr. 1, 5944Online Volltext: dx.doi.org/ (Open Access)
-
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 Jg. 128 (2024) Nr. 17, S. 4266 - 4281Online Volltext: dx.doi.org/
-
Multivalent Molecular Tweezers Disrupt the Essential NDC80 Interaction with MicrotubulesIn: Journal of the American Chemical Society: JACS Jg. 145 (2023) Nr. 28, S. 15251 - 15264Online Volltext: dx.doi.org/
-
Potentiating Tweezer Affinity to a Protein Interface with Sequence-Defined Macromolecules on NanoparticlesIn: Biomacromolecules Jg. 24 (2023) Nr. 8, S. 3666 - 3679Online Volltext: dx.doi.org/
-
The UBX domain in UBXD1 organizes ubiquitin binding at the C-terminus of the VCP/p97 AAA-ATPaseIn: Nature Communications Jg. 14 (2023) Nr. 1, 3258Online Volltext: dx.doi.org/ Online Volltext (Open Access)
-
Ultrastructure and Surface Composition of Glutathione-Terminated Ultrasmall Silver, Gold, Platinum, and Alloyed Silver-Platinum Nanoparticles (2 nm)In: Inorganic Chemistry Jg. 62 (2023) Nr. 42, S. 17470 - 17485Online Volltext: dx.doi.org/
-
Dual activity inhibition of threonine aspartase 1 by a single bisphosphate ligandIn: RSC Advances Jg. 12 (2022) Nr. 53, S. 34176 - 34184Online Volltext: dx.doi.org/ (Open Access)
-
Recognition of a Flexible Protein Loop in Taspase 1 by Multivalent Supramolecular TweezersIn: Biomacromolecules Jg. 23 (2022) Nr. 11, S. 4504 - 4518Online Volltext: dx.doi.org/
-
Water-Based Synthesis of Ultrasmall Nanoparticles of Platinum Group Metal Oxides (1.8 nm)In: Inorganic Chemistry Jg. 61 (2022) Nr. 12, S. 5133 - 5147Online Volltext: dx.doi.org/
-
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 Jg. 125 (2021) Nr. 21, S. 5645 - 5659Online Volltext: dx.doi.org/
-
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 Jg. 125 (2021) Nr. 1, S. 115 - 127Online Volltext: dx.doi.org/ (Open Access)
-
Peptide-Conjugated Ultrasmall Gold Nanoparticles (2 nm) for Selective Protein TargetingIn: ACS Applied Bio Materials Jg. 4 (2021) Nr. 1, S. 945 - 965Online Volltext: dx.doi.org/ (Open Access)
-
Specific inhibition of the Survivin–CRM1 interaction by peptide-modified molecular tweezersIn: Nature Communications Jg. 12 (2021) Nr. 1, S. 1505Online Volltext: dx.doi.org/ Online Volltext (Open Access)
-
Targeting the Surface of the Protein 14-3-3 by Ultrasmall (1.5 nm) Gold Nanoparticles Carrying the Specific Peptide CRafIn: ChemBioChem Jg. 22 (2021) Nr. 8, S. 1456 - 1463Online Volltext: dx.doi.org/ (Open Access)
-
Functional Disruption of the Cancer-Relevant Interaction between Survivin and Histone H3 with a Guanidiniocarbonyl Pyrrole LigandIn: Angewandte Chemie International Edition Jg. 59 (2020) Nr. 14, S. 5567 - 5571Online Volltext: dx.doi.org/ (Open Access)
-
NMR Spectroscopy of supramolecular chemistry on protein surfacesIn: Beilstein Journal of Organic Chemistry Jg. 16 (2020) S. 2505 - 2522Online Volltext: dx.doi.org/ (Open Access)
-
Click chemistry on the surface of ultrasmall gold nanoparticles (2 nm) for covalent ligand attachment followed by nmr spectroscopyIn: Langmuir Jg. 35 (2019) Nr. 22, S. 7191 - 7204Online Volltext: dx.doi.org/
-
Multivalent Ligands with Tailor-Made Anion Binding Motif as Stabilizers of Protein–Protein InteractionsIn: ChemBioChem Jg. 20 (2019) Nr. 23, S. 2921 - 2926Online Volltext: dx.doi.org/
-
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 Jg. 35 (2019) Nr. 3, S. 767 - 778Online Volltext: dx.doi.org/
-
Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPaseIn: Biomolecules Jg. 9 (2019) Nr. 12, 876Online Volltext: dx.doi.org/ Online Volltext (Open Access)
-
An NMR Method To Pinpoint Supramolecular Ligand Binding to Basic Residues on ProteinsIn: Angewandte Chemie International Edition Jg. 56 (2017) Nr. 46, S. 14758 - 14762Online Volltext: dx.doi.org/
-
Molecular tweezers target a protein-protein interface and thereby modulate complex formationIn: Chemical Communications: ChemComm Jg. 52 (2016) Nr. 98, S. 14141 - 14144Online Volltext: dx.doi.org/ (Open Access)
-
Structural Characterization of the Loop at the Alpha-Subunit C-Terminus of the Mixed Lineage Leukemia Protein Activating Protease Taspase1In: PLoS ONE Jg. 11 (2016) Nr. 3, S. e0151431Online Volltext: dx.doi.org/ Online Volltext (Open Access)
-
The acidic domain is a unique structural feature of the splicing factor SYNCRIPIn: Protein Science Jg. 25 (2016) Nr. 8, S. 1545 - 1550Online Volltext: dx.doi.org/ (Open Access)
-
Reversibly locked thionucleobase pairs in DNA to study base flipping enzymesIn: Beilstein Journal of Organic Chemistry Jg. 10 (2014) S. 2293 - 2306Online Volltext: dx.doi.org/ (Open Access)