Serviceeinheit Bioanalytik

Core facility Bioanalytic

The Core Facility Bioanalytics is located in the Biozentrum of the LMU in Martinsried in the laboratory rooms G02.037/G02.039. Our platform specializes in offering a range of techniques for biomolecular interaction analysis and is specifically designed to facilitate academic collaborations.

We provide training on the following instruments and offer assistance in data interpretation: MicroCal PEAQ-ITC for isothermal calorimetry (ITC), NanoTemper Monolith NT.115 (Microscale thermophoresis [MST]), NanoTemper Prometheus NT.48 (nanoDSF), FluoroMax3 (fluorimetry), DynaPro NanoStar Wyatt Technologies (DLS), TwoMP from Refeyn for mass photometry and Varian260 (AAS). After receiving an introduction, users are able to operate these instruments themselves, and there is a fixed fee per hour for their usage. Upon request, we can establish scientific collaborations involving these instruments.

For more advanced techniques such as SPR (Surface Plasmon Resonance), which users are not be able to perform themselves, we offer a full-price service or a scientific collaboration, providing support in technical and scientific matters related to your project. Collaborative projects include consultation, project planning, and data evaluation.

We also offer measurement services to other academic institutions in the Munich area upon request. In such cases, project costs and user fees will be allocated according to a cost plan.

For further information, questions, and support, please contact bioanalytics@bio.lmu.de .

Please take note of our user regulations and protein QC guidelines.

ITC (Isothermal Titration Calorimetry)

Interactions between biomolecules play a crucial role in various cellular processes. These interactions can involve protein-protein, DNA-protein, lipid-protein, or protein-low molecular weight ligand interactions. To understand the functioning of proteins, nucleic acids, lipids, and other molecules in a biological system, it is essential to identify their interaction partners and characterize their interactions. The characterization of biomolecular interactions requires knowledge of affinity, the number of binding sites, and thermodynamic properties. By performing a simple ITC experiment, it is possible to determine parameters such as binding affinity (KD), stoichiometry, enthalpy (ΔH), and entropy (ΔS). Thermodynamic parameters such as ΔH and ΔS provide valuable insights into complex formation and possible conformational changes of a binding partner after the binding event.

The Bioanalytic Core Facility offers the usage of the PEAQ-ITC microcalorimeter from Malvern. For more details about our PEAQ-ITC instrument, please visit the MalvernPanalytical website:https://www.malvernpanalytical.com/en/products/product-range/microcal-range/microcal-itc-range/microcal-peaq-itc

DLS (Dynamic Light Scattering)

Characterizing isolated biomolecules is a fundamental aspect of molecular biology research. Understanding the exact biophysical properties of proteins, for example, is essential to comprehend their functionality. By using DLS (Dynamic Light Scattering), the radii of biomolecules in a calibration-free manner can be determined. This enables clear conclusions to be drawn about the oligomerization state and conformation of macromolecules, including proteins, natural biopolymers, and nanoparticles. Additionally, this knowledge allows us to make inferences about aggregation, stability, and homogeneity of biomolecules, which is crucial for optimizing sample preparation for subsequent studies such as biomolecular interaction analyses or crystallization. The Bioanalytic Core Facility is equipped with a DLS detector (Wyatt DynaPro Nanostar).

MST

Please use the Nanotemper online shop to purchase consumables (https://shop.nanotempertech.com).

Mass Photometry (TwoMP)

Understanding the composition, oligomeric state, and binding behaviour of biomolecules is essential for elucidating their function in biological systems. Mass photometry is a powerful, label-free technique that enables accurate mass measurements of individual molecules in solution, under native conditions and without the need for labelling.

This method allows for quantitative single-molecule analysis of proteins, nucleic acids, and their complexes. It is also well-suited for assessing sample heterogeneity, determining the stoichiometry of molecular assemblies, and studying complex formation and dissociation.

The TwoMP mass photometer from Refeyn enables precise mass determination of single molecules by detecting their light scattering signals. Within minutes, and using only minimal sample volumes and low concentrations, the instrument can measure the mass distribution of biomolecules and quantify the relative abundance of different species.

These features make mass photometry an ideal tool for evaluating sample purity, oligomeric states, and molecular interactions with high sensitivity and minimal sample preparation.