Biophysical Characterization
We offer flexible, cost-effective access to the most requested analytical methods, instruments and techniques. When you need it, a cross-trained Helix expert is ready to go.
Our biophysical characterization services include:
CD (Circular Dichroism)
Instrument
Jasco J-715
Application
Rapid determination of the secondary structure and folding properties of proteins. Analyzes the secondary structure and conformational changes of biomolecules, such as proteins and nucleic acids, in solution.
MP (Mass Photometry)
Instrument
Refeyn / TwoMP
Application
Measures absolute mass of particles in solution and detects the ratio of different species (oligomeric states).
DLS (Dynamic Light Scattering)
Instrument
Malvern / Zetasizer Nano-S
Application
Measures particle size distributions, diffusion coefficients, and molecular weight information.
LC-MS (Mass Spectrometry)
Instrument
Thermo / Orbitrap Fusion Lumos
Application
Identifies and quantifies proteins in both simple and complex formats. Identification and mass measurement of molecules in samples.
SEC-MALS (SEC-Multi-Angle Light Scattering)
Instrument
Wyatt Technology / DAWN HELEOS II / OptiLab rEX
Application
Measures absolute molecular weight, size, and conformation of macromolecules in solution. Analyzes the absolute molar mass and size of macromolecules in solution, providing insights into their structure, aggregation, and interactions.
TSA (Thermal Shift Analysis)
Instrument
Thermo / QuantStudio3
Application
Measures thermal stability of target protein. Measures the stability and melting behavior of biomolecules under varying temperature conditions.
MST (Microscale Thermophoresis)
Instrument
NanoTemper / Monotlith NT.115 Blue/Red
Application
Quantification of biomolecular interaction strength (Kd). An immobilization-free technique for measuring biomolecular interactions.
BLI (Biolayer Interferometry)
Instrument
ForteBio / Octet K2
Application
Measures on/off rate of two molecules. BLI enables real-time analysis of biomolecular binding kinetics and affinity.
SPR (Surface Plasmon Resonance)
Instrument
Cytiva / Biacore T200 & 8K
Application
Measures on/off rate of two molecules. Analyzes biomolecular interactions in real-time, providing insights into binding kinetics, affinity, and specificity.
ITC (Isothermal Titration Calorimetry)
Instrument
TA Instruments / NanoITC
Application
Measures interaction of two molecules, including affinity (KA), enthalpy (ΔH), entropy (ΔS), and stoichiometry (n). A label-free method for measuring binding thermodynamics.
"We have consistently been impressed by Helix's expertise, quality, speed, and thoughtfulness throughout our work together. They have proven to be an ideal partner in our structural biology projects, consistently delivering impressive results and maintaining excellent communication every step of the way."
"Helix Biostructures has been delivering exceptional protein production and characterization services to us in the agricultural biotechnology sector. Our work together is defined by a shared dedication to excellence and an in-depth knowledge of the international regulations and standards necessary for the deregulation of biotechnological crops. Our collaboration makes a substantial contribution to our clients' endeavors in sustainably offering biotechnological solutions for crop protection and increased production."
"Collaborating with Helix to elucidate the structure of our therapeutic antibody in complex with its antigen through Cryo-EM was very valuable for our research. Their expertise in protein sciences and structural biology gave us detailed insights into the antibody-antigen allosteric mechanism, advancing our understanding significantly. The data they provided exceeded our expectations and contributed to the publication of a high-impact paper. The professionalism and technical skill of their team made the entire process smooth and efficient."
"We were highly impressed with Helix BioStructures, who provided a swift collection and analysis of our SAXS samples. Their clear communication and willingness to accommodate specialized handling was invaluable to the success of our experiment."