MMS is an ideal protein characterization tool for measuring changes to higher order structure (HOS) of biomolecules and can be applied to many fields utilizing therapeutic proteins, such as QA in biologics development.
- 20x faster and 30x more sensitive to changes in structure than CD or FTIR* to help you flag unsuitable candidates earlier and meet or beat your project deadlines
- Novel, fully automated technique for higher-order structural measurements of proteins and biomolecules offering walk-away convenience and simple platform methods, even for researchers without expertise in spectroscopy
- Accurate and reproducible measurements with a broad concentration range from 0.1 mg/mL to >200 mg/mL allowing measurements in native conditions and the formulation buffer of interest
- Real-time buffer subtraction minimizes background noise and interference from formulation excipients, resulting in a significant advantage in data accuracy and utility over CD and FTIR
*Journal of Pharmaceutical Sciences, JAN 2020
By incorporating MMS into your analytical suite of tools, you will increase the efficiency and utility of your characterization process by monitoring stability, structure, similarity, and intermolecular aggregation all from a single automated run. With the benefits of MMS plus our state-of-the-art intuitive analytical engine, delta software, you'll gain the confidence in your data that no other biophysical characterization platform can provide.
Learn more about MMS in our newly published app note on the rapid and accurate detection of the higher-order structure of a protein library using MMS!
What are some benefits of measuring secondary structure compared with the other levels of protein structure?
Secondary structure provides direct access to the protein’s function and stability since the global protein structure and shape are closely related to the relative abundance of secondary structural motifs. Changes in the global properties of the protein are often accompanied by secondary structural change. Compared to tertiary and quaternary protein structures which require high experimental effort, secondary protein structure is comparably easy to access, for example through vibrational spectroscopy. On the other hand, secondary protein structure also serves as an ideal reporter on local structural changes, e.g. through binding events or the onset of protein structural aggregation processes.
Are bioinformatics used to measure change in protein structure?
Bioinformatics are most often linked to the organism genome and protein primary sequence as opposed to the structure. However, these tools can absolutely be useful in combination with protein structure characterization to help complete the story. For example, the figure below shows how it is possible to link up the primary sequence to the three-dimensional structure. Bioinformatics could help identify evolutionarily conserved regions, like active sites or binding pockets of the protein and therefore, regions of most importance for the protein function.
How does protein sequencing differ from measurement of protein higher order structure?
Protein sequencing provides the sequence of amino acids within one protein while measurements of protein higher order structure provide the protein’s 3D arrangement either locally (secondary) or globally (tertiary and quaternary).