Keep up-to-date on the latest developments in MMS, biophysical characterization and RedShiftBio by regularly visiting us here. On this page you will find our comprehensive resources, highlights from new papers and other interesting materials that will help you characterize proteins.
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Enhanced Protein Structural Characterization using MMS (Eugene Ma, RedShiftBio)
Introduction to Microfluidic Modulation Spectroscopy (MMS). This technology shows significant increases in sensitivity, dynamic range, accuracy and utility for determination of protein secondary structure, quantitation, similarity, stability and aggregation.
HOS Study for IgG Samples Spiked with Different Amount of BSA by MMS (Libo Wang, RedShiftBio & Brent Kendrick, Elion Labs)
To evaluate the sensitivity of MMS to detect small differences in secondary structure, absorbance spectra are analyzed for protein samples containing BSA spiked into IgG. Results show that MMS is a powerful technique for the measurement and analysis of protein secondary structure and provides HOS data with high sensitivity and accuracy.
Thermal Denaturation Analysis of Bovine Serum Albumin by Microfluidic Modulation Spectroscopy (Lucy Liu, Pfizer)
MMS, a novel mid-IR technique, was used to monitor the thermal denaturation of Bovine Serum Albumin (BSA). Results show that MMS is a powerful technique for the measurement and analysis of protein secondary structure in samples over the wide concentration range of protein concentrations, up to 100 mg/mL.
Repeatability , Concentration Linearity and High Order Structure Analysis of an IgG1 Sample by Microfluidic Modulation Spectroscopy (MMS) (Libo Wang, RedShiftBio & Lucy Liu, Pfizer)
To evaluate the data quality and performance of MMS, an IgG1 sample was analyzed at different concentrations ranging from 0.1 mg/mL to 12.3 mg/mL. MMS has proved to be a powerful protein characterization technique to provide comparability, similarity, quantitation linearity and HOS measurements of protein samples.
Structural Characterization of the Insulin-Degrading Enzyme by Microfluidic Modulation Spectroscopy (Valerie Ivancic, Clark University & Libo Wang, RedShiftBio)
We used a new bioanalytical technique called Microfluidic Modulation Spectroscopy to directly probe the backbone structure of IDE in the absence and presence of ATP and insulin. Together, our results show that the interaction of ATP with IDE is localized to sidechains but the interaction of insulin with IDE leads to a perturbation in the backbone structure of the enzyme.
Early Events in Amyloid Formation by Lysozyme Detected by Microfluidic Modulation Spectroscopy (Quichen Zheng, Clark University & Libo Wang, RedShiftBio)
We used Microfluidic Modulation Spectroscopy (MMS) to characterize the early events in the self-assembly of human lysozyme. Through MMS, we were able to probe the mid-IR absorption band of the protein which is sensitive to both α-helix and β-structure. Results suggest that the first structural transition in the self-assembly of human lysozyme is an α-helix to β-structure conformational rearrangement.
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Whitepapers, Application & Technical Notes
MMS For Protein Therapeutic Drug Analysis - White Paper
This whitepaper provides an overview of RedShiftBio’s Microfluidic Modulation Spectroscopy technology and the performance that can be achieved in protein characterization. Specifically the white paper presents significant increases in sensitivity and concentration range for determining protein similarity (fingerprinting), quantitation, protein secondary structure, and protein stability and aggregation through thermal and chemical denaturation methods
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