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Microfluidic modulation spectroscopy information


Microfluidic modulation spectroscopy (MMS) is an infrared spectroscopy technique that is used to characterize the secondary structure of proteins. Infrared (IR) spectroscopy is well known for this application.[1] However, the lack of automation, repeatability and dynamic range of detection in conventional platforms such as FTIR, have been major limitations which have been addressed with the development of microfluidic modulation spectroscopy.

  1. ^ W. Wang and C.J. Roberts, Aggregation of Therapeutic Proteins (Wiley, 2010), A. Elliott and E.J. Ambrose, Nature 165, 921–922 (1950), H. Susi and D.M. Byler, Methods Enzymol. 130, 290–311 (1986), W. K. Surewicz and H.H. Mantsch, Biochim. Biophys. Acta 952, 115–130 (1988), A. Dong, P. Huang, and W.S. Caughey, Biochemistry 29 (13) 3303–3308 (1990), S.J. Prestrelski, A.L. Williams Jr., and M.N. Liebman, Proteins Structure Function and Bioinformatics 14 (4) 440– 450 (1992), W. K. Surewicz, H.H. Mantsch, and D. Chapman, Biochemistry 32 (2) 389–394 (1993), J.L.R. Arrondo, et al., Prog. Biophys. Mol. Biol. 59 (1) 23–56 (1993)

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