Abstract

A method is described for the quantitative subtraction of water from the transmission infrared spectra of aqueous solutions of proteins. The 2125-cm⁻¹ association band of water is used as an internal intensity standard, and the scaling factor is determined with the use of a second-order least-squares fit. This method eliminates the user bias encountered with interactive methods and takes into account small baseline variations due to instrument drift. Statistical analysis of the results obtained demonstrates that at 10% w/w protein concentration, the error is of the order of 2% in the region of the amide I and II bands.

The Ultraviolet Absorption Spectra of Protein Solutions1

R. Norman Jones and Hugh J. Creech
J. Opt. Soc. Am. 33(4) 209-218 (1943)

Numerical tool for estimating the dielectric constant, the thickness, and the coverage of immobilized inhomogeneous protein films on gold in aqueous solution

Tiago A. T. Sousa, Leiva C. Oliveira, Franz H. Neff, Hervé M. Laborde, and Antonio M. N. Lima
Appl. Opt. 57(24) 6866-6875 (2018)

Mid-IR refractive index sensor for detecting proteins employing an external cavity quantum cascade laser-based Mach-Zehnder interferometer

Alicja Dabrowska, Andreas Schwaighofer, Stefan Lindner, and Bernhard Lendl
Opt. Express 28(24) 36632-36642 (2020)

Infrared Spectroscopy of Biologic Materials in Aqueous Solutions

E. R. Blout and H. Lenormant
J. Opt. Soc. Am. 43(11) 1093-1095 (1953)

Three-dimensional protein shape rendering in magnetized solution with Lambert—Beer law

HongYan Gu and WeiShan Chang
Appl. Opt. 51(20) 4827-4832 (2012)