Conclusion
The distinct functionality of lipoproteins gives rise to differences in structure that are reflected in the infrared spectra. 2D-IR is a data treatment based in the changes induced by an external perturbation, temperature in our study, which increases the sensibility of the infrared analysis. Thus, from the results presented above is clear that in VLDL and LDL, opposite to HDL, the amide I spectrum is dominated by the special characteristics of apoB-100 but the presence of other proteins in VLDL induces a different pattern in the synchronous and asynchronous maps producing a distinctive pattern for every lipoprotein. The lipid moiety of the different lipoproteins also produce 2D-IR plots, but with less features when compared with proteins, and without significant changes in HDL. The use of temperature as perturbing agent in protein thermal denaturation can be enhanced with studies in shorter temperature ranges which will increase the sensitivity of the technique during thermal unfolding.
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Coto, X., Iloro, I., Arrondo, J.L.R. (2005). A 2D-Infrared Study of Human Lipoproteins. In: Pifat-Mrzljak, G. (eds) Supramolecular Structure and Function 8. Springer, Boston, MA. https://doi.org/10.1007/0-306-48662-8_8
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