Issue 21, 2016

Fourier transform infrared spectroscopy on external perturbations inducing secondary structure changes of hemoglobin

Abstract

The secondary structure of proteins and their conformation are intimately related to their biological functions. In this study, heat-induced changes in the secondary structure and conformation of hemoglobin were investigated via infrared attenuated total reflection (IR-ATR) spectroscopy. The secondary structure changes of hemoglobin were derived from IR-ATR spectra using second derivatives and curve fitting. Thereby, the thermal denaturation temperature ranges and the secondary structure changes with temperature were revealed. More detailed information on the secondary structure and conformation was elucidated via two-dimensional infrared correlation spectroscopy. This study deciphers the detailed conformational behavior of hemoglobin molecular changes along with temperature, and creates a general methodological framework for analyzing the heat-induced behavior of biomacromolecules.

Graphical abstract: Fourier transform infrared spectroscopy on external perturbations inducing secondary structure changes of hemoglobin

Supplementary files

Article information

Article type
Paper
Submitted
29 Jun 2016
Accepted
08 Sep 2016
First published
08 Sep 2016

Analyst, 2016,141, 6061-6067

Fourier transform infrared spectroscopy on external perturbations inducing secondary structure changes of hemoglobin

R. Lu, W. Li, A. Katzir, Y. Raichlin, B. Mizaikoff and H. Yu, Analyst, 2016, 141, 6061 DOI: 10.1039/C6AN01477A

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