Jump to main content
Jump to site search

Issue 21, 2016
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 29 Jun 2016, accepted on 08 Sep 2016 and first published on 08 Sep 2016


Article type: Paper
DOI: 10.1039/C6AN01477A
Analyst, 2016,141, 6061-6067

  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements