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Updated: Mar 14, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Fourier transform infrared spectroscopy on external perturbations inducing secondary structure changes of hemoglobin
Rui Lu1, Wen-Wei Li2, Abraham Katzir3
1Jiangsu Key Laboratory of Chemical Pollution Control and Resources Reuse, School of Environmental and Biological Engineering, Nanjing University of Science and Technology, Nanjing, 210094, China and CAS Key Laboratory of Urban Pollutant Conversion, Department of Chemistry, University of Science and Technology of China, Hefei 230026, P.R. China. hqyu@ustc.edu.cn.
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.
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