Fourier transform infrared spectroscopy on external perturbations inducing secondary structure changes of hemoglobin. Issue 21 (30th September 2016)

• Record Type: Journal Article
• Authors: Lu, Rui; Li, Wen-Wei; Katzir, Abraham; Raichlin, Yosef; Mizaikoff, Boris; Yu, Han-Qing
• Is Part Of: Analyst. Volume 141:Issue 21(2016)
• Page Start: 6061
• Page End: 6067
• Publication Date: 2016-09-30
• Subjects: Chemistry, Analytic -- Periodicals; 543
• DOI: 10.1039/c6an01477a
• Languages: English
• ISSNs: 0003-2654

Abstract

Abstract : The secondary structure of proteins and their conformation are intimately related to their biological functions. 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.