Two-Dimensional Mid-Infrared Correlation Spectroscopy in Protein Research
Representative results showing the position and strength of two-dimensional (2D) correlation spectroscopy in protein research are surveyed in this article. Special emphasis is placed on infrared spectroscopy. Different types of external perturbations that
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Two-Dimensional Mid-Infrared Correlation Spectroscopy in Protein Research Bogusława Czarnik-Matusewicz and Young Mee Jung
Abstract Representative results showing the position and strength of two-di mensional (2D) correlation spectroscopy in protein research are surveyed in this article. Special emphasis is placed on infrared spectroscopy. Different types of external perturbations that are particularly useful for exploring properties of proteins are discussed. Most promising developments in 2D correlation spectroscopy are demonstrated through results obtained for protein systems. The aim of this article has been to present 2D correlation spectroscopy as a simple method that significantly improves information about protein structure gained from infrared spectra. Keywords 2D correlation spectroscopy • Infrared spectroscopy • Protein structure • Amide I • Heterospectral correlation
8.1 Introduction Combined with “protein research,” the following three phrases could confuse a reader who is unfamiliar with the subjects and the terminology used: “Two-dimensional infrared (2D IR) spectroscopy”, “Correlation-2D IR spectroscopy” and “Two-dimensional correlation spectroscopy (2DCoS)”. Additionally, the apparent similarities in the graphical presentations of the results from each of these spectroscopies could be very misleading. Generally, all of the phrases relate to methods that have been inspired by the two-dimensional techniques first developed in the field of nuclear magnetic resonance. However, 2D IR spectroscopies and 2D correlation spectroscopies are fundamentally different because they are based on nonlinear and linear interactions of electromagnetic waves with matter, respectively, as was underlined by Noda and Ozaki [1]. According to [2], the method of 2D IR spectroscopy concerns a nonlinear interaction of light and matter in which measurements B. Czarnik-Matusewicz () Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50–383, Wrocław, Poland e-mail: [email protected] Y. M. Jung Department of Chemistry, Kangwon National University, Chuncheon, 200–701 Korea M. Baranska (ed.), Optical Spectroscopy and Computational Methods in Biology and Medicine, Challenges and Advances in Computational Chemistry and Physics 14, DOI 10.1007/978-94-007-7832-0_8, © Springer Science+Business Media Dordrecht 2014
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are performed in two independent time dimensions to derive two-dimensional (2D) spectra in the frequency domain. The extent of the vibrational spectrum over the two frequency axes reports on how the excitation of a vibration with a given frequency influences all the other vibrations within a detection window after a waiting period. Such a spectrum gives insight into the couplings between the different excitations of the system under study and the time evolution of these couplings. Therefore, the 2D IR measurement must be performed within a picosecond or faster, i.e., on a time scale that is fast compared to most protein dynamics. If the waiting time i
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