Electronic Circular Dichroism Spectroscopy in Structural Analysis of Biomolecular Systems
In this chapter, the use of electronic circular dichroism (CD) in structural analysis of biological molecular systems is discussed. The quantum chemical theory of the phenomenon is briefly presented, and the applications of the CD spectroscopy in determin
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Electronic Circular Dichroism Spectroscopy in Structural Analysis of Biomolecular Systems Magdalena Pecul and Wojciech Dzwolak
Abstract In this chapter, the use of electronic circular dichroism (CD) in structural analysis of biological molecular systems is discussed. The quantum chemical theory of the phenomenon is briefly presented, and the applications of the CD spectroscopy in determination of spatial structure of proteins and nucleic acids, and of absolute configuration of small molecules of pharmacological significance are summarized. Some attention is also paid to the emerging technique related to CD—circularly polarized luminscence (CPL). (Dated: 1 February 2013)
Keywords Electronic circular dichroism • Circularly polarized luminscence • Protein structure • Nucleic acid structure • Induced chirality
6.1 Introduction Since the majority of building blocks of living matter are chiral, chiroptical methods have a special significance in structural analysis of compounds of biochemical relevance. Electronic circular dichroism (ECD, usually abbreviated in the literature to CD, after circular dichroism) is the most widespread among them, although vibrational chiroptical spectroscopic methods: vibrational circular dichroism and Raman optical activity are being developed very rapidly nowadays. Dependence of the optical rotation on the incident light wavelength was discovered already in 1817 by Biot [1], but this knowledge was not utilized until midXX century, when optical rotatory dispersion (ORD) measurements started to be routinely conducted [2, 3]. Circular dichroism spectroscopy has a similar history: the phenomenon was first observed in 1847 [4] and the connection between ORD and CD was realized by Cotton half a century later [5], but it became a widespread spectroscopic technique only about 1960 [3]. (Early days of ORD and CD have been reviewed recently by Laur [6].) Since the 1960s, CD has not only replaced optical rotatory dispersion (ORD) as the main biophysical tool to probe static conformations of biopolymers in solution, but it has also successfully evolved into an M. Pecul () · W. Dzwolak Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093, Warszawa, Poland e-mail: [email protected] 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_6, © Springer Science+Business Media Dordrecht 2014
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insightful experimental approach in time-resolved studies of protein folding, as well as in the field of protein-ligand interactions. There are plenty of excellent reviews on applications of CD in protein chemistry and biophysics—either as book chapters [7–15] or up-to-date review papers [16–20]. Out of necessity, in this concise work, we will focus on some general aspects of applications of CD in broadly understood bioscience. First, we discuss briefly the quantum chemical theory underlying the spectroscopic phenomenon and the main
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