Electronic Circular Dichroism Spectroscopy of Proteins

Rogers, David M.; Jasim, Sarah B.; Dyer, Naomi T.; Auvray, François; Réfrégiers, Matthieu; Hirst, Jonathan D.

Abstract

Circular dichroism (CD) is an important spectroscopic technique that enables the characterization of protein secondary and tertiary structure. Proteins can undergo changes in their structure when they participate in processes, for example, ligand binding. CD, therefore, can be used to monitor secondary and tertiary structural changes when a protein (receptor) binds to a drug molecule (ligand).

This review describes experimental studies of protein CD and theoretical and computational methods that compute spectra from structure or structure from spectra. CD is a technique that can be used to complement X-ray, NMR, and ultraviolet-visible (UV-vis) experiments on biomolecules and proteins, all of which can be assisted by molecular modeling, which has the capability of computing CD from first principles. A combination of experimental CD and molecular modeling has the capacity to greatly enhance future multi-disciplinary research to expand our knowledge of the structure, function, and dynamics of proteins.

Citation

Rogers, D. M., Jasim, S. B., Dyer, N. T., Auvray, F., Réfrégiers, M., & Hirst, J. D. (2019). Electronic Circular Dichroism Spectroscopy of Proteins. Chem, 5(11), 2751-2774. https://doi.org/10.1016/j.chempr.2019.07.008

• Journal Article Type: Article
• Acceptance Date: Jul 15, 2019
• Online Publication Date: Aug 19, 2019
• Publication Date: Nov 14, 2019
• Deposit Date: Aug 23, 2019
• Publicly Available Date: Aug 20, 2020
• Journal: Chem
• Electronic ISSN: 2451-9294
• Publisher: Elsevier
• Peer Reviewed: Peer Reviewed
• Volume: 5
• Issue: 11
• Pages: 2751-2774
• DOI: https://doi.org/10.1016/j.chempr.2019.07.008
• Keywords: Materials chemistry; Biochemistry; General chemistry; General chemical engineering; Biochemistry, medical; Environmental chemistry
• Public URL: https://nottingham-repository.worktribe.com/output/2485250
• Publisher URL: https://www.sciencedirect.com/science/article/abs/pii/S2451929419303171?via%3Dihub