David M. Rogers
Electronic Circular Dichroism Spectroscopy of Proteins
Rogers, David M.; Jasim, Sarah B.; Dyer, Naomi T.; Auvray, François; Réfrégiers, Matthieu; Hirst, Jonathan D.
Sarah B. Jasim
Naomi T. Dyer
Jonathan D. Hirst
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.
|Journal Article Type||Article|
|Publication Date||Nov 14, 2019|
|Peer Reviewed||Peer Reviewed|
|APA6 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|
|Keywords||Materials chemistry; Biochemistry; General chemistry; General chemical engineering; Biochemistry, medical; Environmental chemistry|
This file is under embargo until Aug 20, 2020 due to copyright restrictions.
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