DichroCalc: improvements in computing protein circular dichroism spectroscopy in the near-ultraviolet

Jasim, Sarah B., Li, Zhou, Guest, Ellen E. and Hirst, Jonathan D. (2017) DichroCalc: improvements in computing protein circular dichroism spectroscopy in the near-ultraviolet. Journal of Molecular Biology . ISSN 1089-8638

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A fully quantitative theory connecting protein conformation and optical spectroscopy would facilitate deeper insights into biophysical and simulation studies of protein dynamics and folding. The web-server DichroCalc (http://comp.chem.nottingham.ac.uk/dichrocalc) allows one to compute from first principles the electronic circular dichroism spectrum of a (modelled or experimental) protein structure or ensemble of structures. The regular, repeating, chiral nature of secondary structure elements leads to intense bands in the far-ultraviolet. The near-UV bands are much weaker and have been challenging to compute theoretically. We report some advances in the accuracy of calculations in the near-UV, realised through the consideration of the vibrational structure of the electronic transitions of aromatic side chains. The improvements have been assessed over a set of diverse proteins. We illustrate them using bovine pancreatic trypsin inhibitor and present a new, detailed analysis of the interactions which are most important in determining the near-UV CD spectrum.

Item Type: Article
RIS ID: https://nottingham-repository.worktribe.com/output/900091
Keywords: aromatic; vibronic; ab initio; electronic excited states; quantum
Schools/Departments: University of Nottingham, UK > Faculty of Science > School of Chemistry
Identification Number: https://doi.org/10.1016/j.jmb.2017.12.009
Depositing User: Smith, Ruth
Date Deposited: 18 Dec 2017 14:04
Last Modified: 04 May 2020 19:22
URI: https://eprints.nottingham.ac.uk/id/eprint/48783

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