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• W2093013368 startingPage "234" @default.
• W2093013368 abstract "Understanding the relationship between the amino acid sequence of a protein and its unique, compact 3D structure is one of the grand challenges in molecular biophysics. One particularly exciting approach is time-resolved electronic circular dichroism (CD) spectroscopy, which offers resolution on a nanosecond (or faster) time scale, although it does not provide the spatial resolution of techniques like X-ray crystallography or NMR. The thrust of our work is to underpin fast time scale spectroscopic studies of protein folding with a stronger theoretical foundation. Ultimately, we seek to use molecular dynamics simulations to study the influence of conformational dynamics and conformational transitions on the electronic CD spectra of proteins. We discuss how improved quantum chemical models of individual chromophores, including aromatic sidechains, can be incorporated into calculations of the electronic structure of proteins and their CD." @default.
• W2093013368 created "2016-06-24" @default.
• W2093013368 creator A5005611067 @default.
• W2093013368 creator A5051687648 @default.
• W2093013368 date "2004-01-01" @default.
• W2093013368 modified "2023-10-09" @default.
• W2093013368 title "Calculations of protein circular dichroism from first principles" @default.
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• W2093013368 doi "https://doi.org/10.1002/chir.20018" @default.
• W2093013368 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15034906" @default.
• W2093013368 hasPublicationYear "2004" @default.
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