Quantitative first principles calculations of protein circular dichroism in the near-ultraviolet
Author:
Affiliation:
1. School of Chemistry
2. University of Nottingham
3. University Park
4. Nottingham NG7 2RD
5. UK
Abstract
Including the vibrational structure of the electronic transitions of aromatic groups allows quantitative calculation of protein near-UV circular dichroism.
Funder
University Of Nottingham
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2017/SC/C7SC00586E
Reference98 articles.
1. How to study proteins by circular dichroism
2. Aromatic-Aromatic Interaction: A Mechanism of Protein Structure Stabilization
3. Aromatic–Aromatic Interactions Enable α-Helix to β-Sheet Transition of Peptides to Form Supramolecular Hydrogels
4. Molten Globule and Protein Folding
5. Assignment of the Contribution of the Tryptophan Residues to the Circular Dichroism Spectrum of Human Carbonic Anhydrase II
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