Near-Ultraviolet Circular Dichroism and Two-Dimensional Spectroscopy of Polypeptides

A fully quantitative theory of the relationship between protein conformation and optical spectroscopy would facilitate deeper insights into biophysical and simulation studies of protein dynamics and folding. In contrast to intense bands in the far-ultraviolet, near-UV bands are much weaker and have...

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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2021-01, Vol.26 (2), p.396
Main Authors: Segatta, Francesco, Rogers, David M, Dyer, Naomi T, Guest, Ellen E, Li, Zhuo, Do, Hainam, Nenov, Artur, Garavelli, Marco, Hirst, Jonathan D
Format: Article
Language:English
Subjects:
aromatic chromophores
Band theory
Circular Dichroism
computational spectroscopy
Dichroism
electronic structure
Peptides - chemistry
Phenols
Polypeptides
protein
Protein Conformation
Protein folding
Protein structure
Proteins
Spectrophotometry, Ultraviolet
Spectroscopy
Spectrum analysis
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Summary:A fully quantitative theory of the relationship between protein conformation and optical spectroscopy would facilitate deeper insights into biophysical and simulation studies of protein dynamics and folding. In contrast to intense bands in the far-ultraviolet, 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, which were realised through the consideration of the vibrational structure of the electronic transitions of aromatic side chains.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules26020396