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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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
Published: NLM (Medline) 2021
Subjects:
Online Access:https://eprints.nottingham.ac.uk/64723/
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author Segatta, Francesco
Rogers, David M.
Dyer, Naomi T.
Guest, Ellen E.
Li, Zhuo
Do, Hainam
Nenov, Artur
Garavelli, Marco
Hirst, Jonathan D.
author_facet Segatta, Francesco
Rogers, David M.
Dyer, Naomi T.
Guest, Ellen E.
Li, Zhuo
Do, Hainam
Nenov, Artur
Garavelli, Marco
Hirst, Jonathan D.
author_sort Segatta, Francesco
building Nottingham Research Data Repository
collection Online Access
description 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.
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spelling nottingham-647232021-03-10T06:28:47Z https://eprints.nottingham.ac.uk/64723/ Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides Segatta, Francesco Rogers, David M. Dyer, Naomi T. Guest, Ellen E. Li, Zhuo Do, Hainam Nenov, Artur Garavelli, Marco Hirst, Jonathan D. 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. NLM (Medline) 2021-01-13 Article PeerReviewed application/pdf en cc_by https://eprints.nottingham.ac.uk/64723/1/Near-Ultraviolet%20Circular%20Dichroism%20and%20Two-Dimensional%20Spectroscopy%20of%20Polypeptides.pdf Segatta, Francesco, Rogers, David M., Dyer, Naomi T., Guest, Ellen E., Li, Zhuo, Do, Hainam, Nenov, Artur, Garavelli, Marco and Hirst, Jonathan D. (2021) Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides. Molecules, 26 (2). p. 396. ISSN 1420-3049 electronic structure; computational spectroscopy; protein; aromatic chromophores http://dx.doi.org/10.3390/molecules26020396 doi:10.3390/molecules26020396 doi:10.3390/molecules26020396
spellingShingle electronic structure; computational spectroscopy; protein; aromatic chromophores
Segatta, Francesco
Rogers, David M.
Dyer, Naomi T.
Guest, Ellen E.
Li, Zhuo
Do, Hainam
Nenov, Artur
Garavelli, Marco
Hirst, Jonathan D.
Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides
title Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides
title_full Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides
title_fullStr Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides
title_full_unstemmed Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides
title_short Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides
title_sort near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides
topic electronic structure; computational spectroscopy; protein; aromatic chromophores
url https://eprints.nottingham.ac.uk/64723/
https://eprints.nottingham.ac.uk/64723/
https://eprints.nottingham.ac.uk/64723/