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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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Detalles Bibliográficos
Autores principales: Segatta, Francesco, Rogers, David M., Dyer, Naomi T., Guest, Ellen E., Li, Zhuo, Do, Hainam, Nenov, Artur, Garavelli, Marco, Hirst, Jonathan D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7828623/
https://www.ncbi.nlm.nih.gov/pubmed/33451152
http://dx.doi.org/10.3390/molecules26020396
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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
collection PubMed
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 pubmed-78286232021-01-25 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. Molecules Article 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. MDPI 2021-01-13 /pmc/articles/PMC7828623/ /pubmed/33451152 http://dx.doi.org/10.3390/molecules26020396 Text en © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
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 Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7828623/
https://www.ncbi.nlm.nih.gov/pubmed/33451152
http://dx.doi.org/10.3390/molecules26020396
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