Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides

Francesco Segatta; David M. Rogers; Naomi T. Dyer; Ellen E. Guest; Zhuo Li; Hainam Do; Artur Nenov; Marco Garavelli; Jonathan D. Hirst

doi:10.3390/molecules26020396

Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides

Francesco Segatta, David M. Rogers, Naomi T. Dyer, Ellen E. Guest, Zhuo Li, Hainam Do, Artur Nenov, Marco Garavelli, Jonathan D. Hirst

Department of Chemical and Environmental Engineering

Research output: Journal Publication › Article › peer-review

2 Citations (Scopus)

20 Downloads (Pure)

Abstract

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.

Original language	English
Article number	396
Journal	Molecules
Volume	26
Issue number	2
DOIs	https://doi.org/10.3390/molecules26020396
Publication status	Published - Jan 2021

Keywords

Aromatic chromophores
Computational spectroscopy
Electronic structure
Protein

ASJC Scopus subject areas

Analytical Chemistry
Chemistry (miscellaneous)
Molecular Medicine
Pharmaceutical Science
Drug Discovery
Physical and Theoretical Chemistry
Organic Chemistry

Access to Document

10.3390/molecules26020396

29 Near-Ultraviolet Circular Dichroism and Two-Dimensional Spectroscopy of PolypeptidesFinal published version, 1.88 MBLicence: CC BY

Cite this

@article{a2c14ba13c4d40dca88c53cf36848c63,

title = "Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides",

abstract = "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.",

keywords = "Aromatic chromophores, Computational spectroscopy, Electronic structure, Protein",

author = "Francesco Segatta and Rogers, {David M.} and Dyer, {Naomi T.} and Guest, {Ellen E.} and Zhuo Li and Hainam Do and Artur Nenov and Marco Garavelli and Hirst, {Jonathan D.}",

note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2021",

month = jan,

doi = "10.3390/molecules26020396",

language = "English",

volume = "26",

journal = "Molecules",

issn = "1420-3049",

publisher = "MDPI Multidisciplinary Digital Publishing Institute",

number = "2",

}

TY - JOUR

T1 - Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides

AU - Segatta, Francesco

AU - Rogers, David M.

AU - Dyer, Naomi T.

AU - Guest, Ellen E.

AU - Li, Zhuo

AU - Do, Hainam

AU - Nenov, Artur

AU - Garavelli, Marco

AU - Hirst, Jonathan D.

PY - 2021/1

Y1 - 2021/1

N2 - 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.

AB - 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.

KW - Aromatic chromophores

KW - Computational spectroscopy

KW - Electronic structure

KW - Protein

UR - http://www.scopus.com/inward/record.url?scp=85100124893&partnerID=8YFLogxK

U2 - 10.3390/molecules26020396

DO - 10.3390/molecules26020396

M3 - Article

C2 - 33451152

AN - SCOPUS:85100124893

SN - 1420-3049

VL - 26

JO - Molecules

JF - Molecules

IS - 2

M1 - 396

ER -

Near-ultraviolet circular dichroism and two-dimensional spectroscopy of polypeptides

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this