Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Intrinsic fluorescence in non-aromatic peptide structures is induced by collective vibrations, charge reorganisation and short hydrogen bonds, as shown in a new glutamine-related structure

View ORCID ProfileAmberley D. Stephens, View ORCID ProfileMuhammad Nawaz Qaisrani, View ORCID ProfileMichael T. Ruggiero, View ORCID ProfileSaul T.E. Jones, Emiliano Poli, View ORCID ProfileAndrew D. Bond, Philippa J. Woodhams, Elyse M. Kleist, View ORCID ProfileLuca Grisanti, Ralph Gebauer, View ORCID ProfileJ. Axel Zeitler, View ORCID ProfileDan Credgington, View ORCID ProfileAli Hassanali, View ORCID ProfileGabriele S. Kaminski Schierle
doi: https://doi.org/10.1101/2020.01.22.915306
Amberley D. Stephens
1Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Amberley D. Stephens
Muhammad Nawaz Qaisrani
2The Abdus Salam International Centre for Theoretical Physics, Strada Costiera 11, 34151 Trieste,Italy
3International School for Advanced Studies, Via Bonomea 265, 34136 Trieste, Italy
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Muhammad Nawaz Qaisrani
Michael T. Ruggiero
4Department of Chemistry, University of Vermont, 82 University Place, Burlington, VT, 05405 USA
1Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Michael T. Ruggiero
Saul T.E. Jones
5Cavendish Laboratory, University of Cambridge, JJ Thomson Avenue, Cambridge, CB3 0HE, U.K
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Saul T.E. Jones
Emiliano Poli
2The Abdus Salam International Centre for Theoretical Physics, Strada Costiera 11, 34151 Trieste,Italy
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Andrew D. Bond
6Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Andrew D. Bond
Philippa J. Woodhams
1Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Elyse M. Kleist
7Department of Chemistry, Syracuse University, Syracuse, New York 13244, United States
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Luca Grisanti
8Division of Theoretical Physics, Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Luca Grisanti
Ralph Gebauer
2The Abdus Salam International Centre for Theoretical Physics, Strada Costiera 11, 34151 Trieste,Italy
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
J. Axel Zeitler
1Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for J. Axel Zeitler
Dan Credgington
5Cavendish Laboratory, University of Cambridge, JJ Thomson Avenue, Cambridge, CB3 0HE, U.K
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Dan Credgington
Ali Hassanali
2The Abdus Salam International Centre for Theoretical Physics, Strada Costiera 11, 34151 Trieste,Italy
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Ali Hassanali
  • For correspondence: ahassana@ictp.it gsk20@cam.ac.uk
Gabriele S. Kaminski Schierle
1Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, UK
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Gabriele S. Kaminski Schierle
  • For correspondence: ahassana@ictp.it gsk20@cam.ac.uk
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Preview PDF
Loading

Abstract

Disentangling the origin of the optical activity of non-aromatic proteins is challenging due to their size and thus their high computational requisites. Here we show, in a much smaller model system, that the single amino acid glutamine undergoes a chemical transformation leading to an unreported glutamine-like structure which has a similar broad absorption spectrum reported previously for non-aromatic proteins. We further show computationally that the optical activity of the glutamine-like structure is directly coupled to short-hydrogen bonds, but also displays charge and vibrational fluctuations, the latter of which are also present in less optically active structures such as in L-glutamine. Since experimentally the glutamine-like structure is the brightest structure, we conclude that short-hydrogen bonds are the ones responsible for the large Stokes shift observed in optically active non-aromatic proteins.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
Back to top
PreviousNext
Posted January 23, 2020.
Download PDF
Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Intrinsic fluorescence in non-aromatic peptide structures is induced by collective vibrations, charge reorganisation and short hydrogen bonds, as shown in a new glutamine-related structure
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Intrinsic fluorescence in non-aromatic peptide structures is induced by collective vibrations, charge reorganisation and short hydrogen bonds, as shown in a new glutamine-related structure
Amberley D. Stephens, Muhammad Nawaz Qaisrani, Michael T. Ruggiero, Saul T.E. Jones, Emiliano Poli, Andrew D. Bond, Philippa J. Woodhams, Elyse M. Kleist, Luca Grisanti, Ralph Gebauer, J. Axel Zeitler, Dan Credgington, Ali Hassanali, Gabriele S. Kaminski Schierle
bioRxiv 2020.01.22.915306; doi: https://doi.org/10.1101/2020.01.22.915306
Digg logo Reddit logo Twitter logo Facebook logo Google logo LinkedIn logo Mendeley logo
Citation Tools
Intrinsic fluorescence in non-aromatic peptide structures is induced by collective vibrations, charge reorganisation and short hydrogen bonds, as shown in a new glutamine-related structure
Amberley D. Stephens, Muhammad Nawaz Qaisrani, Michael T. Ruggiero, Saul T.E. Jones, Emiliano Poli, Andrew D. Bond, Philippa J. Woodhams, Elyse M. Kleist, Luca Grisanti, Ralph Gebauer, J. Axel Zeitler, Dan Credgington, Ali Hassanali, Gabriele S. Kaminski Schierle
bioRxiv 2020.01.22.915306; doi: https://doi.org/10.1101/2020.01.22.915306

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Biophysics
Subject Areas
All Articles
  • Animal Behavior and Cognition (3609)
  • Biochemistry (7585)
  • Bioengineering (5533)
  • Bioinformatics (20825)
  • Biophysics (10344)
  • Cancer Biology (7995)
  • Cell Biology (11653)
  • Clinical Trials (138)
  • Developmental Biology (6617)
  • Ecology (10224)
  • Epidemiology (2065)
  • Evolutionary Biology (13639)
  • Genetics (9557)
  • Genomics (12856)
  • Immunology (7930)
  • Microbiology (19568)
  • Molecular Biology (7675)
  • Neuroscience (42182)
  • Paleontology (308)
  • Pathology (1259)
  • Pharmacology and Toxicology (2208)
  • Physiology (3271)
  • Plant Biology (7058)
  • Scientific Communication and Education (1295)
  • Synthetic Biology (1953)
  • Systems Biology (5433)
  • Zoology (1119)