Fluorine NMR study of proline-rich sequences using fluoroprolines

<p>Proline homopolymer motifs are found in many proteins; their peculiar conformational and dynamic properties are often directly involved in those proteins' functions. However, the dynamics of proline homopolymers is hard to study by NMR due to a lack of amide protons and small chemical...

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Autores principales:	D. Sinnaeve, A. Ben Bouzayene, E. Ottoy, G.-J. Hofman, E. Erdmann, B. Linclau, I. Kuprov, J. C. Martins, V. Torbeev, B. Kieffer
Formato:	article
Lenguaje:	EN
Publicado:	Copernicus Publications 2021
Materias:	Electricity and magnetism QC501-766
Acceso en línea:	https://doaj.org/article/81d114f9dce942748159c12a17a4fc70
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spelling	oai:doaj.org-article:81d114f9dce942748159c12a17a4fc702021-11-09T10:35:10ZFluorine NMR study of proline-rich sequences using fluoroprolines10.5194/mr-2-795-20212699-0016https://doaj.org/article/81d114f9dce942748159c12a17a4fc702021-11-01T00:00:00Zhttps://mr.copernicus.org/articles/2/795/2021/mr-2-795-2021.pdfhttps://doaj.org/toc/2699-0016<p>Proline homopolymer motifs are found in many proteins; their peculiar conformational and dynamic properties are often directly involved in those proteins' functions. However, the dynamics of proline homopolymers is hard to study by NMR due to a lack of amide protons and small chemical shift dispersion. Exploiting the spectroscopic properties of fluorinated prolines opens interesting perspectives to address these issues. Fluorinated prolines are already widely used in protein structure engineering – they introduce conformational and dynamical biases – but their use as <span class="inline-formula"><sup>19</sup></span>F NMR reporters of proline conformation has not yet been explored. In this work, we look at model peptides where C<span class="inline-formula"><i>γ</i></span>-fluorinated prolines with opposite configurations of the chiral C<span class="inline-formula"><i>γ</i></span> centre have been introduced at two positions in distinct polyproline segments. By looking at the effects of swapping these (4<span class="inline-formula"><i>R</i></span>)-fluoroproline and (4<span class="inline-formula"><i>S</i></span>)-fluoroproline within the polyproline segments, we were able to separate the intrinsic conformational properties of the polyproline sequence from the conformational alterations instilled by fluorination. We assess the fluoroproline <span class="inline-formula"><sup>19</sup></span>F relaxation properties, and we exploit the latter in elucidating binding kinetics to the SH3 (Src homology 3) domain.</p>D. SinnaeveD. SinnaeveA. Ben BouzayeneE. OttoyG.-J. HofmanG.-J. HofmanE. ErdmannB. LinclauI. KuprovJ. C. MartinsV. TorbeevB. KiefferCopernicus PublicationsarticleElectricity and magnetismQC501-766ENMagnetic Resonance, Vol 2, Pp 795-813 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Electricity and magnetism QC501-766
spellingShingle	Electricity and magnetism QC501-766 D. Sinnaeve D. Sinnaeve A. Ben Bouzayene E. Ottoy G.-J. Hofman G.-J. Hofman E. Erdmann B. Linclau I. Kuprov J. C. Martins V. Torbeev B. Kieffer Fluorine NMR study of proline-rich sequences using fluoroprolines
description	<p>Proline homopolymer motifs are found in many proteins; their peculiar conformational and dynamic properties are often directly involved in those proteins' functions. However, the dynamics of proline homopolymers is hard to study by NMR due to a lack of amide protons and small chemical shift dispersion. Exploiting the spectroscopic properties of fluorinated prolines opens interesting perspectives to address these issues. Fluorinated prolines are already widely used in protein structure engineering – they introduce conformational and dynamical biases – but their use as <span class="inline-formula"><sup>19</sup></span>F NMR reporters of proline conformation has not yet been explored. In this work, we look at model peptides where C<span class="inline-formula"><i>γ</i></span>-fluorinated prolines with opposite configurations of the chiral C<span class="inline-formula"><i>γ</i></span> centre have been introduced at two positions in distinct polyproline segments. By looking at the effects of swapping these (4<span class="inline-formula"><i>R</i></span>)-fluoroproline and (4<span class="inline-formula"><i>S</i></span>)-fluoroproline within the polyproline segments, we were able to separate the intrinsic conformational properties of the polyproline sequence from the conformational alterations instilled by fluorination. We assess the fluoroproline <span class="inline-formula"><sup>19</sup></span>F relaxation properties, and we exploit the latter in elucidating binding kinetics to the SH3 (Src homology 3) domain.</p>
format	article
author	D. Sinnaeve D. Sinnaeve A. Ben Bouzayene E. Ottoy G.-J. Hofman G.-J. Hofman E. Erdmann B. Linclau I. Kuprov J. C. Martins V. Torbeev B. Kieffer
author_facet	D. Sinnaeve D. Sinnaeve A. Ben Bouzayene E. Ottoy G.-J. Hofman G.-J. Hofman E. Erdmann B. Linclau I. Kuprov J. C. Martins V. Torbeev B. Kieffer
author_sort	D. Sinnaeve
title	Fluorine NMR study of proline-rich sequences using fluoroprolines
title_short	Fluorine NMR study of proline-rich sequences using fluoroprolines
title_full	Fluorine NMR study of proline-rich sequences using fluoroprolines
title_fullStr	Fluorine NMR study of proline-rich sequences using fluoroprolines
title_full_unstemmed	Fluorine NMR study of proline-rich sequences using fluoroprolines
title_sort	fluorine nmr study of proline-rich sequences using fluoroprolines
publisher	Copernicus Publications
publishDate	2021
url	https://doaj.org/article/81d114f9dce942748159c12a17a4fc70
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_version_	1718441123353985024

Fluorine NMR study of proline-rich sequences using fluoroprolines

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