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Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics
All protein simulations are conducted with varying degrees of simplifications, oftentimes with unknown ramifications on how these simplifications affect the interpretability of the results. In this work we investigated how protein glycosylation and lateral crowding effects modulate an array of prope...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10515755/ https://www.ncbi.nlm.nih.gov/pubmed/37745347 http://dx.doi.org/10.1101/2023.09.10.556910 |
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author | Seitz, Christian Deveci, İlker McCammon, J. Andrew |
author_facet | Seitz, Christian Deveci, İlker McCammon, J. Andrew |
author_sort | Seitz, Christian |
collection | PubMed |
description | All protein simulations are conducted with varying degrees of simplifications, oftentimes with unknown ramifications on how these simplifications affect the interpretability of the results. In this work we investigated how protein glycosylation and lateral crowding effects modulate an array of properties characterizing the stability and dynamics of influenza neuraminidase. We constructed three systems: 1) Glycosylated neuraminidase in a whole virion (i.e. crowded membrane) environment 2) Glycosylated neuraminidase in its own lipid bilayer 3) Unglycosylated neuraminidase in its own lipid bilayer. We saw that glycans tend to stabilize the protein structure and reduce its conformational flexibility while restricting solvent movement. Conversely, a crowded membrane environment encouraged exploration of the free energy landscape and a large scale conformational change while making the protein structure more compact. Understanding these effects informs what factors one must consider while attempting to recapture the desired level of physical accuracy. |
format | Online Article Text |
id | pubmed-10515755 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cold Spring Harbor Laboratory |
record_format | MEDLINE/PubMed |
spelling | pubmed-105157552023-09-23 Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics Seitz, Christian Deveci, İlker McCammon, J. Andrew bioRxiv Article All protein simulations are conducted with varying degrees of simplifications, oftentimes with unknown ramifications on how these simplifications affect the interpretability of the results. In this work we investigated how protein glycosylation and lateral crowding effects modulate an array of properties characterizing the stability and dynamics of influenza neuraminidase. We constructed three systems: 1) Glycosylated neuraminidase in a whole virion (i.e. crowded membrane) environment 2) Glycosylated neuraminidase in its own lipid bilayer 3) Unglycosylated neuraminidase in its own lipid bilayer. We saw that glycans tend to stabilize the protein structure and reduce its conformational flexibility while restricting solvent movement. Conversely, a crowded membrane environment encouraged exploration of the free energy landscape and a large scale conformational change while making the protein structure more compact. Understanding these effects informs what factors one must consider while attempting to recapture the desired level of physical accuracy. Cold Spring Harbor Laboratory 2023-09-19 /pmc/articles/PMC10515755/ /pubmed/37745347 http://dx.doi.org/10.1101/2023.09.10.556910 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Seitz, Christian Deveci, İlker McCammon, J. Andrew Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics |
title | Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics |
title_full | Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics |
title_fullStr | Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics |
title_full_unstemmed | Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics |
title_short | Glycosylation and Crowded Membrane Effects on Influenza Neuraminidase Stability and Dynamics |
title_sort | glycosylation and crowded membrane effects on influenza neuraminidase stability and dynamics |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10515755/ https://www.ncbi.nlm.nih.gov/pubmed/37745347 http://dx.doi.org/10.1101/2023.09.10.556910 |
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